PDGFB

UniProt ID: P01127
Organism: Homo sapiens
Review Status: DRAFT
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Gene Description

PDGFB encodes the platelet-derived growth factor B chain, a secreted, disulfide-linked PDGF ligand subunit. Mature PDGF-B-containing dimers, especially PDGF-BB and PDGF-AB, bind and activate PDGF receptor dimers at the cell surface and drive paracrine growth-factor signaling. The core GO picture is receptor ligand/growth factor activity, PDGF receptor binding, extracellular and extracellular-matrix-associated localization, and PDGF-receptor signaling that promotes mural-cell/pericyte recruitment, vascular development, chemotaxis, migration, and proliferation in supported cell-type contexts. Receptor tyrosine kinase activity, receptor autophosphorylation, PI3K/AKT, ERK/MAPK, ROS/NADPH oxidase, and transcriptional outputs are downstream pathway consequences and should not be treated as core PDGFB molecular functions.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0008284 positive regulation of cell population proliferation
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: positive regulation of cell population proliferation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell population proliferation is a downstream growth-factor outcome. Keep it as supported but non-core; more specific cell-type proliferation terms and the core ligand/receptor-binding function are more informative.
GO:0030335 positive regulation of cell migration
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: positive regulation of cell migration is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell migration is a downstream ligand response. Keep it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis and PDGF receptor signaling terms.
GO:0001525 angiogenesis
IBA
GO_REF:0000033
ACCEPT
Summary: angiogenesis is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Angiogenesis is supported through the PDGF-B/PDGFRB endothelial-mural cell axis, especially pericyte recruitment and vessel stabilization.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IBA
GO_REF:0000033
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IBA
GO_REF:0000033
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
GO:0005161 platelet-derived growth factor receptor binding
IBA
GO_REF:0000033
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
file:human/PDGFB/PDGFB-deep-research-falcon.md
**GO MF recommendations (plain-English):** β€œPDGF receptor binding” and β€œgrowth factor activity,” with the binding scope emphasizing **receptor dimer activation via extracellular ligand**, not receptor catalytic activity (fredriksson2004thepdgffamily pages 5-7, ostman1992pdgfaaandpdgfbb pages 1-2).
GO:0005615 extracellular space
IBA
GO_REF:0000033
ACCEPT
Summary: extracellular space is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular space is an appropriate localization for the mature secreted PDGF-B-containing ligand.
GO:0070374 positive regulation of ERK1 and ERK2 cascade
IBA
GO_REF:0000033
MARK AS OVER ANNOTATED
Summary: positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically connected but over-annotated for the PDGFB ligand compared with the PDGF receptor signaling pathway term.
GO:0050918 positive chemotaxis
IEA
GO_REF:0000108
ACCEPT
Summary: positive chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. positive chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
GO:0005576 extracellular region
IEA
GO_REF:0000044
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway
IEA
GO_REF:0000117
MODIFY
Summary: cell surface receptor protein tyrosine kinase signaling pathway captures a related signaling idea, but the term has the wrong scope or aspect for PDGFB.
Reason: The parent receptor tyrosine kinase signaling term is directionally correct but too broad. PDGFB specifically initiates platelet-derived growth factor receptor signaling.
GO:0008083 growth factor activity
IEA
GO_REF:0000120
ACCEPT
Summary: growth factor activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Growth factor activity is a core PDGFB function. The mature ligand acts extracellularly as a mitogen/chemoattractant for mesenchymal and vascular mural cell populations.
GO:0010468 regulation of gene expression
IEA
GO_REF:0000117
MARK AS OVER ANNOTATED
Summary: regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Regulation of gene expression is a broad downstream response to PDGF signaling and should not be treated as a PDGFB core function.
GO:0010557 positive regulation of macromolecule biosynthetic process
IEA
GO_REF:0000117
KEEP AS NON CORE
Summary: positive regulation of macromolecule biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Macromolecule biosynthesis is a broad downstream response to PDGF signaling and is less informative than PDGF receptor signaling or cell-type-specific growth terms.
GO:0014911 positive regulation of smooth muscle cell migration
IEA
GO_REF:0000117
ACCEPT
Summary: positive regulation of smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. smooth muscle cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
GO:0016020 membrane
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: membrane is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Membrane is too broad for PDGFB; any membrane association is a precursor/retention or receptor-bound context, so keep only as non-core.
GO:0048018 receptor ligand activity
IEA
GO_REF:0000117
ACCEPT
Summary: receptor ligand activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Receptor ligand activity is an appropriate parent-level molecular function for PDGFB because the mature PDGF-B-containing dimer activates cell-surface PDGF receptors.
GO:0048661 positive regulation of smooth muscle cell proliferation
IEA
GO_REF:0000117
ACCEPT
Summary: positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
GO:0051239 regulation of multicellular organismal process
IEA
GO_REF:0000117
KEEP AS NON CORE
Summary: regulation of multicellular organismal process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Regulation of multicellular organismal process is too broad for core PDGFB biology; retain only as a non-core propagated summary of developmental effects.
GO:0051781 positive regulation of cell division
IEA
GO_REF:0000043
KEEP AS NON CORE
Summary: positive regulation of cell division is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Positive regulation of cell division is a broad downstream outcome of growth-factor signaling, not a core ligand function.
GO:1902533 positive regulation of intracellular signal transduction
IEA
GO_REF:0000117
MARK AS OVER ANNOTATED
Summary: positive regulation of intracellular signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of intracellular signal transduction is too broad and downstream for the extracellular PDGFB ligand.
GO:0005515 protein binding
IPI
PMID:10806482
PDGF-C is a new protease-activated ligand for the PDGF alpha...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:10806482
PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor.
GO:0005515 protein binding
IPI
PMID:11297552
Platelet-derived growth factor C (PDGF-C), a novel growth fa...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:11297552
2001 Apr 10. Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor.
GO:0005515 protein binding
IPI
PMID:17981115
Anti-PlGF inhibits growth of VEGF(R)-inhibitor-resistant tum...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:17981115
Anti-PlGF inhibits growth of VEGF(R)-inhibitor-resistant tumors without affecting healthy vessels.
GO:0005515 protein binding
IPI
PMID:20534510
Structures of a platelet-derived growth factor/propeptide co...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:20534510
Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex.
GO:0005515 protein binding
IPI
PMID:32296183
A reference map of the human binary protein interactome.
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:32296183
Apr 8. A reference map of the human binary protein interactome.
GO:0005515 protein binding
IPI
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, a...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor.
GO:0042802 identical protein binding
IPI
PMID:1396586
Crystal structure of human platelet-derived growth factor BB...
ACCEPT
Summary: identical protein binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGFB forms the disulfide-linked PDGF-BB homodimer; identical protein binding captures that ligand-dimer assembly when supported by PDGF-BB structural or receptor-binding evidence.
Supporting Evidence:
PMID:1396586
Crystal structure of human platelet-derived growth factor BB.
GO:0042802 identical protein binding
IPI
PMID:23139410
Unique motifs and hydrophobic interactions shape the binding...
REMOVE
Summary: PMID:23139410 is a modified DNA aptamer/SOMAmer structure with PDGF-BB as the target, not direct evidence for PDGFB-PDGFB identical protein binding.
Reason: Remove this specific GOA evidence row because the publication supports DNA aptamer binding to PDGF-BB rather than PDGFB self-association. The same GO term remains supported by PMID:1396586 and PMID:7679113.
Supporting Evidence:
PMID:23139410
Here we report a unique crystal structure of a SOMAmer bound to its target, platelet-derived growth factor B (PDGF-BB).
GO:0042802 identical protein binding
IPI
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, a...
ACCEPT
Summary: identical protein binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGFB forms the disulfide-linked PDGF-BB homodimer; identical protein binding captures that ligand-dimer assembly when supported by PDGF-BB structural or receptor-binding evidence.
Supporting Evidence:
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor.
GO:0036120 cellular response to platelet-derived growth factor stimulus
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
MARK AS OVER ANNOTATED
Summary: cellular response to platelet-derived growth factor stimulus is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Cellular response to platelet-derived growth factor stimulus describes responding cells; PDGFB is the ligand stimulus, so this is over-annotated for the gene product.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0043410 positive regulation of MAPK cascade
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
MARK AS OVER ANNOTATED
Summary: positive regulation of MAPK cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: MAPK cascade activation is downstream of receptor signaling and is less appropriate for PDGFB than PDGF receptor signaling pathway.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0014805 smooth muscle adaptation
NAS
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and i...
KEEP AS NON CORE
Summary: smooth muscle adaptation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Smooth muscle adaptation is a vascular smooth muscle phenotype downstream of PDGF signaling and should remain non-core.
Supporting Evidence:
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cells.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and i...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cells.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and i...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:16477012
Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cells.
GO:0048008 platelet-derived growth factor receptor signaling pathway
NAS
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, a...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:7679113
Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor.
GO:0035556 intracellular signal transduction
IMP
PMID:24008408
CAP37 activation of PKC promotes human corneal epithelial ce...
MARK AS OVER ANNOTATED
Summary: intracellular signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Intracellular signal transduction is a downstream cellular response and not an activity or localization of the secreted PDGFB ligand.
Supporting Evidence:
PMID:24008408
CAP37 activation of PKC promotes human corneal epithelial cell chemotaxis.
GO:0008284 positive regulation of cell population proliferation
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
KEEP AS NON CORE
Summary: positive regulation of cell population proliferation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell population proliferation is a downstream growth-factor outcome. Keep it as supported but non-core; more specific cell-type proliferation terms and the core ligand/receptor-binding function are more informative.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:0010467 gene expression
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
MARK AS OVER ANNOTATED
Summary: gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Gene expression is a downstream cellular response and is over-annotated for the PDGFB ligand.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:0010629 negative regulation of gene expression
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
MARK AS OVER ANNOTATED
Summary: negative regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Negative regulation of gene expression is a downstream transcriptional response to PDGF signaling, not a core ligand function.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:1904707 positive regulation of vascular associated smooth muscle cell proliferation
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:1905064 negative regulation of vascular associated smooth muscle cell differentiation
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
KEEP AS NON CORE
Summary: negative regulation of vascular associated smooth muscle cell differentiation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Negative regulation of vascular smooth muscle differentiation is a supported VSMC phenotype of PDGF-BB treatment but is secondary to the core ligand/receptor signaling function.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:1905176 positive regulation of vascular associated smooth muscle cell dedifferentiation
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
KEEP AS NON CORE
Summary: positive regulation of vascular associated smooth muscle cell dedifferentiation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Positive regulation of vascular smooth muscle dedifferentiation is a supported VSMC phenotype but is secondary to core PDGFB ligand activity.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:0005161 platelet-derived growth factor receptor binding
EXP
PMID:20534510
Structures of a platelet-derived growth factor/propeptide co...
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
PMID:20534510
Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex.
GO:0010628 positive regulation of gene expression
ISS
GO_REF:0000024
MARK AS OVER ANNOTATED
Summary: positive regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of gene expression is a downstream transcriptional response to PDGF signaling, not a core ligand function.
GO:0036120 cellular response to platelet-derived growth factor stimulus
ISS
GO_REF:0000024
MARK AS OVER ANNOTATED
Summary: cellular response to platelet-derived growth factor stimulus is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Cellular response to platelet-derived growth factor stimulus describes responding cells; PDGFB is the ligand stimulus, so this is over-annotated for the gene product.
GO:0048661 positive regulation of smooth muscle cell proliferation
ISS
GO_REF:0000024
ACCEPT
Summary: positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
GO:0010629 negative regulation of gene expression
IDA
PMID:23554459
MicroRNA-638 is highly expressed in human vascular smooth mu...
MARK AS OVER ANNOTATED
Summary: negative regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Negative regulation of gene expression is a downstream transcriptional response to PDGF signaling, not a core ligand function.
Supporting Evidence:
PMID:23554459
Apr 3. MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
GO:1902894 negative regulation of miRNA transcription
IDA
PMID:26493107
miRNA-34a reduces neointima formation through inhibiting smo...
MARK AS OVER ANNOTATED
Summary: negative regulation of miRNA transcription is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Negative regulation of miRNA transcription is a downstream VSMC transcriptional effect and not a core PDGFB function.
Supporting Evidence:
PMID:26493107
Epub 2015 Oct 19. miRNA-34a reduces neointima formation through inhibiting smooth muscle cell proliferation and migration.
GO:1902895 positive regulation of miRNA transcription
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
MARK AS OVER ANNOTATED
Summary: positive regulation of miRNA transcription is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of miRNA transcription is a downstream VSMC transcriptional effect and not a core PDGFB function.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:19126672
Spontaneous phosphoinositide 3-kinase signaling dynamics dri...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:19126672
Jan 6. Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts.
GO:0010811 positive regulation of cell-substrate adhesion
IDA
PMID:19126672
Spontaneous phosphoinositide 3-kinase signaling dynamics dri...
KEEP AS NON CORE
Summary: positive regulation of cell-substrate adhesion is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Cell-substrate adhesion is a downstream cellular behavior in PDGF-stimulated cells and is non-core relative to ligand binding and receptor signaling.
Supporting Evidence:
PMID:19126672
Jan 6. Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts.
GO:0010628 positive regulation of gene expression
IDA
PMID:23554459
MicroRNA-638 is highly expressed in human vascular smooth mu...
MARK AS OVER ANNOTATED
Summary: positive regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of gene expression is a downstream transcriptional response to PDGF signaling, not a core ligand function.
Supporting Evidence:
PMID:23554459
Apr 3. MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:23554459
MicroRNA-638 is highly expressed in human vascular smooth mu...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:23554459
Apr 3. MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
GO:1904707 positive regulation of vascular associated smooth muscle cell proliferation
IDA
PMID:23554459
MicroRNA-638 is highly expressed in human vascular smooth mu...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:23554459
Apr 3. MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
GO:1904754 positive regulation of vascular associated smooth muscle cell migration
IDA
PMID:23554459
MicroRNA-638 is highly expressed in human vascular smooth mu...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:23554459
Apr 3. MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
GO:0008284 positive regulation of cell population proliferation
IDA
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarco...
KEEP AS NON CORE
Summary: positive regulation of cell population proliferation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell population proliferation is a downstream growth-factor outcome. Keep it as supported but non-core; more specific cell-type proliferation terms and the core ligand/receptor-binding function are more informative.
Supporting Evidence:
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication.
GO:0031012 extracellular matrix
HDA
PMID:23979707
SILAC-based proteomics of human primary endothelial cell mor...
ACCEPT
Summary: extracellular matrix is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular matrix association is supported by the PDGF-B C-terminal retention motif and heparan-sulfate/extracellular-matrix retention evidence.
Supporting Evidence:
PMID:23979707
Epub 2013 Aug 26. SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers.
GO:1904707 positive regulation of vascular associated smooth muscle cell proliferation
IDA
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a plate...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
GO:1904754 positive regulation of vascular associated smooth muscle cell migration
IDA
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a plate...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
GO:0048661 positive regulation of smooth muscle cell proliferation
IDA
PMID:21321938
Interleukin-18/WNT1-inducible signaling pathway protein-1 si...
ACCEPT
Summary: positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. smooth muscle cell proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:21321938
Interleukin-18/WNT1-inducible signaling pathway protein-1 signaling mediates human saphenous vein smooth muscle cell proliferation.
GO:0035655 interleukin-18-mediated signaling pathway
IDA
PMID:21321938
Interleukin-18/WNT1-inducible signaling pathway protein-1 si...
MARK AS OVER ANNOTATED
Summary: interleukin-18-mediated signaling pathway is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Interleukin-18-mediated signaling is a context-specific downstream inflammatory pathway and not a direct PDGFB ligand function.
Supporting Evidence:
PMID:21321938
Interleukin-18/WNT1-inducible signaling pathway protein-1 signaling mediates human saphenous vein smooth muscle cell proliferation.
GO:0010629 negative regulation of gene expression
IDA
PMID:25089138
miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Di...
MARK AS OVER ANNOTATED
Summary: negative regulation of gene expression is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Negative regulation of gene expression is a downstream transcriptional response to PDGF signaling, not a core ligand function.
Supporting Evidence:
PMID:25089138
2014 Jul 25. miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Differentiation by Downregulating Syndecan4.
GO:0045892 negative regulation of DNA-templated transcription
IDA
PMID:25089138
miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Di...
MARK AS OVER ANNOTATED
Summary: negative regulation of DNA-templated transcription is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Negative regulation of DNA-templated transcription is a downstream transcriptional response and is over-annotated for the extracellular ligand.
Supporting Evidence:
PMID:25089138
2014 Jul 25. miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Differentiation by Downregulating Syndecan4.
GO:0005796 Golgi lumen
TAS
Reactome:R-HSA-8865275
KEEP AS NON CORE
Summary: Golgi lumen is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Golgi lumen reflects secretory processing of PDGF-B precursors and should be retained as non-core rather than treated as the mature ligand localization.
GO:0005796 Golgi lumen
TAS
Reactome:R-HSA-8865276
KEEP AS NON CORE
Summary: Golgi lumen is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Golgi lumen reflects secretory processing of PDGF-B precursors and should be retained as non-core rather than treated as the mature ligand localization.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-1524182
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-1524186
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186765
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186773
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186778
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186780
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186786
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186798
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186800
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186819
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186826
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-186834
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-2316434
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-2396337
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-2400009
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-380780
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-380782
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-382052
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-382054
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-382055
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-382056
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-382058
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-389083
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-389086
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-481007
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-5672965
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-8864036
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-8865275
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-8865276
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0005576 extracellular region
TAS
Reactome:R-HSA-9674093
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:1904754 positive regulation of vascular associated smooth muscle cell migration
IDA
PMID:19088079
Induction of microRNA-221 by platelet-derived growth factor ...
ACCEPT
Summary: positive regulation of vascular associated smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. vascular smooth muscle cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:19088079
Dec 15. Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
GO:0005161 platelet-derived growth factor receptor binding
IDA
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarco...
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication.
GO:0008083 growth factor activity
IDA
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a plate...
ACCEPT
Summary: growth factor activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Growth factor activity is a core PDGFB function. The mature ligand acts extracellularly as a mitogen/chemoattractant for mesenchymal and vascular mural cell populations.
Supporting Evidence:
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
GO:0009986 cell surface
IDA
PMID:2538439
Collagen-induced binding to human platelets of platelet-deri...
KEEP AS NON CORE
Summary: cell surface is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Cell surface association is compatible with PDGF receptor binding and heparan-sulfate retention, but extracellular region/matrix are more precise mature ligand locations.
Supporting Evidence:
PMID:2538439
Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation.
GO:0005788 endoplasmic reticulum lumen
TAS
Reactome:R-HSA-382053
KEEP AS NON CORE
Summary: endoplasmic reticulum lumen is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Endoplasmic reticulum lumen reflects precursor folding/dimerization in the secretory pathway and is non-core for the mature extracellular ligand.
GO:0000139 Golgi membrane
TAS
Reactome:R-HSA-382053
KEEP AS NON CORE
Summary: Golgi membrane is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Golgi membrane reflects secretory pathway processing/trafficking context and is non-core for the mature extracellular ligand.
GO:0000139 Golgi membrane
TAS
Reactome:R-HSA-8865275
KEEP AS NON CORE
Summary: Golgi membrane is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Golgi membrane reflects secretory pathway processing/trafficking context and is non-core for the mature extracellular ligand.
GO:0000139 Golgi membrane
TAS
Reactome:R-HSA-8865276
KEEP AS NON CORE
Summary: Golgi membrane is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Golgi membrane reflects secretory pathway processing/trafficking context and is non-core for the mature extracellular ligand.
GO:0031093 platelet alpha granule lumen
TAS
Reactome:R-HSA-481007
KEEP AS NON CORE
Summary: platelet alpha granule lumen is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Platelet alpha granule lumen is a supported storage/release localization for platelet PDGF-B, but not the primary mature-ligand site of action.
GO:0030335 positive regulation of cell migration
IDA
PMID:21245381
Neuropilin-1 signaling through p130Cas tyrosine phosphorylat...
KEEP AS NON CORE
Summary: positive regulation of cell migration is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell migration is a downstream ligand response. Keep it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis and PDGF receptor signaling terms.
Supporting Evidence:
PMID:21245381
Jan 18. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
GO:0042056 chemoattractant activity
IDA
PMID:21245381
Neuropilin-1 signaling through p130Cas tyrosine phosphorylat...
ACCEPT
Summary: chemoattractant activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Chemoattractant activity is consistent with PDGF-BB ligand function and the chemotactic responses to PDGF-B-containing ligands.
Supporting Evidence:
PMID:21245381
Jan 18. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
GO:0071363 cellular response to growth factor stimulus
IDA
PMID:21245381
Neuropilin-1 signaling through p130Cas tyrosine phosphorylat...
MARK AS OVER ANNOTATED
Summary: cellular response to growth factor stimulus is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Cellular response to growth factor stimulus describes responding cells and is over-annotated for the extracellular PDGFB ligand.
Supporting Evidence:
PMID:21245381
Jan 18. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
GO:0005515 protein binding
IPI
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
GO:1900127 positive regulation of hyaluronan biosynthetic process
IDA
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degrada...
KEEP AS NON CORE
Summary: positive regulation of hyaluronan biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Hyaluronan biosynthesis is a fibroblast/extracellular-matrix downstream response to PDGF stimulation and is non-core.
Supporting Evidence:
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degradation in human dermal fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB.
GO:0045893 positive regulation of DNA-templated transcription
IDA
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degrada...
MARK AS OVER ANNOTATED
Summary: positive regulation of DNA-templated transcription is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of DNA-templated transcription is a downstream transcriptional response and is over-annotated for the extracellular ligand.
Supporting Evidence:
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degradation in human dermal fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB.
GO:0048146 positive regulation of fibroblast proliferation
IDA
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degrada...
ACCEPT
Summary: positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:17324121
Growth factor regulation of hyaluronan synthesis and degradation in human dermal fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB.
GO:0030097 hemopoiesis
IMP NOT
PMID:11264163
Basis of hematopoietic defects in platelet-derived growth fa...
ACCEPT
Summary: hemopoiesis is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Accept as a NOT annotation. The cited mouse chimera study indicates hematopoietic PDGF-B/PDGFRB expression is not required for normal hematopoiesis, while non-hematopoietic PDGF signaling has inflammatory roles.
Supporting Evidence:
PMID:11264163
Basis of hematopoietic defects in platelet-derived growth factor (PDGF)-B and PDGF beta-receptor null mice.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:21245381
Neuropilin-1 signaling through p130Cas tyrosine phosphorylat...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:21245381
Jan 18. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
GO:0060326 cell chemotaxis
IDA
PMID:21245381
Neuropilin-1 signaling through p130Cas tyrosine phosphorylat...
ACCEPT
Summary: cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:21245381
Jan 18. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
GO:0035793 positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway
IDA
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemot...
ACCEPT
Summary: positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. metanephric mesenchymal cell migration via PDGFRB signaling is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
GO:2000573 positive regulation of DNA biosynthetic process
IDA
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated ...
KEEP AS NON CORE
Summary: positive regulation of DNA biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling, not a direct PDGFB molecular function.
Supporting Evidence:
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
GO:2000573 positive regulation of DNA biosynthetic process
IDA
PMID:10734101
Platelet-derived growth factor receptor beta regulates migra...
KEEP AS NON CORE
Summary: positive regulation of DNA biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling, not a direct PDGFB molecular function.
Supporting Evidence:
PMID:10734101
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
GO:2000573 positive regulation of DNA biosynthetic process
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
KEEP AS NON CORE
Summary: positive regulation of DNA biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling, not a direct PDGFB molecular function.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:2000573 positive regulation of DNA biosynthetic process
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
KEEP AS NON CORE
Summary: positive regulation of DNA biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling, not a direct PDGFB molecular function.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:2000573 positive regulation of DNA biosynthetic process
IDA
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemot...
KEEP AS NON CORE
Summary: positive regulation of DNA biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling, not a direct PDGFB molecular function.
Supporting Evidence:
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
GO:2000591 positive regulation of metanephric mesenchymal cell migration
IDA
PMID:10734101
Platelet-derived growth factor receptor beta regulates migra...
ACCEPT
Summary: positive regulation of metanephric mesenchymal cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. metanephric mesenchymal cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:10734101
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
GO:0016323 basolateral plasma membrane
ISS
GO_REF:0000024
KEEP AS NON CORE
Summary: basolateral plasma membrane is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Basolateral plasma membrane is a polarized-cell localization context and not the mature ligand core localization.
GO:0045840 positive regulation of mitotic nuclear division
IDA
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated ...
KEEP AS NON CORE
Summary: positive regulation of mitotic nuclear division is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and should not be promoted as a core PDGFB function.
Supporting Evidence:
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
GO:0048146 positive regulation of fibroblast proliferation
IDA
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated ...
ACCEPT
Summary: positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:10644978
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
GO:0060326 cell chemotaxis
IDA
PMID:16014047
Hypoxia regulates PDGF-B interactions between glomerular cap...
ACCEPT
Summary: cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:16014047
Hypoxia regulates PDGF-B interactions between glomerular capillary endothelial and mesangial cells.
GO:0060326 cell chemotaxis
IDA
PMID:17991872
TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced...
ACCEPT
Summary: cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:17991872
TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC.
GO:0070374 positive regulation of ERK1 and ERK2 cascade
IDA
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-ind...
MARK AS OVER ANNOTATED
Summary: positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically connected but over-annotated for the PDGFB ligand compared with the PDGF receptor signaling pathway term.
Supporting Evidence:
PMID:16530387
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
GO:0072126 positive regulation of glomerular mesangial cell proliferation
IDA
PMID:16014047
Hypoxia regulates PDGF-B interactions between glomerular cap...
KEEP AS NON CORE
Summary: positive regulation of glomerular mesangial cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Real but non-core: glomerular mesangial cell proliferation is a tissue-specific process downstream of PDGF-B/PDGFR ligand signaling, not a core molecular function of the secreted ligand. Surfaced by the ASSAY_TO_FUNCTION analysis (indirect signaling-ligand effect on a proliferation readout).
Supporting Evidence:
PMID:16014047
Hypoxia regulates PDGF-B interactions between glomerular capillary endothelial and mesangial cells.
GO:0018108 peptidyl-tyrosine phosphorylation
IDA
PMID:10734101
Platelet-derived growth factor receptor beta regulates migra...
MODIFY
Summary: peptidyl-tyrosine phosphorylation captures a related signaling idea, but the term has the wrong scope or aspect for PDGFB.
Reason: The evidence describes PDGF receptor autophosphorylation after ligand binding. PDGFB is not the tyrosine kinase; replace the phosphorylation term with PDGF receptor signaling pathway.
Supporting Evidence:
PMID:10734101
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
GO:0030335 positive regulation of cell migration
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
KEEP AS NON CORE
Summary: positive regulation of cell migration is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell migration is a downstream ligand response. Keep it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis and PDGF receptor signaling terms.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0043406 positive regulation of MAP kinase activity
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
MARK AS OVER ANNOTATED
Summary: positive regulation of MAP kinase activity is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of MAP kinase activity is a downstream receptor/effectors readout, not a direct PDGFB activity.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0043410 positive regulation of MAPK cascade
IMP
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
MARK AS OVER ANNOTATED
Summary: positive regulation of MAPK cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: MAPK cascade activation is downstream of receptor signaling and is less appropriate for PDGFB than PDGF receptor signaling pathway.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0045840 positive regulation of mitotic nuclear division
IDA
PMID:10734101
Platelet-derived growth factor receptor beta regulates migra...
KEEP AS NON CORE
Summary: positive regulation of mitotic nuclear division is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and should not be promoted as a core PDGFB function.
Supporting Evidence:
PMID:10734101
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:10734101
Platelet-derived growth factor receptor beta regulates migra...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:10734101
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
MARK AS OVER ANNOTATED
Summary: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB molecular function and should not be promoted as core for the ligand.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0070374 positive regulation of ERK1 and ERK2 cascade
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
MARK AS OVER ANNOTATED
Summary: positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically connected but over-annotated for the PDGFB ligand compared with the PDGF receptor signaling pathway term.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0072126 positive regulation of glomerular mesangial cell proliferation
IDA
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat met...
KEEP AS NON CORE
Summary: positive regulation of glomerular mesangial cell proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Real but non-core, consistent with the GO:0072126 annotation from PMID:16014047: a tissue-specific proliferation process downstream of PDGF-B/PDGFR signaling rather than a core molecular function.
Supporting Evidence:
PMID:11788434
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
GO:0006468 protein phosphorylation
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
MODIFY
Summary: protein phosphorylation captures a related signaling idea, but the term has the wrong scope or aspect for PDGFB.
Reason: The evidence describes downstream phosphorylation after PDGFB activates PDGF receptors. PDGFB itself does not catalyze protein phosphorylation, so replace with PDGF receptor signaling pathway.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0016176 superoxide-generating NADPH oxidase activator activity
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
REMOVE
Summary: superoxide-generating NADPH oxidase activator activity is not supported as a PDGFB gene-product function or mature localization.
Reason: Remove. Superoxide-generating NADPH oxidase activator activity belongs to NADPH oxidase regulatory machinery, not to the secreted PDGFB ligand.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0043406 positive regulation of MAP kinase activity
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
MARK AS OVER ANNOTATED
Summary: positive regulation of MAP kinase activity is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Positive regulation of MAP kinase activity is a downstream receptor/effectors readout, not a direct PDGFB activity.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0045840 positive regulation of mitotic nuclear division
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
KEEP AS NON CORE
Summary: positive regulation of mitotic nuclear division is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and should not be promoted as a core PDGFB function.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0050921 positive regulation of chemotaxis
IDA
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemot...
ACCEPT
Summary: positive regulation of chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. positive regulation of chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
GO:0070374 positive regulation of ERK1 and ERK2 cascade
IDA
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
MARK AS OVER ANNOTATED
Summary: positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically connected but over-annotated for the PDGFB ligand compared with the PDGF receptor signaling pathway term.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0072593 reactive oxygen species metabolic process
IMP
PMID:17942966
Mitogenic signaling via platelet-derived growth factor beta ...
MARK AS OVER ANNOTATED
Summary: reactive oxygen species metabolic process is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Reactive oxygen species metabolism is a downstream PDGFR/NADPH oxidase pathway readout and should not be assigned as a PDGFB core process.
Supporting Evidence:
PMID:17942966
2007 Oct 17. Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
GO:0090280 positive regulation of calcium ion import
IDA
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemot...
MARK AS OVER ANNOTATED
Summary: positive regulation of calcium ion import is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Calcium ion import is a downstream PDGFRB signaling response, not a direct PDGFB ligand function.
Supporting Evidence:
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
GO:2000379 positive regulation of reactive oxygen species metabolic process
IDA
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemot...
MARK AS OVER ANNOTATED
Summary: positive regulation of reactive oxygen species metabolic process is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Reactive oxygen species regulation is downstream of receptor signaling and NADPH oxidases and is over-annotated for PDGFB.
Supporting Evidence:
PMID:19019919
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
GO:0001892 embryonic placenta development
ISS
GO_REF:0000024
KEEP AS NON CORE
Summary: embryonic placenta development is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Placenta development is consistent with organismal phenotypes of PDGFB/PDGFRB disruption but is a developmental outcome, not a core molecular function.
GO:0003104 positive regulation of glomerular filtration
ISS
GO_REF:0000024
KEEP AS NON CORE
Summary: positive regulation of glomerular filtration is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Glomerular filtration is an organ-level consequence of PDGFB-dependent glomerular/mesangial development and should be kept as non-core.
GO:0007507 heart development
ISS
GO_REF:0000024
KEEP AS NON CORE
Summary: heart development is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Heart development is a broad developmental outcome of PDGFB pathway function and is non-core for this ligand review.
GO:0038001 paracrine signaling
ISS
GO_REF:0000024
ACCEPT
Summary: paracrine signaling is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Paracrine signaling is appropriate for PDGFB because endothelial and platelet-derived PDGF-B acts as an extracellular signal to neighboring PDGF receptor-expressing cells.
GO:0072255 metanephric glomerular mesangial cell development
ISS
GO_REF:0000024
KEEP AS NON CORE
Summary: metanephric glomerular mesangial cell development is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Metanephric glomerular mesangial cell development is a supported developmental role downstream of PDGFB/PDGFRB signaling, but non-core relative to ligand activity.
GO:0005515 protein binding
IPI
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a plate...
MARK AS OVER ANNOTATED
Summary: protein binding is biologically connected to PDGFB signaling but overstates the direct function of the secreted ligand.
Reason: Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix retention should be used instead.
Supporting Evidence:
PMID:12070119
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
GO:0005737 cytoplasm
ISS
GO_REF:0000024
REMOVE
Summary: cytoplasm is not supported as a PDGFB gene-product function or mature localization.
Reason: Remove. PDGFB is a secretory pathway/extracellular ligand; cytoplasm is not a supported mature localization for this gene product in the reviewed evidence.
GO:0071506 cellular response to mycophenolic acid
ISS
GO_REF:0000024
REMOVE
Summary: cellular response to mycophenolic acid is not supported as a PDGFB gene-product function or mature localization.
Reason: Remove. Cellular response to mycophenolic acid is a drug-response annotation and does not represent PDGFB ligand function.
GO:0002548 monocyte chemotaxis
IDA
PMID:17991872
TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced...
ACCEPT
Summary: monocyte chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. monocyte chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:17991872
TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC.
GO:0005518 collagen binding
IDA
PMID:8900172
Type I, II, III, IV, V, and VI collagens serve as extracellu...
ACCEPT
Summary: collagen binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Collagen binding is a supported, specific extracellular-matrix interaction for PDGF isoforms and is more informative than generic protein binding.
Supporting Evidence:
PMID:8900172
Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB).
GO:0014911 positive regulation of smooth muscle cell migration
IDA
PMID:9409235
Platelet-derived growth factor beta-receptors can both promo...
ACCEPT
Summary: positive regulation of smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. smooth muscle cell migration is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:9409235
Platelet-derived growth factor beta-receptors can both promote and inhibit chemotaxis in human vascular smooth muscle cells.
GO:0050921 positive regulation of chemotaxis
IDA
PMID:9409235
Platelet-derived growth factor beta-receptors can both promo...
ACCEPT
Summary: positive regulation of chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. positive regulation of chemotaxis is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:9409235
Platelet-derived growth factor beta-receptors can both promote and inhibit chemotaxis in human vascular smooth muscle cells.
GO:0005161 platelet-derived growth factor receptor binding
IPI
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence...
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:2536956
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
GO:0005161 platelet-derived growth factor receptor binding
IDA
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B f...
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
GO:0008284 positive regulation of cell population proliferation
IDA
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B f...
KEEP AS NON CORE
Summary: positive regulation of cell population proliferation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell population proliferation is a downstream growth-factor outcome. Keep it as supported but non-core; more specific cell-type proliferation terms and the core ligand/receptor-binding function are more informative.
Supporting Evidence:
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
GO:0008284 positive regulation of cell population proliferation
IDA
PMID:7073684
Platelet-derived growth factor: identification of constituen...
KEEP AS NON CORE
Summary: positive regulation of cell population proliferation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Broad positive regulation of cell population proliferation is a downstream growth-factor outcome. Keep it as supported but non-core; more specific cell-type proliferation terms and the core ligand/receptor-binding function are more informative.
Supporting Evidence:
PMID:7073684
Platelet-derived growth factor: identification of constituent polypeptide chains.
GO:0009611 response to wounding
IDA
PMID:2538439
Collagen-induced binding to human platelets of platelet-deri...
KEEP AS NON CORE
Summary: response to wounding is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Response to wounding is a supported physiological context for platelet-derived PDGF-BB release and signaling, but is non-core relative to the receptor-ligand function.
Supporting Evidence:
PMID:2538439
Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation.
GO:0009986 cell surface
IDA
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B f...
KEEP AS NON CORE
Summary: cell surface is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Cell surface association is compatible with PDGF receptor binding and heparan-sulfate retention, but extracellular region/matrix are more precise mature ligand locations.
Supporting Evidence:
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
GO:0009986 cell surface
IDA
PMID:291037
Platelet-derived growth factor: purification and partial cha...
KEEP AS NON CORE
Summary: cell surface is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Cell surface association is compatible with PDGF receptor binding and heparan-sulfate retention, but extracellular region/matrix are more precise mature ligand locations.
Supporting Evidence:
PMID:291037
Platelet-derived growth factor: purification and partial characterization.
GO:0010512 negative regulation of phosphatidylinositol biosynthetic process
IDA
PMID:2538439
Collagen-induced binding to human platelets of platelet-deri...
KEEP AS NON CORE
Summary: negative regulation of phosphatidylinositol biosynthetic process is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: The platelet phosphoinositide effect is a specific downstream platelet-feedback context, not a core PDGFB function.
Supporting Evidence:
PMID:2538439
Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation.
GO:0010544 negative regulation of platelet activation
IDA
PMID:2538439
Collagen-induced binding to human platelets of platelet-deri...
KEEP AS NON CORE
Summary: negative regulation of platelet activation is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Negative regulation of platelet activation is a specific platelet-feedback context, not the core PDGFB ligand function.
Supporting Evidence:
PMID:2538439
Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation.
GO:0042803 protein homodimerization activity
IDA
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B f...
ACCEPT
Summary: protein homodimerization activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Protein homodimerization activity directly captures PDGF-BB homodimer formation, a core biochemical property of the mature ligand.
Supporting Evidence:
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
GO:0046982 protein heterodimerization activity
IPI
PMID:7073684
Platelet-derived growth factor: identification of constituen...
ACCEPT
Summary: protein heterodimerization activity is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Protein heterodimerization activity captures PDGF-AB formation between PDGFA and PDGFB, a recognized active PDGF ligand dimer.
Supporting Evidence:
PMID:7073684
Platelet-derived growth factor: identification of constituent polypeptide chains.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarco...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication.
GO:0048008 platelet-derived growth factor receptor signaling pathway
IDA
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B f...
ACCEPT
Summary: platelet-derived growth factor receptor signaling pathway is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor signaling pathway is the core biological process initiated by PDGFB ligand binding to PDGFRA/PDGFRB receptor complexes.
Supporting Evidence:
PMID:2836953
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
GO:0048146 positive regulation of fibroblast proliferation
IDA
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarco...
ACCEPT
Summary: positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
Reason: Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
Supporting Evidence:
PMID:2439522
PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication.
GO:0048407 platelet-derived growth factor binding
IPI
PMID:7073684
Platelet-derived growth factor: identification of constituen...
ACCEPT
Summary: platelet-derived growth factor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Platelet-derived growth factor binding is consistent with PDGFB participation in PDGF dimer formation and PDGF ligand complexes, although the more informative core terms are PDGF receptor binding and dimerization.
Supporting Evidence:
PMID:7073684
Platelet-derived growth factor: identification of constituent polypeptide chains.
GO:0001938 positive regulation of endothelial cell proliferation
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
KEEP AS NON CORE
Summary: positive regulation of endothelial cell proliferation is retained as a non-core, context-specific PDGFB annotation pending more specific upstream curation.
Reason: The annotation is connected to PDGFB biology, but the core function is extracellular PDGF receptor ligand activity and PDGF receptor signaling.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0009986 cell surface
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
KEEP AS NON CORE
Summary: cell surface is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Cell surface association is compatible with PDGF receptor binding and heparan-sulfate retention, but extracellular region/matrix are more precise mature ligand locations.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0043536 positive regulation of blood vessel endothelial cell migration
IDA
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-ind...
KEEP AS NON CORE
Summary: positive regulation of blood vessel endothelial cell migration is retained as a non-core, context-specific PDGFB annotation pending more specific upstream curation.
Reason: The annotation is connected to PDGFB biology, but the core function is extracellular PDGF receptor ligand activity and PDGF receptor signaling.
Supporting Evidence:
PMID:9685360
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
GO:0005161 platelet-derived growth factor receptor binding
NAS
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, me...
ACCEPT
Summary: platelet-derived growth factor receptor binding is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands. PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate PDGF receptor signaling.
Supporting Evidence:
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.
GO:0005576 extracellular region
NAS
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, me...
ACCEPT
Summary: extracellular region is supported for PDGFB in the context of its mature extracellular PDGF ligand function.
Reason: Extracellular region is strongly supported for mature PDGFB, which is secreted and acts as an extracellular receptor ligand.
Supporting Evidence:
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.
GO:0009611 response to wounding
NAS
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, me...
KEEP AS NON CORE
Summary: response to wounding is supported or plausible for PDGFB but represents a context-specific localization, storage, processing, or downstream biological outcome.
Reason: Response to wounding is a supported physiological context for platelet-derived PDGF-BB release and signaling, but is non-core relative to the receptor-ligand function.
Supporting Evidence:
PMID:1661670
Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.

Core Functions

PDGFB is the platelet-derived growth factor B-chain ligand subunit. After secretory-pathway processing and disulfide-linked dimer formation, PDGF-B-containing ligands act extracellularly as receptor ligands/growth factors for PDGFRA- and PDGFRB-containing receptor dimers. This function underlies PDGF receptor signaling, paracrine mural-cell/pericyte recruitment, angiogenesis/blood vessel morphogenesis, chemotaxis, and specific smooth muscle/mesenchymal proliferation or migration responses. Receptor autophosphorylation and downstream PI3K, ERK/MAPK, ROS, and transcriptional outputs are consequences in responding cells rather than direct PDGFB molecular functions.

Supporting Evidence:
  • file:human/PDGFB/PDGFB-deep-research-falcon.md
    This report summarizes **GO-relevant evidence for PDGFB as a secreted PDGF ligand**: disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), **direct binding/activation of PDGF receptor dimers (PDGFRA/PDGFRB)**, secretion/localization (extracellular space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only where explicitly stated), and **ligand-attributable biological processes** (pericyte recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing evidence). It **excludes** receptor **intrinsic kinase activity** (peptidyl-tyrosine phosphorylation), downstream pathway terms (PI3K–AKT, ERK/MAPK, ROS/NADPH oxidase), and broad transcriptional/miRNA effects unless strictly necessary to interpret ligand localization or binding (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7).
  • file:human/PDGFB/PDGFB-deep-research-falcon.md
    PDGF‑AA/AB/BB are described as **secreted in active form**, supporting extracellular localization of mature PDGF‑B-containing ligands (duran2018molecularregulationof pages 9-11).

References

Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
Platelet-derived growth factor receptor beta regulates migration and DNA synthesis in metanephric mesenchymal cells.
PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor.
Basis of hematopoietic defects in platelet-derived growth factor (PDGF)-B and PDGF beta-receptor null mice.
Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor.
Effect of platelet-derived growth factor isoforms in rat metanephric mesenchymal cells.
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
Crystal structure of human platelet-derived growth factor BB.
Hypoxia regulates PDGF-B interactions between glomerular capillary endothelial and mesangial cells.
Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cells.
c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells.
Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.
Growth factor regulation of hyaluronan synthesis and degradation in human dermal fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB.
Mitogenic signaling via platelet-derived growth factor beta in metanephric mesenchymal cells.
Anti-PlGF inhibits growth of VEGF(R)-inhibitor-resistant tumors without affecting healthy vessels.
TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC.
PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by PDGF AA.
Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.
Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts.
Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex.
Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.
Interleukin-18/WNT1-inducible signaling pathway protein-1 signaling mediates human saphenous vein smooth muscle cell proliferation.
Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets.
MicroRNA-638 is highly expressed in human vascular smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan nuclear receptor NOR1.
SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers.
CAP37 activation of PKC promotes human corneal epithelial cell chemotaxis.
PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does not stimulate cell replication.
miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Differentiation by Downregulating Syndecan4.
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation.
miRNA-34a reduces neointima formation through inhibiting smooth muscle cell proliferation and migration.
A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
Platelet-derived growth factor: purification and partial characterization.
A reference map of the human binary protein interactome.
Platelet-derived growth factor: identification of constituent polypeptide chains.
Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor.
Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB).
Platelet-derived growth factor beta-receptors can both promote and inhibit chemotaxis in human vascular smooth muscle cells.
Apolipoprotein E inhibits platelet-derived growth factor-induced vascular smooth muscle cell migration and proliferation by suppressing signal transduction and preventing cell entry to G1 phase.
Reactome:R-HSA-1524182
Activated PLC gamma dissociates from the PDGF receptor
Reactome:R-HSA-1524186
Phosphorylation of PLCgamma by PDGFR
Reactome:R-HSA-186765
PLC-gamma binds to the active receptor
Reactome:R-HSA-186773
PDGF dimer binds two receptors simultaneously
Reactome:R-HSA-186778
SHP2 binds to the active receptor
Reactome:R-HSA-186780
PI3-kinase binds to the active receptor
Reactome:R-HSA-186786
Autophosphorylation of PDGF beta receptors
Reactome:R-HSA-186798
GAP binds to PDGF-beta receptors only
Reactome:R-HSA-186800
PI3K catalyses the phosphorylation of PIP2 to PIP3
Reactome:R-HSA-186819
SH2 domain of Src binds to the active receptor
Reactome:R-HSA-186826
GRB2:SOS1 complex binds to the active receptor
Reactome:R-HSA-186834
SOS-mediated nucleotide exchange on RAS (PDGF receptor:GRB2:SOS)
Reactome:R-HSA-2316434
PI3K phosphorylates PIP2 to PIP3
Reactome:R-HSA-2396337
HSPG2 binds FGF2(10-155), Fibronectn matrix, Transthyretin tetramer, PDGFA homodimer, PDGFB homodimer
Reactome:R-HSA-2400009
PI3K inhibitors block PI3K catalytic activity
Reactome:R-HSA-380780
Activation of Src
Reactome:R-HSA-380782
STAT binds to the active receptor
Reactome:R-HSA-382052
p130Cas and C3G bind PDGFR bound Crk
Reactome:R-HSA-382053
Translocation of PDGF from ER to Golgi
Reactome:R-HSA-382054
PDGF binds to extracellular matrix proteins
Reactome:R-HSA-382055
Grb7 binds to the active PDGF receptor
Reactome:R-HSA-382056
Crk binds to the active PDGF receptor
Reactome:R-HSA-382058
Nck binds to the active PDGF receptor
Reactome:R-HSA-389083
Autophosphorylation of PDGF alpha receptors
Reactome:R-HSA-389086
Autophosphorylation of PDGF alpha/beta receptors
Reactome:R-HSA-481007
Exocytosis of platelet alpha granule contents
Reactome:R-HSA-5672965
RAS GEFs promote RAS nucleotide exchange
Reactome:R-HSA-8864036
PTPN12 dephosphorylates PDGFRB at Y1021
Reactome:R-HSA-8865275
PDGF-BB clevage by Furin
Reactome:R-HSA-8865276
PDGF-AB clevage by Furin
Reactome:R-HSA-9674093
PDGFRs bind type I TKI
file:human/PDGFB/PDGFB-deep-research-falcon.md
Falcon deep research report on PDGFB
  • PDGFB is a secreted PDGF ligand whose core GO-relevant evidence is receptor binding, growth factor activity, dimerization, extracellular localization, and ligand-attributable vascular/mural-cell processes.
    "This report summarizes **GO-relevant evidence for PDGFB as a secreted PDGF ligand**: disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), **direct binding/activation of PDGF receptor dimers (PDGFRA/PDGFRB)**, secretion/localization (extracellular space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only where explicitly stated), and **ligand-attributable biological processes** (pericyte recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing evidence). It **excludes** receptor **intrinsic kinase activity** (peptidyl-tyrosine phosphorylation), downstream pathway terms (PI3K–AKT, ERK/MAPK, ROS/NADPH oxidase), and broad transcriptional/miRNA effects unless strictly necessary to interpret ligand localization or binding (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7)."
  • PDGFB should not be annotated with receptor tyrosine kinase activity or generic downstream PI3K/AKT, ERK/MAPK, ROS, or transcriptional outputs as core functions.
    "Do **not** annotate PDGFB with receptor enzymatic activities (e.g., **protein tyrosine kinase activity**, **peptidyl-tyrosine phosphorylation**) or generic downstream pathways (PI3K/AKT, ERK/MAPK, ROS) based solely on PDGFR signaling descriptions; these belong to PDGF receptors or downstream effectors, not the PDGFB ligand itself (fredriksson2004thepdgffamily pages 5-7, strell2024functionalandclinical pages 3-5)."
file:human/PDGFB/PDGFB-uniprot.txt
UniProtKB P01127 record for PDGFB

Deep Research

Falcon

(PDGFB-deep-research-falcon.md)
Question: You are an expert researcher providing comprehensive, well-cited information. Falcon Edison Scientific Literature 32 citations 2026-05-13T00:42:21.188140

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Concise GO annotation research for human PDGFB / UniProt P01127. Focus only on GO-relevant evidence for platelet-derived growth factor subunit B: core molecular function as a secreted/disulfide-linked PDGF receptor ligand and growth factor; PDGFB homodimer and PDGFA-PDGFB heterodimer formation; direct binding/activation of PDGFRA and PDGFRB receptor dimers; platelet-derived growth factor receptor signaling pathway; receptor ligand activity and growth factor activity; extracellular region/space, secreted protein, extracellular matrix retention, ER/Golgi secretory processing, platelet alpha granule if directly supported. Evaluate biological processes including chemotaxis, cell migration, mesenchymal/pericyte/vascular smooth muscle proliferation and recruitment, angiogenesis/blood vessel development, wound healing, placenta/heart/kidney glomerulus development, and mesangial cell proliferation/migration only where directly supported. Distinguish PDGFB ligand functions from receptor intracellular kinase activity, peptidyl-tyrosine phosphorylation, PI3K-AKT/ERK/MAPK downstream signaling, ROS/NADPH oxidase, transcription/gene-expression/miRNA effects, generic protein binding, and broad proliferation/migration terms. Include PMID/DOI citations and keep under 1700 words.

Concise GO annotation research report: Human PDGFB (UniProt P01127)β€”GO-relevant ligand evidence (≀1700 words)

0) Scope and curation rules (GO-focused)

This report summarizes GO-relevant evidence for PDGFB as a secreted PDGF ligand: disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), direct binding/activation of PDGF receptor dimers (PDGFRA/PDGFRB), secretion/localization (extracellular space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only where explicitly stated), and ligand-attributable biological processes (pericyte recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing evidence). It excludes receptor intrinsic kinase activity (peptidyl-tyrosine phosphorylation), downstream pathway terms (PI3K–AKT, ERK/MAPK, ROS/NADPH oxidase), and broad transcriptional/miRNA effects unless strictly necessary to interpret ligand localization or binding (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7).

1) Key GO concepts/definitions (current understanding relevant to PDGFB)

PDGFB encodes the PDGF B-chain, which participates in secreted, disulfide-linked dimeric ligands (notably PDGF‑BB homodimer and PDGF‑AB heterodimer with PDGFA) that activate PDGF receptors by promoting receptor dimerization (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7, duran2018molecularregulationof pages 9-11). PDGF ligands act extracellularly as growth factors for mesenchymal lineage target cells and vascular mural cells (pericytes/smooth muscle) in paracrine signaling contexts (duran2018molecularregulationof pages 9-11, strell2024functionalandclinical pages 3-5).

2) Molecular function (MF): ligand/dimerization and receptor binding specificity

2.1 Disulfide-linked PDGF dimers; PDGF‑BB and PDGF‑AB

A foundational biosynthesis study explicitly describes PDGF as assembled into disulfide-linked AA, AB, and BB dimers and analyzes PDGF‑BB biogenesis (ostman1992pdgfaaandpdgfbb pages 1-2). Review-level summaries also state PDGF ligands (including PDGF‑BB) are disulfide-linked dimers (strell2024functionalandclinical pages 1-3), consistent with the canonical PDGF family description (fredriksson2004thepdgffamily pages 5-7).

2.2 Direct binding/activation of PDGF receptor dimers (PDGFRA/PDGFRB)

A well-cited PDGF family review summarizes receptor specificity at the ligand level: PDGF‑BB can bind/activate PDGFRΞ² and can also stimulate PDGFRΞ±/Ξ² heterodimers; PDGF‑AB and PDGF‑BB can stimulate PDGFRΞ±/Ξ² heterodimers; and PDGF‑AA/AB/BB are among ligands engaging PDGFRΞ±-containing complexes (fredriksson2004thepdgffamily pages 5-7). A classic experimental study provides a direct chain-specific rule: the Ξ± receptor binds A- or B-chain, whereas the Ξ² receptor binds only B-chain, supporting annotation of PDGFB as necessary for PDGFRΞ²-binding ligands (ostman1992pdgfaaandpdgfbb pages 1-2).

GO MF recommendations (plain-English): β€œPDGF receptor binding” and β€œgrowth factor activity,” with the binding scope emphasizing receptor dimer activation via extracellular ligand, not receptor catalytic activity (fredriksson2004thepdgffamily pages 5-7, ostman1992pdgfaaandpdgfbb pages 1-2).

3) Cellular component (CC): secretion, secretory pathway processing, ECM retention, platelet Ξ±-granule

3.1 ER/Golgi secretory processing (direct evidence)

Γ–stman et al. (J Cell Biol; Aug 1992; DOI 10.1083/jcb.118.3.509; https://doi.org/10.1083/jcb.118.3.509) provide direct experimental evidence that PDGF chains dimerize in the ER and that proteolytic processing occurs distal to the ER (Golgi). PDGF‑BB formed a minor secreted ~30 kDa form and a major cell-associated ~24 kDa form; brefeldin A and chloroquine experiments supported ERβ†’Golgi trafficking, Golgi processing, and lysosomal degradation of retained PDGF‑BB (ostman1992pdgfaaandpdgfbb pages 1-2, ostman1992pdgfaaandpdgfbb pages 2-3).

GO CC recommendation: annotate secretory pathway involvement as ER dimerization and Golgi processing/trafficking evidence for a secreted ligand, without over-asserting stable ER/Golgi residence as the mature localization (ostman1992pdgfaaandpdgfbb pages 1-2, ostman1992pdgfaaandpdgfbb pages 2-3).

3.2 Extracellular localization and secretion

PDGF‑AA/AB/BB are described as secreted in active form, supporting extracellular localization of mature PDGF‑B-containing ligands (duran2018molecularregulationof pages 9-11).

GO CC recommendation: β€œextracellular region/space” consistent with secreted ligand function (duran2018molecularregulationof pages 9-11).

3.3 Extracellular matrix (ECM)/cell-surface retention via heparan sulfate (HS) (direct in vivo evidence)

Abramsson et al. (Genes & Development; Feb 2007; DOI 10.1101/gad.398207; https://doi.org/10.1101/gad.398207) provide strong direct evidence that PDGF‑B contains a conserved C-terminal basic/heparin-binding β€˜retention motif’ whose deletion impairs PDGF‑BB retention and produces defective vascular mural cell coverage in vivo, consistent with HS-dependent retention near endothelium (abramsson2007defectivensulfationof pages 1-2). These findings support a GO-relevant CC concept of ECM/cell-surface association mediated by HS rather than purely freely diffusible extracellular localization.

Figure evidence (visual): Abramsson et al. figures include (i) images showing reduced pericyte coverage in retention/HS mutants and (ii) a schematic of HS–PDGF‑BB retention motif interaction (abramsson2007defectivensulfationof media b90fa2f5, abramsson2007defectivensulfationof media cfcc7e5d).

3.4 Platelet Ξ±-granule localization (explicitly stated; review-level)

Karampini et al. (Arterioscler Thromb Vasc Biol; Jun 2020; DOI 10.1161/ATVBAHA.120.314245; https://doi.org/10.1161/ATVBAHA.120.314245) explicitly lists PDGFB among platelet Ξ±-granule contents (karampini2020orchestrationofprimary pages 2-3). This supports annotating platelet Ξ±-granule localization, with the caveat that this is a review statement in the retrieved excerpt (not a primary imaging/proteomics experiment shown here).

4) Biological process (BP): ligand-attributable processes with direct support

4.1 Pericyte recruitment/coverage in vascular development (strong direct support)

Abramsson et al. directly connect PDGF‑BB HS-dependent retention to pericyte recruitment/coverage during vascular development: altering HS sulfation or deleting the PDGF‑B retention motif reduces PDGF‑BB binding/retention and leads to deficient pericyte investment (abramsson2007defectivensulfationof pages 1-2, abramsson2007defectivensulfationof media b90fa2f5). A 2024 authoritative review further summarizes genetic evidence that Pdgfb/Pdgfrb deficiency causes lethal vascular defects including microvascular bleeding and reduced pericyte coverage, and specifically cites impaired endothelial PDGF‑B retention phenotypes (published online 9 Jul 2024; DOI 10.1007/s10555-024-10194-7; https://doi.org/10.1007/s10555-024-10194-7) (strell2024functionalandclinical pages 3-5, strell2024functionalandclinical pages 12-13).

GO BP recommendation: β€œpericyte recruitment,” β€œpericyte coverage,” or β€œmural cell recruitment” in vascular development contexts (abramsson2007defectivensulfationof pages 1-2, strell2024functionalandclinical pages 3-5).

4.2 Angiogenesis/blood vessel morphogenesis (supported via mural cell axis)

PDGF‑B/PDGFRΞ² signaling is summarized as required for vessel function and morphogenesis, with phenotypes including abnormal capillary morphogenesis and endothelial hyperplasia when disrupted; in tumor models, truncation/retention defects in PDGF‑B associate with reduced pericyte coverage and impaired angiogenesis (strell2024functionalandclinical pages 3-5, strell2024functionalandclinical pages 12-13). A comprehensive physiology review also discusses PDGF‑B in new vessel growth contexts and links PDGF‑B/PDGFRΞ² to mural cell migration/proliferation (DOI 10.1002/cphy.c160048; https://doi.org/10.1002/cphy.c160048) (duran2018molecularregulationof pages 9-11).

GO BP recommendation: β€œangiogenesis”/β€œblood vessel morphogenesis,” preferably framed through the endothelial–mural cell axis rather than generic proliferation statements (strell2024functionalandclinical pages 3-5, duran2018molecularregulationof pages 9-11).

4.3 Chemotaxis/cell migration and proliferation (limited specificity)

Some retrieved sources describe PDGF ligands broadly as chemoattractants/mitogens and discuss PDGF-driven migration/proliferation, but these statements are largely review-level and not always cell-type specific in the provided excerpts (chan2019aninvestigationon pages 24-27, duran2018molecularregulationof pages 9-11). For GO annotation, the strongest support in this evidence set is to annotate pericyte/mural cell recruitment and related vascular processes, rather than broad β€œcell migration” or β€œcell proliferation” (abramsson2007defectivensulfationof pages 1-2, strell2024functionalandclinical pages 3-5).

4.4 Requested developmental/kidney/mesangial/placenta termsβ€”status

Within the retrieved and excerpted evidence, there is no direct support sufficient to annotate PDGFB specifically to: placenta development, heart development, kidney glomerulus development, or mesangial cell proliferation/migration (as distinct BP terms) without importing additional primary sources beyond those gathered here (duran2018molecularregulationof pages 9-11, strell2024functionalandclinical pages 3-5).

5) Recent developments (prioritizing 2023–2024) and real-world implementations (GO-relevant)

5.1 2023: Engineering PDGF‑BB for ECM retention (localization-focused application)

Alshoubaki et al. (NPJ Regenerative Medicine; May 2023; DOI 10.1038/s41536-023-00297-0; https://doi.org/10.1038/s41536-023-00297-0) report a translational approach that increases ECM binding/retention of therapeutic proteins by fusing an amphiregulin-derived ECM-binding motif; fusion to PDGF‑BB increased ECM binding affinity (reported 5–50Γ—) and enhanced local retention in ECM-mimetic matrices compared with wild-type PDGF‑BB (alshoubaki2023asuperiorextracellular pages 3-4). While the excerpt does not reproduce all numeric time-course values, it provides GO-relevant, quantitative assay context including hydrogel composition (e.g., inclusion of heparan sulfate), PDGF‑BB loading (500 ng/ml), plasmin-triggered release, and typical sample sizes (nβ‰ˆ4 per time point in the described assays) (alshoubaki2023asuperiorextracellular pages 9-10).

GO relevance: supports the general principle that ECM-binding/retention of PDGF‑BB modulates localization, but engineered constructs are not direct evidence of native PDGFB CC terms; use primarily as application context (alshoubaki2023asuperiorextracellular pages 3-4).

5.2 2024: Authoritative synthesis of PDGF‑BB/PDGFRΞ² vascular mural cell axis

Strell et al. (Cancer Metastasis Reviews; published online 9 Jul 2024; DOI 10.1007/s10555-024-10194-7) synthesize genetic and disease evidence highlighting the PDGF‑BB/PDGFRΞ² endothelial–mural cell axis and vascular phenotypes tied to PDGF‑B ligand function (strell2024functionalandclinical pages 3-5, strell2024functionalandclinical pages 1-3).

GO aspect Recommended GO concept Evidence summary Key supporting citation(s) with DOI/URL Notes/exclusions
MF PDGF receptor binding PDGF-B-containing ligands directly bind/activate PDGF receptors; the B-chain binds the Ξ± receptor and is required for Ξ² receptor binding, with PDGF-BB engaging PDGFRΞ²-containing dimers and PDGF-AB/BB engaging PDGFRΞ±Ξ². Γ–stman et al., 1992, J Cell Biol, DOI: https://doi.org/10.1083/jcb.118.3.509; Fredriksson et al., 2004, DOI: https://doi.org/10.1016/j.cytogfr.2004.03.007; Strell et al., 2024, DOI: https://doi.org/10.1007/s10555-024-10194-7 (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7, strell2024functionalandclinical pages 1-3) Annotate ligand binding/activation only; exclude receptor intrinsic kinase activity, transphosphorylation, PI3K-AKT/ERK/MAPK downstream terms.
MF Growth factor activity PDGF-B is described as a potent mitogen/growth factor for mesenchymal-derived target cells, consistent with canonical growth factor activity. Γ–stman et al., 1992, DOI: https://doi.org/10.1083/jcb.118.3.509; Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048 (ostman1992pdgfaaandpdgfbb pages 1-2, duran2018molecularregulationof pages 9-11) Keep broad growth factor activity only where tied to extracellular ligand action, not downstream gene-expression outputs.
MF Secreted disulfide-linked dimer PDGF family ligands are secreted disulfide-linked dimers, and PDGF-B participates in these active extracellular dimers. Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048; Strell et al., 2024, DOI: https://doi.org/10.1007/s10555-024-10194-7 (duran2018molecularregulationof pages 9-11, strell2024functionalandclinical pages 1-3) Structural/biochemical property; do not confuse with receptor dimerization or intracellular receptor complexes.
MF PDGF-BB homodimer and PDGF-AB heterodimer formation PDGF is assembled as AA, AB, and BB dimers; PDGF-B therefore forms both PDGF-BB homodimer and PDGF-AB heterodimer. Γ–stman et al., 1992, DOI: https://doi.org/10.1083/jcb.118.3.509; Fredriksson et al., 2004, DOI: https://doi.org/10.1016/j.cytogfr.2004.03.007 (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily pages 5-7) Appropriate for complex/dimer formation language; avoid unsupported claims about other isoforms not containing PDGFB.
CC Endoplasmic reticulum dimerization during secretion Pulse-chase and brefeldin A studies showed newly synthesized PDGF chains dimerize in the ER before later proteolytic processing. Γ–stman et al., 1992, DOI: https://doi.org/10.1083/jcb.118.3.509 (ostman1992pdgfaaandpdgfbb pages 1-2, ostman1992pdgfaaandpdgfbb pages 2-3) Best used as secretory-pathway processing support; not evidence for stable ER residency as final localization.
CC Golgi processing / secretory pathway PDGF-B precursors undergo proteolytic processing distal to the ER in the Golgi, yielding a minor secreted 30-kD form and a major intracellular retained 24-kD form. Γ–stman et al., 1992, DOI: https://doi.org/10.1083/jcb.118.3.509 (ostman1992pdgfaaandpdgfbb pages 1-2, ostman1992pdgfaaandpdgfbb pages 2-3) Supports biosynthetic processing, not a final functional localization term at the plasma membrane or cytosol.
CC Extracellular region / extracellular space / secreted protein PDGF-AA, -AB, and -BB are secreted in active form, supporting extracellular localization of the mature ligand. Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048; Corsinovi, 2018 (duran2018molecularregulationof pages 9-11, corsinovi2018daniorerioand pages 15-19) Strong CC support for extracellular/secreted protein; more specific extracellular matrix annotation needs separate retention evidence.
CC Extracellular matrix or cell-surface heparan sulfate-dependent retention via C-terminal basic motif A conserved C-terminal basic/heparin-binding retention motif in PDGF-B mediates HS-dependent cell-surface/ECM retention, and loss of this motif reduces retention. Abramsson et al., 2007, Genes Dev, DOI: https://doi.org/10.1101/gad.398207; Fredriksson et al., 2004, DOI: https://doi.org/10.1016/j.cytogfr.2004.03.007 (abramsson2007defectivensulfationof pages 1-2, fredriksson2004thepdgffamily pages 5-7) Good support for matrix/cell-surface retention of the ligand; distinguish from generic protein binding and from engineered ECM-binding studies.
CC Platelet alpha granule Review evidence explicitly states PDGFB/PDGF-B is present in platelet Ξ±-granules and released with Ξ±-granule contents upon activation. Karampini et al., 2020, DOI: https://doi.org/10.1161/ATVBAHA.120.314245 (karampini2020orchestrationofprimary pages 2-3) Direct support is review-level rather than a primary localization experiment here; use cautiously if stricter experimental evidence is required.
BP Pericyte recruitment / pericyte coverage during vascular development Endothelial PDGF-BB is a key ligand for mural cell recruitment, and impaired HS-dependent retention or Pdgfb loss causes defective pericyte investment/coverage. Abramsson et al., 2007, DOI: https://doi.org/10.1101/gad.398207; Strell et al., 2024, DOI: https://doi.org/10.1007/s10555-024-10194-7 (abramsson2007defectivensulfationof pages 1-2, strell2024functionalandclinical pages 3-5, strell2024functionalandclinical pages 12-13) Strongly supported BP; preferable to generic β€œcell migration” because it is directly linked to PDGF-B ligand function in vivo.
BP Angiogenesis / blood vessel morphogenesis Loss of PDGF-B signaling causes microvascular defects, abnormal capillary morphogenesis, reduced pericyte coverage, and impaired angiogenesis, supporting vascular development roles. Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048; Strell et al., 2024, DOI: https://doi.org/10.1007/s10555-024-10194-7 (duran2018molecularregulationof pages 9-11, strell2024functionalandclinical pages 3-5, strell2024functionalandclinical pages 12-13) Attribute to ligand-driven mural cell recruitment and vessel stabilization; exclude receptor downstream signaling terms.
BP Wound healing / granulation tissue formation PDGF-B/PDGF-BB is described as promoting new vessel growth in wound-healing contexts, and PDGF-BB-stimulated granulation tissue formation is reported in vivo. Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048; Prasad et al., 2019, DOI: https://doi.org/10.1111/wrr.12744 (via cited evidence summary) (duran2018molecularregulationof pages 9-11) Support exists, but some cited wound-healing data are from PDGF-BB reagent studies rather than direct human PDGFB gene perturbation; annotate conservatively.
BP Positive regulation of mesenchymal/pericyte/VSMC proliferation and migration/chemotaxis PDGF-BB directly supports pericyte migration/proliferation and mesenchymal/VSMC recruitment in vascular development, with older literature and reviews also describing PDGF as a chemoattractant/mitogen. Duran et al., 2018, DOI: https://doi.org/10.1002/cphy.c160048; Abramsson et al., 2007, DOI: https://doi.org/10.1101/gad.398207; Chan, 2019 (duran2018molecularregulationof pages 9-11, abramsson2007defectivensulfationof pages 1-2, chan2019aninvestigationon pages 24-27) Use only qualified, cell-type-specific terms; avoid broad generic proliferation/migration annotations unless directly tied to PDGF-B ligand action.

Table: This table summarizes recommended GO-relevant annotations for human PDGFB based on direct evidence for ligand function, secretion/localization, and supported biological processes. It is useful for separating bona fide PDGFB ligand annotations from excluded receptor-kinase and downstream signaling claims.

7) Key exclusions (to avoid mis-annotation)

Do not annotate PDGFB with receptor enzymatic activities (e.g., protein tyrosine kinase activity, peptidyl-tyrosine phosphorylation) or generic downstream pathways (PI3K/AKT, ERK/MAPK, ROS) based solely on PDGFR signaling descriptions; these belong to PDGF receptors or downstream effectors, not the PDGFB ligand itself (fredriksson2004thepdgffamily pages 5-7, strell2024functionalandclinical pages 3-5).

8) Core references (URLs/DOIs; publication dates)

  • Γ–stman A. et al. Aug 1992. PDGF-AA and PDGF-BB biosynthesis… J Cell Biol. DOI: 10.1083/jcb.118.3.509. https://doi.org/10.1083/jcb.118.3.509 (ostman1992pdgfaaandpdgfbb pages 1-2)
  • Abramsson A. et al. Feb 2007. Defective N-sulfation… limits PDGF-BB binding and pericyte recruitment… Genes Dev. DOI: 10.1101/gad.398207. https://doi.org/10.1101/gad.398207 (abramsson2007defectivensulfationof pages 1-2)
  • Fredriksson L. et al. Aug 2004. The PDGF family: four gene products form five dimeric isoforms. Cytokine Growth Factor Rev. DOI: 10.1016/j.cytogfr.2004.03.007. https://doi.org/10.1016/j.cytogfr.2004.03.007 (fredriksson2004thepdgffamily pages 5-7)
  • Karampini E. et al. Jun 2020. Orchestration of primary hemostasis… ATVB. DOI: 10.1161/ATVBAHA.120.314245. https://doi.org/10.1161/ATVBAHA.120.314245 (karampini2020orchestrationofprimary pages 2-3)
  • Alshoubaki YK. et al. May 2023. A superior extracellular matrix binding motif… NPJ Regen Med. DOI: 10.1038/s41536-023-00297-0. https://doi.org/10.1038/s41536-023-00297-0 (alshoubaki2023asuperiorextracellular pages 3-4)
  • Strell C. et al. Jul 2024 (online 9 Jul 2024). Functional and clinical roles of stromal PDGF receptors in tumor biology. Cancer Metastasis Rev. DOI: 10.1007/s10555-024-10194-7. https://doi.org/10.1007/s10555-024-10194-7 (strell2024functionalandclinical pages 1-3)

References

  1. (ostman1992pdgfaaandpdgfbb pages 1-2): A. Γ–stman, J. Thyberg, B. Westermark, and C. Heldin. Pdgf-aa and pdgf-bb biosynthesis: proprotein processing in the golgi complex and lysosomal degradation of pdgf-bb retained intracellularly. The Journal of Cell Biology, 118:509-519, Aug 1992. URL: https://doi.org/10.1083/jcb.118.3.509, doi:10.1083/jcb.118.3.509. This article has 120 citations.

  2. (fredriksson2004thepdgffamily pages 5-7): Linda Fredriksson, Hong Li, and Ulf Eriksson. The pdgf family: four gene products form five dimeric isoforms. Cytokine & growth factor reviews, 15 4:197-204, Aug 2004. URL: https://doi.org/10.1016/j.cytogfr.2004.03.007, doi:10.1016/j.cytogfr.2004.03.007. This article has 1215 citations and is from a peer-reviewed journal.

  3. (duran2018molecularregulationof pages 9-11): Camille L. Duran, David W. Howell, J. Dave, Rebecca Smith, M. Torrie, J. Essner, and K. Bayless. Molecular regulation of sprouting angiogenesis. Comprehensive Physiology, 8 1:153-235, Dec 2018. URL: https://doi.org/10.1002/cphy.c160048, doi:10.1002/cphy.c160048. This article has 107 citations and is from a peer-reviewed journal.

  4. (strell2024functionalandclinical pages 3-5): Carina Strell, Elisabet RodrΓ­guez-TomΓ s, and Arne Γ–stman. Functional and clinical roles of stromal pdgf receptors in tumor biology. Cancer Metastasis Reviews, 43:1593-1609, Jul 2024. URL: https://doi.org/10.1007/s10555-024-10194-7, doi:10.1007/s10555-024-10194-7. This article has 26 citations.

  5. (strell2024functionalandclinical pages 1-3): Carina Strell, Elisabet RodrΓ­guez-TomΓ s, and Arne Γ–stman. Functional and clinical roles of stromal pdgf receptors in tumor biology. Cancer Metastasis Reviews, 43:1593-1609, Jul 2024. URL: https://doi.org/10.1007/s10555-024-10194-7, doi:10.1007/s10555-024-10194-7. This article has 26 citations.

  6. (ostman1992pdgfaaandpdgfbb pages 2-3): A. Γ–stman, J. Thyberg, B. Westermark, and C. Heldin. Pdgf-aa and pdgf-bb biosynthesis: proprotein processing in the golgi complex and lysosomal degradation of pdgf-bb retained intracellularly. The Journal of Cell Biology, 118:509-519, Aug 1992. URL: https://doi.org/10.1083/jcb.118.3.509, doi:10.1083/jcb.118.3.509. This article has 120 citations.

  7. (abramsson2007defectivensulfationof pages 1-2): Alexandra Abramsson, Sindhulakshmi Kurup, Marta Busse, Shuhei Yamada, Per Lindblom, Edith Schallmeiner, Denise Stenzel, Dominique Sauvaget, Johan Ledin, Maria Ringvall, Ulf Landegren, Lena KjellΓ©n, GΓΆran Bondjers, Jin-ping Li, Ulf Lindahl, Dorothe Spillmann, Christer Betsholtz, and Holger Gerhardt. Defective n-sulfation of heparan sulfate proteoglycans limits pdgf-bb binding and pericyte recruitment in vascular development. Genes & development, 21 3:316-31, Feb 2007. URL: https://doi.org/10.1101/gad.398207, doi:10.1101/gad.398207. This article has 239 citations and is from a highest quality peer-reviewed journal.

  8. (abramsson2007defectivensulfationof media b90fa2f5): Alexandra Abramsson, Sindhulakshmi Kurup, Marta Busse, Shuhei Yamada, Per Lindblom, Edith Schallmeiner, Denise Stenzel, Dominique Sauvaget, Johan Ledin, Maria Ringvall, Ulf Landegren, Lena KjellΓ©n, GΓΆran Bondjers, Jin-ping Li, Ulf Lindahl, Dorothe Spillmann, Christer Betsholtz, and Holger Gerhardt. Defective n-sulfation of heparan sulfate proteoglycans limits pdgf-bb binding and pericyte recruitment in vascular development. Genes & development, 21 3:316-31, Feb 2007. URL: https://doi.org/10.1101/gad.398207, doi:10.1101/gad.398207. This article has 239 citations and is from a highest quality peer-reviewed journal.

  9. (abramsson2007defectivensulfationof media cfcc7e5d): Alexandra Abramsson, Sindhulakshmi Kurup, Marta Busse, Shuhei Yamada, Per Lindblom, Edith Schallmeiner, Denise Stenzel, Dominique Sauvaget, Johan Ledin, Maria Ringvall, Ulf Landegren, Lena KjellΓ©n, GΓΆran Bondjers, Jin-ping Li, Ulf Lindahl, Dorothe Spillmann, Christer Betsholtz, and Holger Gerhardt. Defective n-sulfation of heparan sulfate proteoglycans limits pdgf-bb binding and pericyte recruitment in vascular development. Genes & development, 21 3:316-31, Feb 2007. URL: https://doi.org/10.1101/gad.398207, doi:10.1101/gad.398207. This article has 239 citations and is from a highest quality peer-reviewed journal.

  10. (karampini2020orchestrationofprimary pages 2-3): Ellie Karampini, Ruben Bierings, and Jan Voorberg. Orchestration of primary hemostasis by platelet and endothelial lysosome-related organelles. Arteriosclerosis, Thrombosis, and Vascular Biology, 40:1441-1453, Jun 2020. URL: https://doi.org/10.1161/atvbaha.120.314245, doi:10.1161/atvbaha.120.314245. This article has 63 citations and is from a domain leading peer-reviewed journal.

  11. (strell2024functionalandclinical pages 12-13): Carina Strell, Elisabet RodrΓ­guez-TomΓ s, and Arne Γ–stman. Functional and clinical roles of stromal pdgf receptors in tumor biology. Cancer Metastasis Reviews, 43:1593-1609, Jul 2024. URL: https://doi.org/10.1007/s10555-024-10194-7, doi:10.1007/s10555-024-10194-7. This article has 26 citations.

  12. (chan2019aninvestigationon pages 24-27): CPSL Chan. An investigation on the role of non-canonical hedgehog signalling in cell migration. Unknown journal, 2019.

  13. (alshoubaki2023asuperiorextracellular pages 3-4): Yasmin K. Alshoubaki, Yen-Zhen Lu, Julien M. D. Legrand, Rezvan Karami, Mathilde Fossat, Ekaterina Salimova, Ziad Julier, and MikaΓ«l M. Martino. A superior extracellular matrix binding motif to enhance the regenerative activity and safety of therapeutic proteins. NPJ Regenerative Medicine, May 2023. URL: https://doi.org/10.1038/s41536-023-00297-0, doi:10.1038/s41536-023-00297-0. This article has 14 citations and is from a peer-reviewed journal.

  14. (alshoubaki2023asuperiorextracellular pages 9-10): Yasmin K. Alshoubaki, Yen-Zhen Lu, Julien M. D. Legrand, Rezvan Karami, Mathilde Fossat, Ekaterina Salimova, Ziad Julier, and MikaΓ«l M. Martino. A superior extracellular matrix binding motif to enhance the regenerative activity and safety of therapeutic proteins. NPJ Regenerative Medicine, May 2023. URL: https://doi.org/10.1038/s41536-023-00297-0, doi:10.1038/s41536-023-00297-0. This article has 14 citations and is from a peer-reviewed journal.

  15. (corsinovi2018daniorerioand pages 15-19): D Corsinovi. Danio rerio and xenopus laevis embryos: alternative and valuable models to unveil new molecular mechanisms involved in glioma progression. Unknown journal, 2018.

Citations

  1. ostman1992pdgfaaandpdgfbb pages 1-2
  2. strell2024functionalandclinical pages 1-3
  3. fredriksson2004thepdgffamily pages 5-7
  4. duran2018molecularregulationof pages 9-11
  5. abramsson2007defectivensulfationof pages 1-2
  6. karampini2020orchestrationofprimary pages 2-3
  7. alshoubaki2023asuperiorextracellular pages 3-4
  8. alshoubaki2023asuperiorextracellular pages 9-10
  9. strell2024functionalandclinical pages 3-5
  10. ostman1992pdgfaaandpdgfbb pages 2-3
  11. strell2024functionalandclinical pages 12-13
  12. chan2019aninvestigationon pages 24-27
  13. corsinovi2018daniorerioand pages 15-19
  14. https://doi.org/10.1083/jcb.118.3.509
  15. https://doi.org/10.1101/gad.398207
  16. https://doi.org/10.1161/ATVBAHA.120.314245
  17. https://doi.org/10.1007/s10555-024-10194-7
  18. https://doi.org/10.1002/cphy.c160048
  19. https://doi.org/10.1038/s41536-023-00297-0
  20. https://doi.org/10.1083/jcb.118.3.509;
  21. https://doi.org/10.1016/j.cytogfr.2004.03.007;
  22. https://doi.org/10.1002/cphy.c160048;
  23. https://doi.org/10.1016/j.cytogfr.2004.03.007
  24. https://doi.org/10.1101/gad.398207;
  25. https://doi.org/10.1111/wrr.12744
  26. https://doi.org/10.1083/jcb.118.3.509,
  27. https://doi.org/10.1016/j.cytogfr.2004.03.007,
  28. https://doi.org/10.1002/cphy.c160048,
  29. https://doi.org/10.1007/s10555-024-10194-7,
  30. https://doi.org/10.1101/gad.398207,
  31. https://doi.org/10.1161/atvbaha.120.314245,
  32. https://doi.org/10.1038/s41536-023-00297-0,

πŸ“š Additional Documentation

Notes

(PDGFB-notes.md)

PDGFB notes

2026-05-13 Falcon deep research integration

Falcon synthesis supports PDGFB as a secreted PDGF ligand rather than a receptor
kinase or downstream signaling enzyme
[file:human/PDGFB/PDGFB-deep-research-falcon.md "This report summarizes GO-relevant evidence for PDGFB as a secreted PDGF ligand: disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), direct binding/activation of PDGF receptor dimers (PDGFRA/PDGFRB), secretion/localization (extracellular space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only where explicitly stated), and ligand-attributable biological processes (pericyte recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing evidence)."].

The review decisions therefore keep receptor binding, growth factor/receptor
ligand activity, extracellular/extracellular-matrix localization, dimerization,
PDGF receptor signaling, angiogenesis, chemotaxis, and supported mural-cell or
mesenchymal responses. Receptor autophosphorylation, PI3K/AKT, ERK/MAPK,
ROS/NADPH oxidase, and transcription/miRNA terms were marked as downstream
over-annotations or modified to PDGF receptor signaling where the source really
supported ligand-triggered receptor activation
[file:human/PDGFB/PDGFB-deep-research-falcon.md "Do not annotate PDGFB with receptor enzymatic activities (e.g., protein tyrosine kinase activity, peptidyl-tyrosine phosphorylation) or generic downstream pathways (PI3K/AKT, ERK/MAPK, ROS) based solely on PDGFR signaling descriptions; these belong to PDGF receptors or downstream effectors, not the PDGFB ligand itself"].

πŸ“„ View Raw YAML

id: P01127
gene_symbol: PDGFB
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  PDGFB encodes the platelet-derived growth factor B chain, a secreted, disulfide-linked PDGF
  ligand subunit. Mature PDGF-B-containing dimers, especially PDGF-BB and PDGF-AB, bind and
  activate PDGF receptor dimers at the cell surface and drive paracrine growth-factor signaling.
  The core GO picture is receptor ligand/growth factor activity, PDGF receptor binding, extracellular
  and extracellular-matrix-associated localization, and PDGF-receptor signaling that promotes
  mural-cell/pericyte recruitment, vascular development, chemotaxis, migration, and proliferation
  in supported cell-type contexts. Receptor tyrosine kinase activity, receptor autophosphorylation,
  PI3K/AKT, ERK/MAPK, ROS/NADPH oxidase, and transcriptional outputs are downstream pathway
  consequences and should not be treated as core PDGFB molecular functions.
existing_annotations:
  - term:
      id: GO:0008284
      label: positive regulation of cell population proliferation
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        positive regulation of cell population proliferation is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Broad positive regulation of cell population proliferation is a downstream growth-factor
        outcome. Keep it as supported but non-core; more specific cell-type proliferation
        terms and the core ligand/receptor-binding function are more informative.
  - term:
      id: GO:0030335
      label: positive regulation of cell migration
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        positive regulation of cell migration is supported or plausible for PDGFB but represents
        a context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Broad positive regulation of cell migration is a downstream ligand response. Keep
        it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis
        and PDGF receptor signaling terms.
  - term:
      id: GO:0001525
      label: angiogenesis
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        angiogenesis is supported for PDGFB in the context of its mature extracellular PDGF
        ligand function.
      action: ACCEPT
      reason: >-
        Angiogenesis is supported through the PDGF-B/PDGFRB endothelial-mural cell axis, especially
        pericyte recruitment and vessel stabilization.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
      supported_by:
        - reference_id: file:human/PDGFB/PDGFB-deep-research-falcon.md
          supporting_text: >-
            **GO MF recommendations (plain-English):** β€œPDGF receptor binding” and β€œgrowth
            factor activity,” with the binding scope emphasizing **receptor dimer activation
            via extracellular ligand**, not receptor catalytic activity (fredriksson2004thepdgffamily
            pages 5-7, ostman1992pdgfaaandpdgfbb pages 1-2).
  - term:
      id: GO:0005615
      label: extracellular space
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        extracellular space is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular space is an appropriate localization for the mature secreted PDGF-B-containing
        ligand.
  - term:
      id: GO:0070374
      label: positive regulation of ERK1 and ERK2 cascade
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: >-
        positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically
        connected but over-annotated for the PDGFB ligand compared with the PDGF receptor
        signaling pathway term.
  - term:
      id: GO:0050918
      label: positive chemotaxis
    evidence_type: IEA
    original_reference_id: GO_REF:0000108
    review:
      summary: >-
        positive chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis
        process.
      action: ACCEPT
      reason: >-
        Accept. positive chemotaxis is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0007169
      label: cell surface receptor protein tyrosine kinase signaling pathway
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        cell surface receptor protein tyrosine kinase signaling pathway captures a related
        signaling idea, but the term has the wrong scope or aspect for PDGFB.
      action: MODIFY
      reason: >-
        The parent receptor tyrosine kinase signaling term is directionally correct but too
        broad. PDGFB specifically initiates platelet-derived growth factor receptor signaling.
      proposed_replacement_terms:
        - id: GO:0048008
          label: platelet-derived growth factor receptor signaling pathway
  - term:
      id: GO:0008083
      label: growth factor activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: >-
        growth factor activity is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Growth factor activity is a core PDGFB function. The mature ligand acts extracellularly
        as a mitogen/chemoattractant for mesenchymal and vascular mural cell populations.
  - term:
      id: GO:0010468
      label: regulation of gene expression
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        regulation of gene expression is biologically connected to PDGFB signaling but overstates
        the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        Regulation of gene expression is a broad downstream response to PDGF signaling and
        should not be treated as a PDGFB core function.
  - term:
      id: GO:0010557
      label: positive regulation of macromolecule biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        positive regulation of macromolecule biosynthetic process is supported or plausible
        for PDGFB but represents a context-specific localization, storage, processing, or
        downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Macromolecule biosynthesis is a broad downstream response to PDGF signaling and is
        less informative than PDGF receptor signaling or cell-type-specific growth terms.
  - term:
      id: GO:0014911
      label: positive regulation of smooth muscle cell migration
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        positive regulation of smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      reason: >-
        Accept. smooth muscle cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0016020
      label: membrane
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    review:
      summary: >-
        membrane is supported or plausible for PDGFB but represents a context-specific localization,
        storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Membrane is too broad for PDGFB; any membrane association is a precursor/retention
        or receptor-bound context, so keep only as non-core.
  - term:
      id: GO:0048018
      label: receptor ligand activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        receptor ligand activity is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Receptor ligand activity is an appropriate parent-level molecular function for PDGFB
        because the mature PDGF-B-containing dimer activates cell-surface PDGF receptors.
  - term:
      id: GO:0048661
      label: positive regulation of smooth muscle cell proliferation
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      reason: >-
        Accept. smooth muscle cell proliferation is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0051239
      label: regulation of multicellular organismal process
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        regulation of multicellular organismal process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Regulation of multicellular organismal process is too broad for core PDGFB biology;
        retain only as a non-core propagated summary of developmental effects.
  - term:
      id: GO:0051781
      label: positive regulation of cell division
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: >-
        positive regulation of cell division is supported or plausible for PDGFB but represents
        a context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Positive regulation of cell division is a broad downstream outcome of growth-factor
        signaling, not a core ligand function.
  - term:
      id: GO:1902533
      label: positive regulation of intracellular signal transduction
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: >-
        positive regulation of intracellular signal transduction is biologically connected
        to PDGFB signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        Positive regulation of intracellular signal transduction is too broad and downstream
        for the extracellular PDGFB ligand.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:10806482
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:10806482
          supporting_text: PDGF-C is a new protease-activated ligand for the PDGF
            alpha-receptor.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:11297552
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:11297552
          supporting_text: 2001 Apr 10. Platelet-derived growth factor C (PDGF-C), a
            novel growth factor that binds to PDGF alpha and beta receptor.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:17981115
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17981115
          supporting_text: Anti-PlGF inhibits growth of VEGF(R)-inhibitor-resistant
            tumors without affecting healthy vessels.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:20534510
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:20534510
          supporting_text: Structures of a platelet-derived growth factor/propeptide
            complex and a platelet-derived growth factor/receptor complex.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:32296183
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:32296183
          supporting_text: Apr 8. A reference map of the human binary protein
            interactome.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:7679113
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:7679113
          supporting_text: Mechanism of platelet-derived growth factor (PDGF) AA, AB,
            and BB binding to alpha and beta PDGF receptor.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0042802
      label: identical protein binding
    evidence_type: IPI
    original_reference_id: PMID:1396586
    review:
      summary: >-
        identical protein binding is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:1396586
          supporting_text: Crystal structure of human platelet-derived growth factor BB.
      reason: >-
        PDGFB forms the disulfide-linked PDGF-BB homodimer; identical protein binding captures
        that ligand-dimer assembly when supported by PDGF-BB structural or receptor-binding
        evidence.
  - term:
      id: GO:0042802
      label: identical protein binding
    evidence_type: IPI
    original_reference_id: PMID:23139410
    review:
      summary: >-
        PMID:23139410 is a modified DNA aptamer/SOMAmer structure with PDGF-BB as the target,
        not direct evidence for PDGFB-PDGFB identical protein binding.
      action: REMOVE
      supported_by:
        - reference_id: PMID:23139410
          supporting_text: >-
            Here we report a unique crystal structure of a SOMAmer bound to its target,
            platelet-derived growth factor B (PDGF-BB).
      reason: >-
        Remove this specific GOA evidence row because the publication supports DNA aptamer
        binding to PDGF-BB rather than PDGFB self-association. The same GO term remains supported
        by PMID:1396586 and PMID:7679113.
  - term:
      id: GO:0042802
      label: identical protein binding
    evidence_type: IPI
    original_reference_id: PMID:7679113
    review:
      summary: >-
        identical protein binding is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:7679113
          supporting_text: Mechanism of platelet-derived growth factor (PDGF) AA, AB,
            and BB binding to alpha and beta PDGF receptor.
      reason: >-
        PDGFB forms the disulfide-linked PDGF-BB homodimer; identical protein binding captures
        that ligand-dimer assembly when supported by PDGF-BB structural or receptor-binding
        evidence.
  - term:
      id: GO:0036120
      label: cellular response to platelet-derived growth factor stimulus
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        cellular response to platelet-derived growth factor stimulus is biologically connected
        to PDGFB signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        Cellular response to platelet-derived growth factor stimulus describes responding
        cells; PDGFB is the ligand stimulus, so this is over-annotated for the gene product.
  - term:
      id: GO:0043410
      label: positive regulation of MAPK cascade
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        positive regulation of MAPK cascade is biologically connected to PDGFB signaling but
        overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        MAPK cascade activation is downstream of receptor signaling and is less appropriate
        for PDGFB than PDGF receptor signaling pathway.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0014805
      label: smooth muscle adaptation
    evidence_type: NAS
    original_reference_id: PMID:16477012
    review:
      summary: >-
        smooth muscle adaptation is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:16477012
          supporting_text: Synergistic roles of platelet-derived growth factor-BB and
            interleukin-1beta in phenotypic modulation of human aortic smooth muscle
            cells.
      reason: >-
        Smooth muscle adaptation is a vascular smooth muscle phenotype downstream of PDGF
        signaling and should remain non-core.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:16477012
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:16477012
          supporting_text: Synergistic roles of platelet-derived growth factor-BB and
            interleukin-1beta in phenotypic modulation of human aortic smooth muscle
            cells.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:16477012
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:16477012
          supporting_text: Synergistic roles of platelet-derived growth factor-BB and
            interleukin-1beta in phenotypic modulation of human aortic smooth muscle
            cells.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: NAS
    original_reference_id: PMID:7679113
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:7679113
          supporting_text: Mechanism of platelet-derived growth factor (PDGF) AA, AB,
            and BB binding to alpha and beta PDGF receptor.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0035556
      label: intracellular signal transduction
    evidence_type: IMP
    original_reference_id: PMID:24008408
    review:
      summary: >-
        intracellular signal transduction is biologically connected to PDGFB signaling but
        overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:24008408
          supporting_text: CAP37 activation of PKC promotes human corneal epithelial
            cell chemotaxis.
      reason: >-
        Intracellular signal transduction is a downstream cellular response and not an activity
        or localization of the secreted PDGFB ligand.
  - term:
      id: GO:0008284
      label: positive regulation of cell population proliferation
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        positive regulation of cell population proliferation is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        Broad positive regulation of cell population proliferation is a downstream growth-factor
        outcome. Keep it as supported but non-core; more specific cell-type proliferation
        terms and the core ligand/receptor-binding function are more informative.
  - term:
      id: GO:0010467
      label: gene expression
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        gene expression is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        Gene expression is a downstream cellular response and is over-annotated for the PDGFB
        ligand.
  - term:
      id: GO:0010629
      label: negative regulation of gene expression
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        negative regulation of gene expression is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        Negative regulation of gene expression is a downstream transcriptional response to
        PDGF signaling, not a core ligand function.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:1904707
      label: positive regulation of vascular associated smooth muscle cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell proliferation is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        Accept. vascular smooth muscle cell proliferation is a supported biological process
        downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain
        for PDGFB.
  - term:
      id: GO:1905064
      label: negative regulation of vascular associated smooth muscle cell
        differentiation
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        negative regulation of vascular associated smooth muscle cell differentiation is supported
        or plausible for PDGFB but represents a context-specific localization, storage, processing,
        or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        Negative regulation of vascular smooth muscle differentiation is a supported VSMC
        phenotype of PDGF-BB treatment but is secondary to the core ligand/receptor signaling
        function.
  - term:
      id: GO:1905176
      label: positive regulation of vascular associated smooth muscle cell
        dedifferentiation
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell dedifferentiation is
        supported or plausible for PDGFB but represents a context-specific localization, storage,
        processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        Positive regulation of vascular smooth muscle dedifferentiation is a supported VSMC
        phenotype but is secondary to core PDGFB ligand activity.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: EXP
    original_reference_id: PMID:20534510
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:20534510
          supporting_text: Structures of a platelet-derived growth factor/propeptide
            complex and a platelet-derived growth factor/receptor complex.
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
  - term:
      id: GO:0010628
      label: positive regulation of gene expression
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        positive regulation of gene expression is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        Positive regulation of gene expression is a downstream transcriptional response to
        PDGF signaling, not a core ligand function.
  - term:
      id: GO:0036120
      label: cellular response to platelet-derived growth factor stimulus
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        cellular response to platelet-derived growth factor stimulus is biologically connected
        to PDGFB signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        Cellular response to platelet-derived growth factor stimulus describes responding
        cells; PDGFB is the ligand stimulus, so this is over-annotated for the gene product.
  - term:
      id: GO:0048661
      label: positive regulation of smooth muscle cell proliferation
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      reason: >-
        Accept. smooth muscle cell proliferation is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0010629
      label: negative regulation of gene expression
    evidence_type: IDA
    original_reference_id: PMID:23554459
    review:
      summary: >-
        negative regulation of gene expression is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:23554459
          supporting_text: Apr 3. MicroRNA-638 is highly expressed in human vascular
            smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and
            migration through targeting orphan nuclear receptor NOR1.
      reason: >-
        Negative regulation of gene expression is a downstream transcriptional response to
        PDGF signaling, not a core ligand function.
  - term:
      id: GO:1902894
      label: negative regulation of miRNA transcription
    evidence_type: IDA
    original_reference_id: PMID:26493107
    review:
      summary: >-
        negative regulation of miRNA transcription is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:26493107
          supporting_text: Epub 2015 Oct 19. miRNA-34a reduces neointima formation
            through inhibiting smooth muscle cell proliferation and migration.
      reason: >-
        Negative regulation of miRNA transcription is a downstream VSMC transcriptional effect
        and not a core PDGFB function.
  - term:
      id: GO:1902895
      label: positive regulation of miRNA transcription
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        positive regulation of miRNA transcription is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        Positive regulation of miRNA transcription is a downstream VSMC transcriptional effect
        and not a core PDGFB function.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:19126672
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:19126672
          supporting_text: Jan 6. Spontaneous phosphoinositide 3-kinase signaling
            dynamics drive spreading and random migration of fibroblasts.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0010811
      label: positive regulation of cell-substrate adhesion
    evidence_type: IDA
    original_reference_id: PMID:19126672
    review:
      summary: >-
        positive regulation of cell-substrate adhesion is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:19126672
          supporting_text: Jan 6. Spontaneous phosphoinositide 3-kinase signaling
            dynamics drive spreading and random migration of fibroblasts.
      reason: >-
        Cell-substrate adhesion is a downstream cellular behavior in PDGF-stimulated cells
        and is non-core relative to ligand binding and receptor signaling.
  - term:
      id: GO:0010628
      label: positive regulation of gene expression
    evidence_type: IDA
    original_reference_id: PMID:23554459
    review:
      summary: >-
        positive regulation of gene expression is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:23554459
          supporting_text: Apr 3. MicroRNA-638 is highly expressed in human vascular
            smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and
            migration through targeting orphan nuclear receptor NOR1.
      reason: >-
        Positive regulation of gene expression is a downstream transcriptional response to
        PDGF signaling, not a core ligand function.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:23554459
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:23554459
          supporting_text: Apr 3. MicroRNA-638 is highly expressed in human vascular
            smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and
            migration through targeting orphan nuclear receptor NOR1.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:1904707
      label: positive regulation of vascular associated smooth muscle cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:23554459
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell proliferation is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:23554459
          supporting_text: Apr 3. MicroRNA-638 is highly expressed in human vascular
            smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and
            migration through targeting orphan nuclear receptor NOR1.
      reason: >-
        Accept. vascular smooth muscle cell proliferation is a supported biological process
        downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain
        for PDGFB.
  - term:
      id: GO:1904754
      label: positive regulation of vascular associated smooth muscle cell migration
    evidence_type: IDA
    original_reference_id: PMID:23554459
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell migration is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:23554459
          supporting_text: Apr 3. MicroRNA-638 is highly expressed in human vascular
            smooth muscle cells and inhibits PDGF-BB-induced cell proliferation and
            migration through targeting orphan nuclear receptor NOR1.
      reason: >-
        Accept. vascular smooth muscle cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0008284
      label: positive regulation of cell population proliferation
    evidence_type: IDA
    original_reference_id: PMID:2439522
    review:
      summary: >-
        positive regulation of cell population proliferation is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2439522
          supporting_text: PDGF induces c-myc mRNA expression in MG-63 human
            osteosarcoma cells but does not stimulate cell replication.
      reason: >-
        Broad positive regulation of cell population proliferation is a downstream growth-factor
        outcome. Keep it as supported but non-core; more specific cell-type proliferation
        terms and the core ligand/receptor-binding function are more informative.
  - term:
      id: GO:0031012
      label: extracellular matrix
    evidence_type: HDA
    original_reference_id: PMID:23979707
    review:
      summary: >-
        extracellular matrix is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:23979707
          supporting_text: Epub 2013 Aug 26. SILAC-based proteomics of human primary
            endothelial cell morphogenesis unveils tumor angiogenic markers.
      reason: >-
        Extracellular matrix association is supported by the PDGF-B C-terminal retention motif
        and heparan-sulfate/extracellular-matrix retention evidence.
  - term:
      id: GO:1904707
      label: positive regulation of vascular associated smooth muscle cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:12070119
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell proliferation is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:12070119
          supporting_text: Adipocyte-derived plasma protein adiponectin acts as a
            platelet-derived growth factor-BB-binding protein and regulates growth
            factor-induced common postreceptor signal in vascular smooth muscle cell.
      reason: >-
        Accept. vascular smooth muscle cell proliferation is a supported biological process
        downstream of PDGF-B-containing ligand signaling and is sufficiently specific to retain
        for PDGFB.
  - term:
      id: GO:1904754
      label: positive regulation of vascular associated smooth muscle cell migration
    evidence_type: IDA
    original_reference_id: PMID:12070119
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell migration is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:12070119
          supporting_text: Adipocyte-derived plasma protein adiponectin acts as a
            platelet-derived growth factor-BB-binding protein and regulates growth
            factor-induced common postreceptor signal in vascular smooth muscle cell.
      reason: >-
        Accept. vascular smooth muscle cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0048661
      label: positive regulation of smooth muscle cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:21321938
    review:
      summary: >-
        positive regulation of smooth muscle cell proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:21321938
          supporting_text: Interleukin-18/WNT1-inducible signaling pathway protein-1
            signaling mediates human saphenous vein smooth muscle cell proliferation.
      reason: >-
        Accept. smooth muscle cell proliferation is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0035655
      label: interleukin-18-mediated signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:21321938
    review:
      summary: >-
        interleukin-18-mediated signaling pathway is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:21321938
          supporting_text: Interleukin-18/WNT1-inducible signaling pathway protein-1
            signaling mediates human saphenous vein smooth muscle cell proliferation.
      reason: >-
        Interleukin-18-mediated signaling is a context-specific downstream inflammatory pathway
        and not a direct PDGFB ligand function.
  - term:
      id: GO:0010629
      label: negative regulation of gene expression
    evidence_type: IDA
    original_reference_id: PMID:25089138
    review:
      summary: >-
        negative regulation of gene expression is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:25089138
          supporting_text: 2014 Jul 25. miR-18a-5p MicroRNA Increases Vascular Smooth
            Muscle Cell Differentiation by Downregulating Syndecan4.
      reason: >-
        Negative regulation of gene expression is a downstream transcriptional response to
        PDGF signaling, not a core ligand function.
  - term:
      id: GO:0045892
      label: negative regulation of DNA-templated transcription
    evidence_type: IDA
    original_reference_id: PMID:25089138
    review:
      summary: >-
        negative regulation of DNA-templated transcription is biologically connected to PDGFB
        signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:25089138
          supporting_text: 2014 Jul 25. miR-18a-5p MicroRNA Increases Vascular Smooth
            Muscle Cell Differentiation by Downregulating Syndecan4.
      reason: >-
        Negative regulation of DNA-templated transcription is a downstream transcriptional
        response and is over-annotated for the extracellular ligand.
  - term:
      id: GO:0005796
      label: Golgi lumen
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865275
    review:
      summary: >-
        Golgi lumen is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Golgi lumen reflects secretory processing of PDGF-B precursors and should be retained
        as non-core rather than treated as the mature ligand localization.
  - term:
      id: GO:0005796
      label: Golgi lumen
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865276
    review:
      summary: >-
        Golgi lumen is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Golgi lumen reflects secretory processing of PDGF-B precursors and should be retained
        as non-core rather than treated as the mature ligand localization.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-1524182
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-1524186
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186765
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186773
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186778
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186780
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186786
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186798
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186800
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186819
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186826
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-186834
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-2316434
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-2396337
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-2400009
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-380780
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-380782
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382052
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382054
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382055
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382056
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382058
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-389083
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-389086
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-481007
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-5672965
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8864036
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865275
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865276
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-9674093
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:1904754
      label: positive regulation of vascular associated smooth muscle cell migration
    evidence_type: IDA
    original_reference_id: PMID:19088079
    review:
      summary: >-
        positive regulation of vascular associated smooth muscle cell migration is supported
        as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:19088079
          supporting_text: Dec 15. Induction of microRNA-221 by platelet-derived growth
            factor signaling is critical for modulation of vascular smooth muscle
            phenotype.
      reason: >-
        Accept. vascular smooth muscle cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: IDA
    original_reference_id: PMID:2439522
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2439522
          supporting_text: PDGF induces c-myc mRNA expression in MG-63 human
            osteosarcoma cells but does not stimulate cell replication.
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
  - term:
      id: GO:0008083
      label: growth factor activity
    evidence_type: IDA
    original_reference_id: PMID:12070119
    review:
      summary: >-
        growth factor activity is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:12070119
          supporting_text: Adipocyte-derived plasma protein adiponectin acts as a
            platelet-derived growth factor-BB-binding protein and regulates growth
            factor-induced common postreceptor signal in vascular smooth muscle cell.
      reason: >-
        Growth factor activity is a core PDGFB function. The mature ligand acts extracellularly
        as a mitogen/chemoattractant for mesenchymal and vascular mural cell populations.
  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IDA
    original_reference_id: PMID:2538439
    review:
      summary: >-
        cell surface is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2538439
          supporting_text: Collagen-induced binding to human platelets of
            platelet-derived growth factor leading to inhibition of P43 and P20
            phosphorylation.
      reason: >-
        Cell surface association is compatible with PDGF receptor binding and heparan-sulfate
        retention, but extracellular region/matrix are more precise mature ligand locations.
  - term:
      id: GO:0005788
      label: endoplasmic reticulum lumen
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382053
    review:
      summary: >-
        endoplasmic reticulum lumen is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Endoplasmic reticulum lumen reflects precursor folding/dimerization in the secretory
        pathway and is non-core for the mature extracellular ligand.
  - term:
      id: GO:0000139
      label: Golgi membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-382053
    review:
      summary: >-
        Golgi membrane is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Golgi membrane reflects secretory pathway processing/trafficking context and is non-core
        for the mature extracellular ligand.
  - term:
      id: GO:0000139
      label: Golgi membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865275
    review:
      summary: >-
        Golgi membrane is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Golgi membrane reflects secretory pathway processing/trafficking context and is non-core
        for the mature extracellular ligand.
  - term:
      id: GO:0000139
      label: Golgi membrane
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-8865276
    review:
      summary: >-
        Golgi membrane is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Golgi membrane reflects secretory pathway processing/trafficking context and is non-core
        for the mature extracellular ligand.
  - term:
      id: GO:0031093
      label: platelet alpha granule lumen
    evidence_type: TAS
    original_reference_id: Reactome:R-HSA-481007
    review:
      summary: >-
        platelet alpha granule lumen is supported or plausible for PDGFB but represents a
        context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Platelet alpha granule lumen is a supported storage/release localization for platelet
        PDGF-B, but not the primary mature-ligand site of action.
  - term:
      id: GO:0030335
      label: positive regulation of cell migration
    evidence_type: IDA
    original_reference_id: PMID:21245381
    review:
      summary: >-
        positive regulation of cell migration is supported or plausible for PDGFB but represents
        a context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:21245381
          supporting_text: Jan 18. Neuropilin-1 signaling through p130Cas tyrosine
            phosphorylation is essential for growth factor-dependent migration of glioma
            and endothelial cells.
      reason: >-
        Broad positive regulation of cell migration is a downstream ligand response. Keep
        it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis
        and PDGF receptor signaling terms.
  - term:
      id: GO:0042056
      label: chemoattractant activity
    evidence_type: IDA
    original_reference_id: PMID:21245381
    review:
      summary: >-
        chemoattractant activity is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:21245381
          supporting_text: Jan 18. Neuropilin-1 signaling through p130Cas tyrosine
            phosphorylation is essential for growth factor-dependent migration of glioma
            and endothelial cells.
      reason: >-
        Chemoattractant activity is consistent with PDGF-BB ligand function and the chemotactic
        responses to PDGF-B-containing ligands.
  - term:
      id: GO:0071363
      label: cellular response to growth factor stimulus
    evidence_type: IDA
    original_reference_id: PMID:21245381
    review:
      summary: >-
        cellular response to growth factor stimulus is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:21245381
          supporting_text: Jan 18. Neuropilin-1 signaling through p130Cas tyrosine
            phosphorylation is essential for growth factor-dependent migration of glioma
            and endothelial cells.
      reason: >-
        Cellular response to growth factor stimulus describes responding cells and is over-annotated
        for the extracellular PDGFB ligand.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:2536956
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:2536956
          supporting_text: Isolation of a novel receptor cDNA establishes the existence
            of two PDGF receptor genes.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:1900127
      label: positive regulation of hyaluronan biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:17324121
    review:
      summary: >-
        positive regulation of hyaluronan biosynthetic process is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:17324121
          supporting_text: 'Growth factor regulation of hyaluronan synthesis and degradation
            in human dermal fibroblasts: importance of hyaluronan for the mitogenic response
            of PDGF-BB.'
      reason: >-
        Hyaluronan biosynthesis is a fibroblast/extracellular-matrix downstream response to
        PDGF stimulation and is non-core.
  - term:
      id: GO:0045893
      label: positive regulation of DNA-templated transcription
    evidence_type: IDA
    original_reference_id: PMID:17324121
    review:
      summary: >-
        positive regulation of DNA-templated transcription is biologically connected to PDGFB
        signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17324121
          supporting_text: 'Growth factor regulation of hyaluronan synthesis and degradation
            in human dermal fibroblasts: importance of hyaluronan for the mitogenic response
            of PDGF-BB.'
      reason: >-
        Positive regulation of DNA-templated transcription is a downstream transcriptional
        response and is over-annotated for the extracellular ligand.
  - term:
      id: GO:0048146
      label: positive regulation of fibroblast proliferation
    evidence_type: IDA
    original_reference_id: PMID:17324121
    review:
      summary: >-
        positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:17324121
          supporting_text: 'Growth factor regulation of hyaluronan synthesis and degradation
            in human dermal fibroblasts: importance of hyaluronan for the mitogenic response
            of PDGF-BB.'
      reason: >-
        Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0030097
      label: hemopoiesis
    evidence_type: IMP
    original_reference_id: PMID:11264163
    negated: true
    review:
      summary: >-
        hemopoiesis is supported for PDGFB in the context of its mature extracellular PDGF
        ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:11264163
          supporting_text: Basis of hematopoietic defects in platelet-derived growth
            factor (PDGF)-B and PDGF beta-receptor null mice.
      reason: >-
        Accept as a NOT annotation. The cited mouse chimera study indicates hematopoietic
        PDGF-B/PDGFRB expression is not required for normal hematopoiesis, while non-hematopoietic
        PDGF signaling has inflammatory roles.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:21245381
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:21245381
          supporting_text: Jan 18. Neuropilin-1 signaling through p130Cas tyrosine
            phosphorylation is essential for growth factor-dependent migration of glioma
            and endothelial cells.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0060326
      label: cell chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:21245381
    review:
      summary: >-
        cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:21245381
          supporting_text: Jan 18. Neuropilin-1 signaling through p130Cas tyrosine
            phosphorylation is essential for growth factor-dependent migration of glioma
            and endothelial cells.
      reason: >-
        Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0035793
      label: positive regulation of metanephric mesenchymal cell migration by
        platelet-derived growth factor receptor-beta signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:19019919
    review:
      summary: >-
        positive regulation of metanephric mesenchymal cell migration by platelet-derived
        growth factor receptor-beta signaling pathway is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:19019919
          supporting_text: PDGF receptor-{beta} modulates metanephric mesenchyme
            chemotaxis induced by PDGF AA.
      reason: >-
        Accept. metanephric mesenchymal cell migration via PDGFRB signaling is a supported
        biological process downstream of PDGF-B-containing ligand signaling and is sufficiently
        specific to retain for PDGFB.
  - term:
      id: GO:2000573
      label: positive regulation of DNA biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:10644978
    review:
      summary: >-
        positive regulation of DNA biosynthetic process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:10644978
          supporting_text: PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated
            mitogenesis.
      reason: >-
        DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling,
        not a direct PDGFB molecular function.
  - term:
      id: GO:2000573
      label: positive regulation of DNA biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:10734101
    review:
      summary: >-
        positive regulation of DNA biosynthetic process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:10734101
          supporting_text: Platelet-derived growth factor receptor beta regulates
            migration and DNA synthesis in metanephric mesenchymal cells.
      reason: >-
        DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling,
        not a direct PDGFB molecular function.
  - term:
      id: GO:2000573
      label: positive regulation of DNA biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of DNA biosynthetic process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling,
        not a direct PDGFB molecular function.
  - term:
      id: GO:2000573
      label: positive regulation of DNA biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        positive regulation of DNA biosynthetic process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling,
        not a direct PDGFB molecular function.
  - term:
      id: GO:2000573
      label: positive regulation of DNA biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:19019919
    review:
      summary: >-
        positive regulation of DNA biosynthetic process is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:19019919
          supporting_text: PDGF receptor-{beta} modulates metanephric mesenchyme
            chemotaxis induced by PDGF AA.
      reason: >-
        DNA biosynthetic process is a downstream mitogenic readout of PDGF receptor signaling,
        not a direct PDGFB molecular function.
  - term:
      id: GO:2000591
      label: positive regulation of metanephric mesenchymal cell migration
    evidence_type: IDA
    original_reference_id: PMID:10734101
    review:
      summary: >-
        positive regulation of metanephric mesenchymal cell migration is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:10734101
          supporting_text: Platelet-derived growth factor receptor beta regulates
            migration and DNA synthesis in metanephric mesenchymal cells.
      reason: >-
        Accept. metanephric mesenchymal cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0016323
      label: basolateral plasma membrane
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        basolateral plasma membrane is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Basolateral plasma membrane is a polarized-cell localization context and not the mature
        ligand core localization.
  - term:
      id: GO:0045840
      label: positive regulation of mitotic nuclear division
    evidence_type: IDA
    original_reference_id: PMID:10644978
    review:
      summary: >-
        positive regulation of mitotic nuclear division is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:10644978
          supporting_text: PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated
            mitogenesis.
      reason: >-
        Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and
        should not be promoted as a core PDGFB function.
  - term:
      id: GO:0048146
      label: positive regulation of fibroblast proliferation
    evidence_type: IDA
    original_reference_id: PMID:10644978
    review:
      summary: >-
        positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:10644978
          supporting_text: PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated
            mitogenesis.
      reason: >-
        Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0060326
      label: cell chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:16014047
    review:
      summary: >-
        cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:16014047
          supporting_text: Hypoxia regulates PDGF-B interactions between glomerular
            capillary endothelial and mesangial cells.
      reason: >-
        Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0060326
      label: cell chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:17991872
    review:
      summary: >-
        cell chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:17991872
          supporting_text: 'TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis
            in different cell types: involvement of Src and PLC.'
      reason: >-
        Accept. cell chemotaxis is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0070374
      label: positive regulation of ERK1 and ERK2 cascade
    evidence_type: IDA
    original_reference_id: PMID:16530387
    review:
      summary: >-
        positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:16530387
          supporting_text: c-Src couples PI 3 kinase/Akt and MAPK signaling to
            PDGF-induced DNA synthesis in mesangial cells.
      reason: >-
        ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically
        connected but over-annotated for the PDGFB ligand compared with the PDGF receptor
        signaling pathway term.
  - term:
      id: GO:0072126
      label: positive regulation of glomerular mesangial cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:16014047
    review:
      summary: >-
        positive regulation of glomerular mesangial cell proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:16014047
          supporting_text: Hypoxia regulates PDGF-B interactions between glomerular
            capillary endothelial and mesangial cells.
      reason: >-
        Real but non-core: glomerular mesangial cell proliferation is a
        tissue-specific process downstream of PDGF-B/PDGFR ligand signaling, not
        a core molecular function of the secreted ligand. Surfaced by the
        ASSAY_TO_FUNCTION analysis (indirect signaling-ligand effect on a
        proliferation readout).
  - term:
      id: GO:0018108
      label: peptidyl-tyrosine phosphorylation
    evidence_type: IDA
    original_reference_id: PMID:10734101
    review:
      summary: >-
        peptidyl-tyrosine phosphorylation captures a related signaling idea, but the term
        has the wrong scope or aspect for PDGFB.
      action: MODIFY
      proposed_replacement_terms:
        - id: GO:0048008
          label: platelet-derived growth factor receptor signaling pathway
      supported_by:
        - reference_id: PMID:10734101
          supporting_text: Platelet-derived growth factor receptor beta regulates
            migration and DNA synthesis in metanephric mesenchymal cells.
      reason: >-
        The evidence describes PDGF receptor autophosphorylation after ligand binding. PDGFB
        is not the tyrosine kinase; replace the phosphorylation term with PDGF receptor signaling
        pathway.
  - term:
      id: GO:0030335
      label: positive regulation of cell migration
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of cell migration is supported or plausible for PDGFB but represents
        a context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        Broad positive regulation of cell migration is a downstream ligand response. Keep
        it as non-core where supported, while prioritizing cell-type-specific migration/chemotaxis
        and PDGF receptor signaling terms.
  - term:
      id: GO:0043406
      label: positive regulation of MAP kinase activity
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of MAP kinase activity is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        Positive regulation of MAP kinase activity is a downstream receptor/effectors readout,
        not a direct PDGFB activity.
  - term:
      id: GO:0043410
      label: positive regulation of MAPK cascade
    evidence_type: IMP
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of MAPK cascade is biologically connected to PDGFB signaling but
        overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        MAPK cascade activation is downstream of receptor signaling and is less appropriate
        for PDGFB than PDGF receptor signaling pathway.
  - term:
      id: GO:0045840
      label: positive regulation of mitotic nuclear division
    evidence_type: IDA
    original_reference_id: PMID:10734101
    review:
      summary: >-
        positive regulation of mitotic nuclear division is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:10734101
          supporting_text: Platelet-derived growth factor receptor beta regulates
            migration and DNA synthesis in metanephric mesenchymal cells.
      reason: >-
        Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and
        should not be promoted as a core PDGFB function.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:10734101
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:10734101
          supporting_text: Platelet-derived growth factor receptor beta regulates
            migration and DNA synthesis in metanephric mesenchymal cells.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0051897
      label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B
        signal transduction
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
        is biologically connected to PDGFB signaling but overstates the direct function of
        the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        PI3K/AKT signaling is a downstream PDGF receptor pathway. It is not a direct PDGFB
        molecular function and should not be promoted as core for the ligand.
  - term:
      id: GO:0070374
      label: positive regulation of ERK1 and ERK2 cascade
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically
        connected but over-annotated for the PDGFB ligand compared with the PDGF receptor
        signaling pathway term.
  - term:
      id: GO:0072126
      label: positive regulation of glomerular mesangial cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:11788434
    review:
      summary: >-
        positive regulation of glomerular mesangial cell proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:11788434
          supporting_text: Effect of platelet-derived growth factor isoforms in rat
            metanephric mesenchymal cells.
      reason: >-
        Real but non-core, consistent with the GO:0072126 annotation from
        PMID:16014047: a tissue-specific proliferation process downstream of
        PDGF-B/PDGFR signaling rather than a core molecular function.
  - term:
      id: GO:0006468
      label: protein phosphorylation
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        protein phosphorylation captures a related signaling idea, but the term has the wrong
        scope or aspect for PDGFB.
      action: MODIFY
      proposed_replacement_terms:
        - id: GO:0048008
          label: platelet-derived growth factor receptor signaling pathway
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        The evidence describes downstream phosphorylation after PDGFB activates PDGF receptors.
        PDGFB itself does not catalyze protein phosphorylation, so replace with PDGF receptor
        signaling pathway.
  - term:
      id: GO:0016176
      label: superoxide-generating NADPH oxidase activator activity
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        superoxide-generating NADPH oxidase activator activity is not supported as a PDGFB
        gene-product function or mature localization.
      action: REMOVE
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        Remove. Superoxide-generating NADPH oxidase activator activity belongs to NADPH oxidase
        regulatory machinery, not to the secreted PDGFB ligand.
  - term:
      id: GO:0043406
      label: positive regulation of MAP kinase activity
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        positive regulation of MAP kinase activity is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        Positive regulation of MAP kinase activity is a downstream receptor/effectors readout,
        not a direct PDGFB activity.
  - term:
      id: GO:0045840
      label: positive regulation of mitotic nuclear division
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        positive regulation of mitotic nuclear division is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        Mitotic nuclear division is a downstream proliferation readout of PDGF signaling and
        should not be promoted as a core PDGFB function.
  - term:
      id: GO:0050921
      label: positive regulation of chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:19019919
    review:
      summary: >-
        positive regulation of chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type
        or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:19019919
          supporting_text: PDGF receptor-{beta} modulates metanephric mesenchyme
            chemotaxis induced by PDGF AA.
      reason: >-
        Accept. positive regulation of chemotaxis is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0070374
      label: positive regulation of ERK1 and ERK2 cascade
    evidence_type: IDA
    original_reference_id: PMID:17942966
    review:
      summary: >-
        positive regulation of ERK1 and ERK2 cascade is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        ERK1/ERK2 cascade activation is downstream of PDGF receptor signaling. It is biologically
        connected but over-annotated for the PDGFB ligand compared with the PDGF receptor
        signaling pathway term.
  - term:
      id: GO:0072593
      label: reactive oxygen species metabolic process
    evidence_type: IMP
    original_reference_id: PMID:17942966
    review:
      summary: >-
        reactive oxygen species metabolic process is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:17942966
          supporting_text: 2007 Oct 17. Mitogenic signaling via platelet-derived growth
            factor beta in metanephric mesenchymal cells.
      reason: >-
        Reactive oxygen species metabolism is a downstream PDGFR/NADPH oxidase pathway readout
        and should not be assigned as a PDGFB core process.
  - term:
      id: GO:0090280
      label: positive regulation of calcium ion import
    evidence_type: IDA
    original_reference_id: PMID:19019919
    review:
      summary: >-
        positive regulation of calcium ion import is biologically connected to PDGFB signaling
        but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:19019919
          supporting_text: PDGF receptor-{beta} modulates metanephric mesenchyme
            chemotaxis induced by PDGF AA.
      reason: >-
        Calcium ion import is a downstream PDGFRB signaling response, not a direct PDGFB ligand
        function.
  - term:
      id: GO:2000379
      label: positive regulation of reactive oxygen species metabolic process
    evidence_type: IDA
    original_reference_id: PMID:19019919
    review:
      summary: >-
        positive regulation of reactive oxygen species metabolic process is biologically connected
        to PDGFB signaling but overstates the direct function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:19019919
          supporting_text: PDGF receptor-{beta} modulates metanephric mesenchyme
            chemotaxis induced by PDGF AA.
      reason: >-
        Reactive oxygen species regulation is downstream of receptor signaling and NADPH oxidases
        and is over-annotated for PDGFB.
  - term:
      id: GO:0001892
      label: embryonic placenta development
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        embryonic placenta development is supported or plausible for PDGFB but represents
        a context-specific localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Placenta development is consistent with organismal phenotypes of PDGFB/PDGFRB disruption
        but is a developmental outcome, not a core molecular function.
  - term:
      id: GO:0003104
      label: positive regulation of glomerular filtration
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        positive regulation of glomerular filtration is supported or plausible for PDGFB but
        represents a context-specific localization, storage, processing, or downstream biological
        outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Glomerular filtration is an organ-level consequence of PDGFB-dependent glomerular/mesangial
        development and should be kept as non-core.
  - term:
      id: GO:0007507
      label: heart development
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        heart development is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Heart development is a broad developmental outcome of PDGFB pathway function and is
        non-core for this ligand review.
  - term:
      id: GO:0038001
      label: paracrine signaling
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        paracrine signaling is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      reason: >-
        Paracrine signaling is appropriate for PDGFB because endothelial and platelet-derived
        PDGF-B acts as an extracellular signal to neighboring PDGF receptor-expressing cells.
  - term:
      id: GO:0072255
      label: metanephric glomerular mesangial cell development
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        metanephric glomerular mesangial cell development is supported or plausible for PDGFB
        but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      reason: >-
        Metanephric glomerular mesangial cell development is a supported developmental role
        downstream of PDGFB/PDGFRB signaling, but non-core relative to ligand activity.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:12070119
    review:
      summary: >-
        protein binding is biologically connected to PDGFB signaling but overstates the direct
        function of the secreted ligand.
      action: MARK_AS_OVER_ANNOTATED
      supported_by:
        - reference_id: PMID:12070119
          supporting_text: Adipocyte-derived plasma protein adiponectin acts as a
            platelet-derived growth factor-BB-binding protein and regulates growth
            factor-induced common postreceptor signal in vascular smooth muscle cell.
      reason: >-
        Generic protein binding is uninformative for PDGFB. Specific terms such as PDGF receptor
        binding, collagen binding, homodimerization, heterodimerization, or extracellular-matrix
        retention should be used instead.
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        cytoplasm is not supported as a PDGFB gene-product function or mature localization.
      action: REMOVE
      reason: >-
        Remove. PDGFB is a secretory pathway/extracellular ligand; cytoplasm is not a supported
        mature localization for this gene product in the reviewed evidence.
  - term:
      id: GO:0071506
      label: cellular response to mycophenolic acid
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    review:
      summary: >-
        cellular response to mycophenolic acid is not supported as a PDGFB gene-product function
        or mature localization.
      action: REMOVE
      reason: >-
        Remove. Cellular response to mycophenolic acid is a drug-response annotation and does
        not represent PDGFB ligand function.
  - term:
      id: GO:0002548
      label: monocyte chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:17991872
    review:
      summary: >-
        monocyte chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type or chemotaxis
        process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:17991872
          supporting_text: 'TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis
            in different cell types: involvement of Src and PLC.'
      reason: >-
        Accept. monocyte chemotaxis is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0005518
      label: collagen binding
    evidence_type: IDA
    original_reference_id: PMID:8900172
    review:
      summary: >-
        collagen binding is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:8900172
          supporting_text: Type I, II, III, IV, V, and VI collagens serve as
            extracellular ligands for the isoforms of platelet-derived growth factor
            (AA, BB, and AB).
      reason: >-
        Collagen binding is a supported, specific extracellular-matrix interaction for PDGF
        isoforms and is more informative than generic protein binding.
  - term:
      id: GO:0014911
      label: positive regulation of smooth muscle cell migration
    evidence_type: IDA
    original_reference_id: PMID:9409235
    review:
      summary: >-
        positive regulation of smooth muscle cell migration is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:9409235
          supporting_text: Platelet-derived growth factor beta-receptors can both
            promote and inhibit chemotaxis in human vascular smooth muscle cells.
      reason: >-
        Accept. smooth muscle cell migration is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0050921
      label: positive regulation of chemotaxis
    evidence_type: IDA
    original_reference_id: PMID:9409235
    review:
      summary: >-
        positive regulation of chemotaxis is supported as a PDGF-B/PDGFR-dependent cell-type
        or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:9409235
          supporting_text: Platelet-derived growth factor beta-receptors can both
            promote and inhibit chemotaxis in human vascular smooth muscle cells.
      reason: >-
        Accept. positive regulation of chemotaxis is a supported biological process downstream
        of PDGF-B-containing ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: IPI
    original_reference_id: PMID:2536956
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2536956
          supporting_text: Isolation of a novel receptor cDNA establishes the existence
            of two PDGF receptor genes.
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:2536956
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2536956
          supporting_text: Isolation of a novel receptor cDNA establishes the existence
            of two PDGF receptor genes.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: IDA
    original_reference_id: PMID:2836953
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2836953
          supporting_text: A common PDGF receptor is activated by homodimeric A and B
            forms of PDGF.
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
  - term:
      id: GO:0008284
      label: positive regulation of cell population proliferation
    evidence_type: IDA
    original_reference_id: PMID:2836953
    review:
      summary: >-
        positive regulation of cell population proliferation is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2836953
          supporting_text: A common PDGF receptor is activated by homodimeric A and B
            forms of PDGF.
      reason: >-
        Broad positive regulation of cell population proliferation is a downstream growth-factor
        outcome. Keep it as supported but non-core; more specific cell-type proliferation
        terms and the core ligand/receptor-binding function are more informative.
  - term:
      id: GO:0008284
      label: positive regulation of cell population proliferation
    evidence_type: IDA
    original_reference_id: PMID:7073684
    review:
      summary: >-
        positive regulation of cell population proliferation is supported or plausible for
        PDGFB but represents a context-specific localization, storage, processing, or downstream
        biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:7073684
          supporting_text: 'Platelet-derived growth factor: identification of constituent
            polypeptide chains.'
      reason: >-
        Broad positive regulation of cell population proliferation is a downstream growth-factor
        outcome. Keep it as supported but non-core; more specific cell-type proliferation
        terms and the core ligand/receptor-binding function are more informative.
  - term:
      id: GO:0009611
      label: response to wounding
    evidence_type: IDA
    original_reference_id: PMID:2538439
    review:
      summary: >-
        response to wounding is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2538439
          supporting_text: Collagen-induced binding to human platelets of
            platelet-derived growth factor leading to inhibition of P43 and P20
            phosphorylation.
      reason: >-
        Response to wounding is a supported physiological context for platelet-derived PDGF-BB
        release and signaling, but is non-core relative to the receptor-ligand function.
  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IDA
    original_reference_id: PMID:2836953
    review:
      summary: >-
        cell surface is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2836953
          supporting_text: A common PDGF receptor is activated by homodimeric A and B
            forms of PDGF.
      reason: >-
        Cell surface association is compatible with PDGF receptor binding and heparan-sulfate
        retention, but extracellular region/matrix are more precise mature ligand locations.
  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IDA
    original_reference_id: PMID:291037
    review:
      summary: >-
        cell surface is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:291037
          supporting_text: 'Platelet-derived growth factor: purification and partial characterization.'
      reason: >-
        Cell surface association is compatible with PDGF receptor binding and heparan-sulfate
        retention, but extracellular region/matrix are more precise mature ligand locations.
  - term:
      id: GO:0010512
      label: negative regulation of phosphatidylinositol biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:2538439
    review:
      summary: >-
        negative regulation of phosphatidylinositol biosynthetic process is supported or plausible
        for PDGFB but represents a context-specific localization, storage, processing, or
        downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2538439
          supporting_text: Collagen-induced binding to human platelets of
            platelet-derived growth factor leading to inhibition of P43 and P20
            phosphorylation.
      reason: >-
        The platelet phosphoinositide effect is a specific downstream platelet-feedback context,
        not a core PDGFB function.
  - term:
      id: GO:0010544
      label: negative regulation of platelet activation
    evidence_type: IDA
    original_reference_id: PMID:2538439
    review:
      summary: >-
        negative regulation of platelet activation is supported or plausible for PDGFB but
        represents a context-specific localization, storage, processing, or downstream biological
        outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:2538439
          supporting_text: Collagen-induced binding to human platelets of
            platelet-derived growth factor leading to inhibition of P43 and P20
            phosphorylation.
      reason: >-
        Negative regulation of platelet activation is a specific platelet-feedback context,
        not the core PDGFB ligand function.
  - term:
      id: GO:0042803
      label: protein homodimerization activity
    evidence_type: IDA
    original_reference_id: PMID:2836953
    review:
      summary: >-
        protein homodimerization activity is supported for PDGFB in the context of its mature
        extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2836953
          supporting_text: A common PDGF receptor is activated by homodimeric A and B
            forms of PDGF.
      reason: >-
        Protein homodimerization activity directly captures PDGF-BB homodimer formation, a
        core biochemical property of the mature ligand.
  - term:
      id: GO:0046982
      label: protein heterodimerization activity
    evidence_type: IPI
    original_reference_id: PMID:7073684
    review:
      summary: >-
        protein heterodimerization activity is supported for PDGFB in the context of its mature
        extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:7073684
          supporting_text: 'Platelet-derived growth factor: identification of constituent
            polypeptide chains.'
      reason: >-
        Protein heterodimerization activity captures PDGF-AB formation between PDGFA and PDGFB,
        a recognized active PDGF ligand dimer.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:2439522
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2439522
          supporting_text: PDGF induces c-myc mRNA expression in MG-63 human
            osteosarcoma cells but does not stimulate cell replication.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0048008
      label: platelet-derived growth factor receptor signaling pathway
    evidence_type: IDA
    original_reference_id: PMID:2836953
    review:
      summary: >-
        platelet-derived growth factor receptor signaling pathway is supported for PDGFB in
        the context of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2836953
          supporting_text: A common PDGF receptor is activated by homodimeric A and B
            forms of PDGF.
      reason: >-
        PDGF receptor signaling pathway is the core biological process initiated by PDGFB
        ligand binding to PDGFRA/PDGFRB receptor complexes.
  - term:
      id: GO:0048146
      label: positive regulation of fibroblast proliferation
    evidence_type: IDA
    original_reference_id: PMID:2439522
    review:
      summary: >-
        positive regulation of fibroblast proliferation is supported as a PDGF-B/PDGFR-dependent
        cell-type or chemotaxis process.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:2439522
          supporting_text: PDGF induces c-myc mRNA expression in MG-63 human
            osteosarcoma cells but does not stimulate cell replication.
      reason: >-
        Accept. fibroblast proliferation is a supported biological process downstream of PDGF-B-containing
        ligand signaling and is sufficiently specific to retain for PDGFB.
  - term:
      id: GO:0048407
      label: platelet-derived growth factor binding
    evidence_type: IPI
    original_reference_id: PMID:7073684
    review:
      summary: >-
        platelet-derived growth factor binding is supported for PDGFB in the context of its
        mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:7073684
          supporting_text: 'Platelet-derived growth factor: identification of constituent
            polypeptide chains.'
      reason: >-
        Platelet-derived growth factor binding is consistent with PDGFB participation in PDGF
        dimer formation and PDGF ligand complexes, although the more informative core terms
        are PDGF receptor binding and dimerization.
  - term:
      id: GO:0001938
      label: positive regulation of endothelial cell proliferation
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        positive regulation of endothelial cell proliferation is retained as a non-core, context-specific
        PDGFB annotation pending more specific upstream curation.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        The annotation is connected to PDGFB biology, but the core function is extracellular
        PDGF receptor ligand activity and PDGF receptor signaling.
  - term:
      id: GO:0009986
      label: cell surface
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        cell surface is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        Cell surface association is compatible with PDGF receptor binding and heparan-sulfate
        retention, but extracellular region/matrix are more precise mature ligand locations.
  - term:
      id: GO:0043536
      label: positive regulation of blood vessel endothelial cell migration
    evidence_type: IDA
    original_reference_id: PMID:9685360
    review:
      summary: >-
        positive regulation of blood vessel endothelial cell migration is retained as a non-core,
        context-specific PDGFB annotation pending more specific upstream curation.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:9685360
          supporting_text: Apolipoprotein E inhibits platelet-derived growth
            factor-induced vascular smooth muscle cell migration and proliferation by
            suppressing signal transduction and preventing cell entry to G1 phase.
      reason: >-
        The annotation is connected to PDGFB biology, but the core function is extracellular
        PDGF receptor ligand activity and PDGF receptor signaling.
  - term:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    evidence_type: NAS
    original_reference_id: PMID:1661670
    review:
      summary: >-
        platelet-derived growth factor receptor binding is supported for PDGFB in the context
        of its mature extracellular PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:1661670
          supporting_text: Two PDGF-B chain residues, arginine 27 and isoleucine 30,
            mediate receptor binding and activation.
      reason: >-
        PDGF receptor binding is a defining molecular function for PDGF-B-containing ligands.
        PDGF-BB and PDGF-AB bind PDGFRA/PDGFRB receptor dimers extracellularly and initiate
        PDGF receptor signaling.
  - term:
      id: GO:0005576
      label: extracellular region
    evidence_type: NAS
    original_reference_id: PMID:1661670
    review:
      summary: >-
        extracellular region is supported for PDGFB in the context of its mature extracellular
        PDGF ligand function.
      action: ACCEPT
      supported_by:
        - reference_id: PMID:1661670
          supporting_text: Two PDGF-B chain residues, arginine 27 and isoleucine 30,
            mediate receptor binding and activation.
      reason: >-
        Extracellular region is strongly supported for mature PDGFB, which is secreted and
        acts as an extracellular receptor ligand.
  - term:
      id: GO:0009611
      label: response to wounding
    evidence_type: NAS
    original_reference_id: PMID:1661670
    review:
      summary: >-
        response to wounding is supported or plausible for PDGFB but represents a context-specific
        localization, storage, processing, or downstream biological outcome.
      action: KEEP_AS_NON_CORE
      supported_by:
        - reference_id: PMID:1661670
          supporting_text: Two PDGF-B chain residues, arginine 27 and isoleucine 30,
            mediate receptor binding and activation.
      reason: >-
        Response to wounding is a supported physiological context for platelet-derived PDGF-BB
        release and signaling, but is non-core relative to the receptor-ligand function.
references:
  - id: GO_REF:0000002
    title: Gene Ontology annotation through association of InterPro records with GO
      terms
    findings: []
  - id: GO_REF:0000024
    title: Manual transfer of experimentally-verified manual GO annotation data to
      orthologs by curator judgment of sequence similarity
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings: []
  - id: GO_REF:0000043
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
    findings: []
  - id: GO_REF:0000044
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
      vocabulary mapping, accompanied by conservative changes to GO terms applied by
      UniProt
    findings: []
  - id: GO_REF:0000108
    title: Automatic assignment of GO terms using logical inference, based on on
      inter-ontology links
    findings: []
  - id: GO_REF:0000117
    title: Electronic Gene Ontology annotations created by ARBA machine learning models
    findings: []
  - id: GO_REF:0000120
    title: Combined Automated Annotation using Multiple IEA Methods
    findings: []
  - id: PMID:10644978
    title: PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
    findings: []
  - id: PMID:10734101
    title: Platelet-derived growth factor receptor beta regulates migration and DNA
      synthesis in metanephric mesenchymal cells.
    findings: []
  - id: PMID:10806482
    title: PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor.
    findings: []
  - id: PMID:11264163
    title: Basis of hematopoietic defects in platelet-derived growth factor (PDGF)-B and
      PDGF beta-receptor null mice.
    findings: []
  - id: PMID:11297552
    title: Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds
      to PDGF alpha and beta receptor.
    findings: []
  - id: PMID:11788434
    title: Effect of platelet-derived growth factor isoforms in rat metanephric
      mesenchymal cells.
    findings: []
  - id: PMID:12070119
    title: Adipocyte-derived plasma protein adiponectin acts as a platelet-derived
      growth factor-BB-binding protein and regulates growth factor-induced common
      postreceptor signal in vascular smooth muscle cell.
    findings: []
  - id: PMID:1396586
    title: Crystal structure of human platelet-derived growth factor BB.
    findings: []
  - id: PMID:16014047
    title: Hypoxia regulates PDGF-B interactions between glomerular capillary
      endothelial and mesangial cells.
    findings: []
  - id: PMID:16477012
    title: Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta
      in phenotypic modulation of human aortic smooth muscle cells.
    findings: []
  - id: PMID:16530387
    title: c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA
      synthesis in mesangial cells.
    findings: []
  - id: PMID:1661670
    title: Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor
      binding and activation.
    findings: []
  - id: PMID:17324121
    title: 'Growth factor regulation of hyaluronan synthesis and degradation in human dermal
      fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB.'
    findings: []
  - id: PMID:17942966
    title: Mitogenic signaling via platelet-derived growth factor beta in metanephric
      mesenchymal cells.
    findings: []
  - id: PMID:17981115
    title: Anti-PlGF inhibits growth of VEGF(R)-inhibitor-resistant tumors without
      affecting healthy vessels.
    findings: []
  - id: PMID:17991872
    title: 'TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different
      cell types: involvement of Src and PLC.'
    findings: []
  - id: PMID:19019919
    title: PDGF receptor-{beta} modulates metanephric mesenchyme chemotaxis induced by
      PDGF AA.
    findings: []
  - id: PMID:19088079
    title: Induction of microRNA-221 by platelet-derived growth factor signaling is
      critical for modulation of vascular smooth muscle phenotype.
    findings: []
  - id: PMID:19126672
    title: Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and
      random migration of fibroblasts.
    findings: []
  - id: PMID:20534510
    title: Structures of a platelet-derived growth factor/propeptide complex and a
      platelet-derived growth factor/receptor complex.
    findings: []
  - id: PMID:21245381
    title: Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential
      for growth factor-dependent migration of glioma and endothelial cells.
    findings: []
  - id: PMID:21321938
    title: Interleukin-18/WNT1-inducible signaling pathway protein-1 signaling mediates
      human saphenous vein smooth muscle cell proliferation.
    findings: []
  - id: PMID:23139410
    title: Unique motifs and hydrophobic interactions shape the binding of modified DNA
      ligands to protein targets.
    findings: []
  - id: PMID:23554459
    title: MicroRNA-638 is highly expressed in human vascular smooth muscle cells and
      inhibits PDGF-BB-induced cell proliferation and migration through targeting orphan
      nuclear receptor NOR1.
    findings: []
  - id: PMID:23979707
    title: SILAC-based proteomics of human primary endothelial cell morphogenesis
      unveils tumor angiogenic markers.
    findings: []
  - id: PMID:24008408
    title: CAP37 activation of PKC promotes human corneal epithelial cell chemotaxis.
    findings: []
  - id: PMID:2439522
    title: PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma cells but does
      not stimulate cell replication.
    findings: []
  - id: PMID:25089138
    title: miR-18a-5p MicroRNA Increases Vascular Smooth Muscle Cell Differentiation by
      Downregulating Syndecan4.
    findings: []
  - id: PMID:2536956
    title: Isolation of a novel receptor cDNA establishes the existence of two PDGF
      receptor genes.
    findings: []
  - id: PMID:2538439
    title: Collagen-induced binding to human platelets of platelet-derived growth factor
      leading to inhibition of P43 and P20 phosphorylation.
    findings: []
  - id: PMID:26493107
    title: miRNA-34a reduces neointima formation through inhibiting smooth muscle cell
      proliferation and migration.
    findings: []
  - id: PMID:2836953
    title: A common PDGF receptor is activated by homodimeric A and B forms of PDGF.
    findings: []
  - id: PMID:291037
    title: 'Platelet-derived growth factor: purification and partial characterization.'
    findings: []
  - id: PMID:32296183
    title: A reference map of the human binary protein interactome.
    findings: []
  - id: PMID:7073684
    title: 'Platelet-derived growth factor: identification of constituent polypeptide chains.'
    findings: []
  - id: PMID:7679113
    title: Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to
      alpha and beta PDGF receptor.
    findings: []
  - id: PMID:8900172
    title: Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for
      the isoforms of platelet-derived growth factor (AA, BB, and AB).
    findings: []
  - id: PMID:9409235
    title: Platelet-derived growth factor beta-receptors can both promote and inhibit
      chemotaxis in human vascular smooth muscle cells.
    findings: []
  - id: PMID:9685360
    title: Apolipoprotein E inhibits platelet-derived growth factor-induced vascular
      smooth muscle cell migration and proliferation by suppressing signal transduction
      and preventing cell entry to G1 phase.
    findings: []
  - id: Reactome:R-HSA-1524182
    title: Activated PLC gamma dissociates from the PDGF receptor
    findings: []
  - id: Reactome:R-HSA-1524186
    title: Phosphorylation of PLCgamma by PDGFR
    findings: []
  - id: Reactome:R-HSA-186765
    title: PLC-gamma binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-186773
    title: PDGF dimer binds two receptors simultaneously
    findings: []
  - id: Reactome:R-HSA-186778
    title: SHP2 binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-186780
    title: PI3-kinase binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-186786
    title: Autophosphorylation of PDGF beta receptors
    findings: []
  - id: Reactome:R-HSA-186798
    title: GAP binds to PDGF-beta receptors only
    findings: []
  - id: Reactome:R-HSA-186800
    title: PI3K catalyses the phosphorylation of PIP2 to PIP3
    findings: []
  - id: Reactome:R-HSA-186819
    title: SH2 domain of Src binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-186826
    title: GRB2:SOS1 complex binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-186834
    title: SOS-mediated nucleotide exchange on RAS (PDGF receptor:GRB2:SOS)
    findings: []
  - id: Reactome:R-HSA-2316434
    title: PI3K phosphorylates PIP2 to PIP3
    findings: []
  - id: Reactome:R-HSA-2396337
    title: HSPG2 binds FGF2(10-155), Fibronectn matrix, Transthyretin tetramer, PDGFA
      homodimer, PDGFB homodimer
    findings: []
  - id: Reactome:R-HSA-2400009
    title: PI3K inhibitors block PI3K catalytic activity
    findings: []
  - id: Reactome:R-HSA-380780
    title: Activation of Src
    findings: []
  - id: Reactome:R-HSA-380782
    title: STAT binds to the active receptor
    findings: []
  - id: Reactome:R-HSA-382052
    title: p130Cas and C3G bind PDGFR bound Crk
    findings: []
  - id: Reactome:R-HSA-382053
    title: Translocation of PDGF from ER to Golgi
    findings: []
  - id: Reactome:R-HSA-382054
    title: PDGF binds to extracellular matrix proteins
    findings: []
  - id: Reactome:R-HSA-382055
    title: Grb7 binds to the active PDGF receptor
    findings: []
  - id: Reactome:R-HSA-382056
    title: Crk binds to the active PDGF receptor
    findings: []
  - id: Reactome:R-HSA-382058
    title: Nck binds to the active PDGF receptor
    findings: []
  - id: Reactome:R-HSA-389083
    title: Autophosphorylation of PDGF alpha receptors
    findings: []
  - id: Reactome:R-HSA-389086
    title: Autophosphorylation of PDGF alpha/beta receptors
    findings: []
  - id: Reactome:R-HSA-481007
    title: Exocytosis of platelet alpha granule contents
    findings: []
  - id: Reactome:R-HSA-5672965
    title: RAS GEFs promote RAS nucleotide exchange
    findings: []
  - id: Reactome:R-HSA-8864036
    title: PTPN12 dephosphorylates PDGFRB at Y1021
    findings: []
  - id: Reactome:R-HSA-8865275
    title: PDGF-BB clevage by Furin
    findings: []
  - id: Reactome:R-HSA-8865276
    title: PDGF-AB clevage by Furin
    findings: []
  - id: Reactome:R-HSA-9674093
    title: PDGFRs bind type I TKI
    findings: []
  - id: file:human/PDGFB/PDGFB-deep-research-falcon.md
    title: Falcon deep research report on PDGFB
    findings:
      - statement: >-
          PDGFB is a secreted PDGF ligand whose core GO-relevant evidence is receptor binding,
          growth factor activity, dimerization, extracellular localization, and ligand-attributable
          vascular/mural-cell processes.
        supporting_text: >-
          This report summarizes **GO-relevant evidence for PDGFB as a secreted PDGF ligand**:
          disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), **direct binding/activation
          of PDGF receptor dimers (PDGFRA/PDGFRB)**, secretion/localization (extracellular
          space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only
          where explicitly stated), and **ligand-attributable biological processes** (pericyte
          recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing
          evidence). It **excludes** receptor **intrinsic kinase activity** (peptidyl-tyrosine
          phosphorylation), downstream pathway terms (PI3K–AKT, ERK/MAPK, ROS/NADPH oxidase),
          and broad transcriptional/miRNA effects unless strictly necessary to interpret ligand
          localization or binding (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily
          pages 5-7).
      - statement: >-
          PDGFB should not be annotated with receptor tyrosine kinase activity or generic
          downstream PI3K/AKT, ERK/MAPK, ROS, or transcriptional outputs as core functions.
        supporting_text: >-
          Do **not** annotate PDGFB with receptor enzymatic activities (e.g., **protein tyrosine
          kinase activity**, **peptidyl-tyrosine phosphorylation**) or generic downstream
          pathways (PI3K/AKT, ERK/MAPK, ROS) based solely on PDGFR signaling descriptions;
          these belong to PDGF receptors or downstream effectors, not the PDGFB ligand itself
          (fredriksson2004thepdgffamily pages 5-7, strell2024functionalandclinical pages 3-5).
  - id: file:human/PDGFB/PDGFB-uniprot.txt
    title: UniProtKB P01127 record for PDGFB
    findings: []
core_functions:
  - molecular_function:
      id: GO:0005161
      label: platelet-derived growth factor receptor binding
    description: >-
      PDGFB is the platelet-derived growth factor B-chain ligand subunit. After secretory-pathway
      processing and disulfide-linked dimer formation, PDGF-B-containing ligands act extracellularly
      as receptor ligands/growth factors for PDGFRA- and PDGFRB-containing receptor dimers.
      This function underlies PDGF receptor signaling, paracrine mural-cell/pericyte recruitment,
      angiogenesis/blood vessel morphogenesis, chemotaxis, and specific smooth muscle/mesenchymal
      proliferation or migration responses. Receptor autophosphorylation and downstream PI3K,
      ERK/MAPK, ROS, and transcriptional outputs are consequences in responding cells rather
      than direct PDGFB molecular functions.
    directly_involved_in:
      - id: GO:0048008
        label: platelet-derived growth factor receptor signaling pathway
      - id: GO:0038001
        label: paracrine signaling
      - id: GO:0001525
        label: angiogenesis
      - id: GO:0060326
        label: cell chemotaxis
    locations:
      - id: GO:0005576
        label: extracellular region
      - id: GO:0031012
        label: extracellular matrix
    supported_by:
      - reference_id: file:human/PDGFB/PDGFB-deep-research-falcon.md
        supporting_text: >-
          This report summarizes **GO-relevant evidence for PDGFB as a secreted PDGF ligand**:
          disulfide-linked dimer formation (PDGF‑BB; PDGF‑AB), **direct binding/activation
          of PDGF receptor dimers (PDGFRA/PDGFRB)**, secretion/localization (extracellular
          space; ER/Golgi processing; ECM/HS retention), platelet α‑granule localization (only
          where explicitly stated), and **ligand-attributable biological processes** (pericyte
          recruitment/coverage; angiogenesis/blood vessel morphogenesis; limited wound-healing
          evidence). It **excludes** receptor **intrinsic kinase activity** (peptidyl-tyrosine
          phosphorylation), downstream pathway terms (PI3K–AKT, ERK/MAPK, ROS/NADPH oxidase),
          and broad transcriptional/miRNA effects unless strictly necessary to interpret ligand
          localization or binding (ostman1992pdgfaaandpdgfbb pages 1-2, fredriksson2004thepdgffamily
          pages 5-7).
      - reference_id: file:human/PDGFB/PDGFB-deep-research-falcon.md
        supporting_text: >-
          PDGF‑AA/AB/BB are described as **secreted in active form**, supporting extracellular
          localization of mature PDGF‑B-containing ligands (duran2018molecularregulationof
          pages 9-11).
proposed_new_terms: []
suggested_questions: []
suggested_experiments: []