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.
| 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):** βPDGF receptor bindingβ and βgrowth factor activity,β 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. Proposed replacements: platelet-derived growth factor receptor signaling pathway |
| 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. Proposed replacements: platelet-derived growth factor 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. Proposed replacements: platelet-derived growth factor 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. |
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