The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The research target FGF10 (UniProt accession O15520) encodes fibroblast growth factor 10, also known as keratinocyte growth factor 2 (KGF-2), in humans (Homo sapiens). This protein belongs to the heparin-binding growth factors family and is specifically classified within the FGF7 subfamily, which also includes FGF3, FGF7, and FGF22 (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2024decodingfgffgfrsignaling pages 5-7). The human FGF10 gene maps to chromosome 5p12-p13, spans approximately 89 kb, and contains three coding exons (bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2025pathologyandtherapeutic pages 8-10). This confirms that the research is focused on the correct human protein as specified.
FGF10 is synthesized as a 208-amino-acid precursor protein with an approximate molecular weight of 23.4 kDa (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2025pathologyandtherapeutic pages 8-10). The protein architecture consists of an N-terminal signal peptide spanning residues 1-37, which directs the protein into the endoplasmic reticulum-Golgi secretory pathway, and a mature FGF domain comprising residues 38-208 (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5). Two glycosylation sites have been identified at residues 51 and 196 (bzdega2022phenotypicspectrumof pages 3-5).
Structurally, the mature FGF10 protein adopts the characteristic FGF β-trefoil fold composed of 12 antiparallel β-strands (edirisinghe2024decodingfgffgfrsignaling pages 7-8). Compared to FGF1 and FGF2, FGF10 exhibits a longer β1 strand and less-organized β10 and β11 strands. Additionally, the first five N-terminal residues form a short helix termed gN, which is linked to β1 by a short loop, making the receptor-bound N-terminus more structurally defined (edirisinghe2024decodingfgffgfrsignaling pages 7-8). These structural features place FGF10 within the Fibroblast_GF_fam domain (IPR002209) and IL1/FGF structural superfamily (IPR008996), consistent with the UniProt annotation provided.
FGF10 functions as a secreted paracrine signaling molecule rather than as an enzyme or transporter (bzdega2022phenotypicspectrumof pages 1-3, edirisinghe2024decodingfgffgfrsignaling pages 7-8). Its primary molecular role is to transmit extracellular growth and developmental signals from mesenchymal or stromal cells to adjacent epithelial cells expressing cognate fibroblast growth factor receptors (bzdega2022phenotypicspectrumof pages 3-5, baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8). The N-terminal signal peptide directs FGF10 through the classical ER-Golgi secretory pathway, resulting in protein secretion into the extracellular space where it functions (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5).
FGF10 is predominantly produced by mesenchymal cells and acts locally on neighboring epithelial cells in a paracrine manner (baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8, ornitz2022newdevelopmentsin pages 59-60, yin2020fgf9andfgf10 pages 8-9). This spatially organized signaling is critical for coordinating epithelial-mesenchymal interactions during organogenesis and tissue repair. The protein's activity is physiologically restricted to the local microenvironment through binding to cell-surface heparan sulfate proteoglycans, which stabilize the molecule near its source and prevent long-range diffusion (chen2025fgfbaseddrugdiscovery pages 2-4, baran2025fibroblastgrowthfactors pages 7-8).
FGF10 signals predominantly through FGFR2b, the epithelial IgIIIb splice isoform of fibroblast growth factor receptor 2 (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2024decodingfgffgfrsignaling pages 5-7). This receptor specificity is a defining characteristic of the FGF7 subfamily, whose members signal exclusively through the "b" isoforms of FGFRs rather than the mesenchymal "c" isoforms (edirisinghe2024decodingfgffgfrsignaling pages 5-7). The interaction between FGF10 and FGFR2b involves an extensive network of contacts with the receptor's D3 domain. Specific FGF10 regions involved in receptor binding include the βB′ strand, βB′-βC loop, N-terminus, β1 and β4 strands, and β7-β8 loop (edirisinghe2024decodingfgffgfrsignaling pages 7-8). Mutagenesis studies have identified Asp76, Arg78, and Thr114 as critical residues for FGF10-mediated cell proliferation (edirisinghe2024decodingfgffgfrsignaling pages 7-8).
While FGFR2b is the principal and best-characterized receptor, FGF10 can also bind to FGFR1b, the epithelial IgIIIb splice isoform of FGFR1 (ferguson2021fibroblastgrowthfactor pages 2-3, francavilla2022fibroblastgrowthfactor pages 3-4). This broader receptor usage within the "b" isoform family allows FGF10 to signal in multiple epithelial contexts. However, FGFR2b remains the dominant developmental receptor and the most extensively studied (baran2025fibroblastgrowthfactors pages 5-7, edirisinghe2024decodingfgffgfrsignaling pages 8-10). There is no substantial evidence that FGF10 productively binds FGFR1c, FGFR2c, FGFR3, or FGFR4 under physiological conditions (bzdega2022phenotypicspectrumof pages 3-5).
Heparan sulfate proteoglycans (HSPGs) function as essential cofactors for FGF10 signaling (bzdega2022phenotypicspectrumof pages 3-5, francavilla2022fibroblastgrowthfactor pages 3-4, chen2025fgfbaseddrugdiscovery pages 2-4). These include membrane-anchored syndecans and glypicans, as well as extracellular matrix perlecans. HSPGs contain heparan sulfate (HS) chains with sulfated regions that interact with positively charged residues in FGF10's heparan-sulfate-binding site (chen2025fgfbaseddrugdiscovery pages 2-4, farooq2021theroleof pages 5-6). The HS-FGF10-FGFR interaction serves multiple critical functions: it stabilizes the ligand-receptor complex, promotes productive FGFR dimerization and activation, and retains FGF10 within the pericellular matrix near its site of production, thereby restricting signaling to nearby cells (bzdega2022phenotypicspectrumof pages 3-5, francavilla2022fibroblastgrowthfactor pages 3-4, chen2025fgfbaseddrugdiscovery pages 2-4, chen2022rolesofthe pages 3-4, edirisinghe2024decodingfgffgfrsignaling pages 5-7, ferguson2021fibroblastgrowthfactor pages 3-5).
The canonical FGF signaling mechanism requires formation of a ternary FGF-FGFR-HSPG complex at the cell surface, which enables receptor dimerization and trans-autophosphorylation of intracellular tyrosine residues (bzdega2022phenotypicspectrumof pages 3-5, bzdega2022phenotypicspectrumof pages 1-3, farooq2021theroleof pages 5-6, chen2022rolesofthe pages 3-4).
FGF10 binding to FGFR2b (or FGFR1b) initiates multiple intracellular signaling cascades that regulate cellular proliferation, survival, migration, differentiation, and metabolism.
The RAS-MAPK pathway is a major downstream effector of FGF10-FGFR2b signaling. Following receptor autophosphorylation, the adaptor protein FRS2α is recruited and phosphorylated, which in turn recruits GRB2 and SOS to activate the RAS-RAF-MEK-ERK cascade (francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, liu2021fgfmechanismof pages 4-5, liu2026fgffamilyin pages 3-4). In the developing lung epithelium during the pseudoglandular stage, FGF10-FGFR2b signaling preferentially activates ERK phosphorylation and promotes epithelial proliferation and bud outgrowth (yin2020fgf9andfgf10 pages 9-9, yin2020fgf9andfgf10 pages 1-2, yin2020fgf9andfgf10 pages 7-8). This MAPK/ERK activation is the dominant experimentally demonstrated output in lung branching morphogenesis, though pathway weighting can vary depending on tissue and developmental context (yin2020fgf9andfgf10 pages 9-9).
FGF10-FGFR2b activation can directly recruit the PI3K p85 regulatory subunit to phosphorylated FGFR2 tyrosine residue Y734 (ferguson2021fibroblastgrowthfactor pages 3-5, ferguson2021fibroblastgrowthfactor pages 5-7). Additionally, FRS2α recruits GAB1, which activates the PI3K-AKT pathway (francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, liu2026fgffamilyin pages 3-4). AKT activation leads to downstream effects including mTOR complex 1 activation, phosphorylation of FOXO1 transcription factor, and regulation of survival through inactivation of pro-apoptotic proteins such as Caspase 9, BAD, and BAX (francavilla2022fibroblastgrowthfactor pages 2-3, liu2026fgffamilyin pages 3-4, ferguson2021fibroblastgrowthfactor pages 5-7). While both ERK and AKT can be activated by FGF10, the relative strength varies by context, with ERK activation typically more prominent in embryonic lung development (yin2020fgf9andfgf10 pages 9-9).
Activated FGFR can recruit phospholipase C-gamma (PLCγ), which hydrolyzes PIP2 into IP3 and DAG, causing intracellular calcium release and protein kinase C (PKC) activation (bzdega2022phenotypicspectrumof pages 3-5, francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, liu2026fgffamilyin pages 3-4, ferguson2021fibroblastgrowthfactor pages 5-7). Additionally, FGFR signaling can activate STAT proteins (STAT1, STAT3, STAT5), leading to their nuclear translocation and transcriptional regulation (francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, liu2021fgfmechanismof pages 4-5, ferguson2021fibroblastgrowthfactor pages 5-7, wang2021fgffgfrsignalingin pages 2-4). These pathways collectively regulate diverse cellular responses including gene expression, proliferation, migration, and differentiation.
FGF10 is a classically secreted protein that functions in the extracellular space and pericellular matrix (edirisinghe2024decodingfgffgfrsignaling pages 7-8, baran2025fibroblastgrowthfactors pages 7-8, bzdega2022phenotypicspectrumof pages 3-5). The N-terminal signal peptide (residues 1-37) directs nascent FGF10 into the endoplasmic reticulum, where it enters the secretory pathway through the ER-Golgi system (edirisinghe2024decodingfgffgfrsignaling pages 7-8). Following secretion, FGF10 does not act systemically but is retained locally through interactions with heparan sulfate proteoglycans in the extracellular matrix and on cell surfaces (chen2025fgfbaseddrugdiscovery pages 2-4, baran2025fibroblastgrowthfactors pages 7-8).
The primary site of FGF10 function is outside the producing cell, at the HS-rich surface and matrix surrounding target cells (edirisinghe2024decodingfgffgfrsignaling pages 7-8, baran2025fibroblastgrowthfactors pages 7-8). This represents classic mesenchyme-to-epithelium paracrine signaling: FGF10 is typically produced by mesenchymal or stromal fibroblasts and acts on adjacent epithelial cells expressing FGFR2b (baran2025fibroblastgrowthfactors pages 5-7, bzdega2022phenotypicspectrumof pages 3-5, ornitz2022newdevelopmentsin pages 59-60, yin2020fgf9andfgf10 pages 8-9). In developing lung, for example, FGF10 is expressed in the submesothelial mesenchyme surrounding distal lung buds and signals to epithelial FGFR2b-positive progenitor cells (baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8, yin2020fgf9andfgf10 pages 8-9).
The most comprehensively studied and best-characterized function of FGF10 is its essential role in lung development, particularly in directing branching morphogenesis of the respiratory epithelium.
FGF10 is absolutely required for lung formation. Genetic deletion of Fgf10 or its receptor Fgfr2b in mice results in lung agenesis, with lung buds failing to develop beyond initial formation (sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 7-8, yin2020fgf9andfgf10 pages 1-2). This demonstrates that FGF10-FGFR2b signaling is not merely contributory but essential for lung organogenesis. When FGF10 or FGFR2b is conditionally disrupted after initial bud formation, lung growth arrests, branching is severely impaired, and epithelial cell death increases (sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 7-8, yin2020fgf9andfgf10 pages 1-2).
During the pseudoglandular stage of lung development, mesenchymal FGF10 signals to epithelial FGFR2b to coordinate multiple aspects of airway development (sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 5-7, yin2020fgf9andfgf10 pages 1-2). FGF10 promotes epithelial chemotaxis toward the mesenchymal signal, helping direct the growth and positioning of distal buds (sedighi2021theroleof pages 20-23). It stimulates epithelial proliferation and outgrowth, drives branching morphogenesis, and regulates epithelial cell survival (baran2025fibroblastgrowthfactors pages 7-8, baran2025fibroblastgrowthfactors pages 5-7, yin2020fgf9andfgf10 pages 1-2, yin2020fgf9andfgf10 pages 7-8).
FGF10-FGFR2b signaling activates the WNT/β-catenin pathway, which increases expression of BMP4 and SOX9 in distal epithelial progenitors while activating SOX2 in proximal regions (baran2025fibroblastgrowthfactors pages 5-7). This establishes proximal-distal patterning: FGF10 helps maintain distal SOX9+/ID2+ epithelial progenitors in an undifferentiated state, supporting continued branching and preserving the progenitor pool, while more proximal cells express SOX2 and differentiate toward bronchial epithelium (baran2025fibroblastgrowthfactors pages 7-8, sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 5-7).
Importantly, FGF10 activity must be precisely regulated. Transient inhibition of FGF10 signaling during embryogenesis causes lung growth arrest and severely impaired branching (baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8). Conversely, prolonged or excessive FGF10 activity paradoxically inhibits normal branching and drives distal epithelial cells toward cyst-like proliferation and differentiation (baran2025fibroblastgrowthfactors pages 7-8). Spatial restriction of FGF10 activity is achieved through negative feedback by Sonic Hedgehog (SHH) signaling from the distal mesenchyme (baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8).
Beyond airway branching, FGF10-FGFR2b signaling contributes to alveolar lineage formation, including development of alveolar myofibroblasts, secondary septa, and differentiation toward alveolar epithelial type II (AT2) cells (sedighi2021theroleof pages 20-23). FGF10 continues to function postnatally in alveolar development, epithelial regeneration, and protection from lung injury (sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 18-19).
Beyond the lung, FGF10 plays critical roles in the development of multiple organs through similar mesenchymal-to-epithelial paracrine signaling mechanisms.
FGF10 is essential for lacrimal and salivary gland development. High Fgf10 expression occurs in neural crest-derived mesenchyme of the forming salivary gland and in mesenchyme surrounding the developing lacrimal gland epithelial bud in mice (bzdega2022phenotypicspectrumof pages 3-5). Human genetic evidence strongly supports this developmental role: heterozygous pathogenic variants in FGF10 cause aplasia of the lacrimal and salivary glands (ALSG) and contribute to lacrimo-auriculo-dento-digital syndrome (LADD), a multisystem developmental disorder (edirisinghe2025pathologyandtherapeutic pages 8-10, edirisinghe2024decodingfgffgfrsignaling pages 7-8, sedighi2021theroleof pages 20-23). These syndromes involve malformations of multiple organs including ears, teeth, fingers, kidneys, respiratory system, and genitals, demonstrating FGF10's broad developmental importance and dosage sensitivity (sedighi2021theroleof pages 20-23).
In the gastrointestinal tract, FGF10 is expressed in mesenchyme and signals to adjacent epithelium (ornitz2022newdevelopmentsin pages 59-60). Loss of Fgf10 or Fgfr2b disrupts development of the stomach, duodenum, cecum, and colon, and can produce duodenal or colonic atresia (ornitz2022newdevelopmentsin pages 59-60). In the colon, Fgfr2b deficiency is associated with increased epithelial apoptosis, abnormal epithelial architecture, and discontinuity of the basal lamina, demonstrating FGF10-FGFR2b's role in maintaining epithelial organization and survival (ornitz2022newdevelopmentsin pages 59-60). Postnatally, FGF10 overexpression increases small intestinal crypt depth and villus height and promotes goblet cell differentiation (ornitz2022newdevelopmentsin pages 59-60).
During embryonic liver development, Fgf10 is expressed in mesoderm located near the hepatic endoderm (ornitz2022newdevelopmentsin pages 59-60). Fgf10-null embryos exhibit smaller livers with reduced hepatoblast proliferation and survival, indicating that FGF10 is required for embryonic liver growth and hepatoblast expansion (ornitz2022newdevelopmentsin pages 59-60).
FGF10 also contributes to tooth development, facial formation during embryogenesis, prostatic growth, thalamocortical axon navigation, and ocular development (edirisinghe2025pathologyandtherapeutic pages 8-10, edirisinghe2024decodingfgffgfrsignaling pages 7-8). FGF10 expression has been documented in the sclera and in the second heart field, indicating roles in eye and cardiac development (bzdega2022phenotypicspectrumof pages 3-5).
The paracrine signaling mechanisms employed during development are redeployed after injury, positioning FGF10 as a candidate regenerative factor. Experimental evidence demonstrates that FGF10 promotes epithelial survival and regeneration across multiple tissues.
In lung injury models, FGF10 supports epithelial regeneration by activating bronchioalveolar stem cells, promoting their expansion, and helping repair damaged airways (baran2025fibroblastgrowthfactors pages 10-12). It mediates stromal niche support for epithelial regeneration and may mobilize and proliferate mesenchymal stem cells (baran2025fibroblastgrowthfactors pages 10-12). After bleomycin-induced lung injury, FGF10/FGFR2b signaling can induce airway basal stem cells to differentiate into AT2 cells, with some subsequently becoming AT1 cells, suggesting a route toward alveolar repair (baran2025fibroblastgrowthfactors pages 10-12).
FGF10 treatment has shown protective effects in multiple injury models. In kidney ischemia/reperfusion injury, FGF10 improved renal function and histological integrity while suppressing excessive autophagy and endoplasmic reticulum stress (chen2022rolesofthe pages 8-10). In intestinal injury, FGF10 promoted repair of resected small bowel through activation of epithelial FGFR2IIIb (chen2022rolesofthe pages 8-10). For skin wounds, FGF10 enhanced healing in diabetic rats and stimulated keratinocyte proliferation while inhibiting endoplasmic reticulum stress, thereby accelerating wound healing and hair growth (chen2022rolesofthe pages 8-10, chen2022rolesofthe pages 10-11).
Recent translational research has identified FGF10 as a promising therapeutic target for chronic obstructive pulmonary disease (COPD) and emphysema, supported by compelling preclinical evidence published in 2023.
A landmark 2023 study published in the European Respiratory Journal demonstrated reduced FGF10 expression in alveolar walls and primary interstitial fibroblasts isolated from COPD patient lungs compared to healthy controls (hadzic2023fibroblastgrowthfactor pages 1-2, hadzic2023fibroblastgrowthfactor pages 3-4). Even after in vitro propagation, fibroblasts from end-stage emphysema/COPD lungs maintained persistently reduced FGF10 expression, and cigarette smoke extract further reduced FGF10 expression in both healthy and COPD fibroblasts (hadzic2023fibroblastgrowthfactor pages 3-4). These findings link impaired FGF10 signaling to COPD pathogenesis.
Mice with genetically impaired FGF10/FGFR2b signaling (Fgf10+/− and Fgfr2b+/− heterozygotes) spontaneously developed emphysema, pulmonary hypertension, and other pathomechanistic features that typically arise from cigarette smoke exposure (hadzic2023fibroblastgrowthfactor pages 1-2, hadzic2023fibroblastgrowthfactor pages 3-4). This establishes that deficient alveolar FGF10 signaling is sufficient to produce disease-like phenotypes, supporting a causal rather than merely correlative relationship.
Most significantly, FGF10 overexpression successfully restored lung alveolar and vascular structure in mice with established cigarette smoke-induced and elastase-induced emphysema and pulmonary hypertension (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 1-2, hadzic2023fibroblastgrowthfactor pages 13-14, hadzic2023fibroblastgrowthfactor pages 3-4). This therapeutic intervention reversed rather than merely prevented disease progression. FGF10 treatment initially increased alveolar type 2 (AT2) cell numbers, which gradually returned toward baseline as the FGF10-mediated repair process progressed, suggesting engagement of epithelial regenerative mechanisms (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 13-14). The reversal of pulmonary hypertension may be linked to recovery of the pulmonary capillary network and reversal of vascular remodeling (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 13-14).
The 2023 study validated findings in precision-cut lung slices (PCLS) obtained from COPD patients. Recombinant FGF10 treatment increased AT2 cell numbers in human COPD tissue and activated the canonical β-catenin pathway, identifying a downstream mechanism for epithelial regeneration (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 13-14). This human ex vivo evidence improves translational relevance, though clinical efficacy, optimal dosing, delivery route, and long-term safety in patients remain to be established.
FGF10 also protects pulmonary endothelium in COPD models. It reduces endothelial cell apoptosis and restores damaged glycocalyx components including heparan sulfate, chondroitin sulfate, and syndecan-1 (baran2025fibroblastgrowthfactors pages 13-14, jiang2022fibroblastgrowthfactor pages 1-2). The protective mechanism involves FGF10 activation of FGFR1 and downstream ERK/SOX9/HS6ST1 signaling, which promotes heparan sulfate biosynthesis (baran2025fibroblastgrowthfactors pages 13-14, jiang2022fibroblastgrowthfactor pages 1-2). This illustrates a context where FGFR1-associated activity complements the canonical epithelial FGFR2b axis and contributes to pulmonary vascular protection.
Based on the preclinical evidence, recombinant FGF10, gene delivery approaches, stabilized FGF10 variants, and downstream pathway stimulation are under investigation for emphysema, pulmonary hypertension, lung injury, wound repair, organoid culture, and regenerative medicine applications (hadzic2023fibroblastgrowthfactor pages 14-15, baran2025fibroblastgrowthfactors pages 10-12, baran2025fibroblastgrowthfactors pages 14-16). However, no approved FGF10-based medicine or proven patient benefit has been established in the cited literature.
Major translational barriers include FGF10's inherent protein instability at physiological temperature, heparan sulfate-dependent tissue distribution requirements, challenges in delivery and dosing, potential for unwanted ectopic growth, context-dependent receptor usage, and possible pro-tumorigenic signaling in certain settings (chen2025fgfbaseddrugdiscovery pages 2-4, baran2025fibroblastgrowthfactors pages 7-8). Engineered thermostable FGF10 variants with improved stability have been developed and show enhanced activity in experimental models, potentially addressing one barrier to therapeutic application (baran2025fibroblastgrowthfactors pages 13-14).
| Category | FGF10 annotation and evidence | Functional interpretation | Key citations |
|---|---|---|---|
| Identity | Human FGF10 encodes fibroblast growth factor 10, also called keratinocyte growth factor 2 (KGF-2). It belongs to the heparin-binding FGF family and the FGF7 subfamily with FGF3, FGF7, and FGF22. | Confirms that UniProt O15520 is the intended human protein and not a similarly named gene from another organism. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2024decodingfgffgfrsignaling pages 5-7) |
| Protein architecture | FGF10 is synthesized as a 208-amino-acid precursor of approximately 23.4 kDa. Residues 1–37 form an N-terminal signal peptide; residues 38–208 encompass the mature FGF domain. Reported glycosylation sites occur at residues 51 and 196. | The signal peptide routes FGF10 through the classical ER–Golgi secretory pathway; the mature extracellular protein supplies the receptor- and heparan-sulfate-binding surfaces. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5) |
| Fold and structural features | The mature protein adopts the characteristic FGF β-trefoil fold, containing 12 antiparallel β-strands. Relative to FGF1/FGF2, FGF10 has a longer β1 strand, less-organized β10–β11 regions, and a short N-terminal helix connected to β1. | These features support classification in the Fibroblast_GF_fam/IL1–FGF structural superfamily and help determine receptor selectivity. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8) |
| Primary molecular function | FGF10 is not an enzyme or transporter. It is a locally acting extracellular growth-factor ligand that converts mesenchymal positional and regenerative cues into receptor-tyrosine-kinase signaling in nearby target cells. | Its most precise functional annotation is a heparan-sulfate-dependent paracrine agonist of epithelial FGFR2b, regulating proliferation, survival, migration, differentiation, and morphogenesis. | (bzdega2022phenotypicspectrumof pages 1-3, bzdega2022phenotypicspectrumof pages 3-5, chen2025fgfbaseddrugdiscovery pages 2-4, edirisinghe2024decodingfgffgfrsignaling pages 7-8) |
| Principal receptor | The best-established receptor is FGFR2b, the epithelial IgIIIb splice isoform of FGFR2. FGF10 contacts receptor D2/D3 regions; implicated ligand surfaces include its N terminus, β1 and β4 strands, βB′–βC region, and β7–β8 loop. Asp76, Arg78, and Thr114 have experimentally supported functional importance. | Alternative splicing creates receptor specificity: FGF10 preferentially signals from mesenchyme to cells bearing epithelial b isoforms rather than mesenchymal c isoforms. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8, bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2024decodingfgffgfrsignaling pages 5-7) |
| Additional receptor activity | Some receptor-specificity maps and functional studies support signaling through FGFR1b, although FGFR2b remains the characteristic and dominant developmental receptor. Evidence does not support treating FGFR1c, FGFR2c, FGFR3, or FGFR4 as equivalent physiological receptors. | Functional annotation should state FGFR2b primarily; FGFR1b in selected contexts, avoiding the overstatement that FGF10 is absolutely exclusive to FGFR2b in every tissue. | (ferguson2021fibroblastgrowthfactor pages 2-3, francavilla2022fibroblastgrowthfactor pages 3-4, edirisinghe2024decodingfgffgfrsignaling pages 8-10) |
| Heparan-sulfate cofactor | Cell-surface or extracellular-matrix heparan sulfate proteoglycans (HSPGs)—including syndecans, glypicans, and perlecan—bind FGF10 through sulfated HS chains. HS stabilizes the ligand–receptor complex, facilitates productive FGFR dimerization/activation, and retains FGF10 near its source. | HSPGs both enable signaling and restrict diffusion, thereby creating local morphogen fields and preventing endocrine-like systemic action. They are cofactors, not the signal-transducing receptor. | (bzdega2022phenotypicspectrumof pages 3-5, chen2025fgfbaseddrugdiscovery pages 2-4, farooq2021theroleof pages 5-6, edirisinghe2024decodingfgffgfrsignaling pages 5-7) |
| Receptor activation mechanism | FGF10–HS engagement promotes FGFR dimerization and trans-autophosphorylation of cytoplasmic tyrosines. Activated receptors recruit FRS2α, GRB2/SOS, GAB1, PI3K, and PLCγ; FGF10-induced FGFR2 phosphorylation at Y734 can recruit PI3K regulatory subunits and trafficking proteins. | The ligand has no catalytic activity itself; it allosterically assembles an extracellular signaling complex that activates the intracellular FGFR kinase domains. | (bzdega2022phenotypicspectrumof pages 3-5, ferguson2021fibroblastgrowthfactor pages 3-5, ferguson2021fibroblastgrowthfactor pages 5-7) |
| MAPK pathway | FRS2α–GRB2–SOS activates RAS–RAF–MEK–ERK, with possible p38/JNK branches. In pseudoglandular lung epithelium, FGF10–FGFR2b preferentially produced strong ERK activation and promoted epithelial proliferation and bud outgrowth. | MAPK/ERK is the dominant experimentally demonstrated output in developing lung epithelium, though pathway weighting is tissue- and state-dependent. | (francavilla2022fibroblastgrowthfactor pages 2-3, yin2020fgf9andfgf10 pages 9-9, yin2020fgf9andfgf10 pages 1-2, yin2020fgf9andfgf10 pages 7-8) |
| PI3K pathway | FGFR2b can recruit GAB1/PI3K and activate PI3K–AKT–mTOR, supporting survival, metabolism, and growth. Direct FGF10-dependent recruitment of PI3K to FGFR2b has been described, although AKT activation is weaker than ERK in some embryonic-lung contexts. | PI3K/AKT is a genuine downstream branch but should not automatically be described as the dominant FGF10 output in every cell type. | (francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, ferguson2021fibroblastgrowthfactor pages 5-7, yin2020fgf9andfgf10 pages 9-9) |
| PLCγ and STAT pathways | Activated FGFR can recruit PLCγ, which hydrolyzes PIP2 into IP3 and DAG, causing Ca²⁺ release and PKC activation. FGFR signaling can also activate STAT1/3/5 and nuclear transcription. | These are recognized canonical FGFR outputs; evidence is less often resolved specifically for endogenous FGF10–FGFR2b than for ERK in lung development. | (bzdega2022phenotypicspectrumof pages 3-5, francavilla2022fibroblastgrowthfactor pages 2-3, ferguson2021fibroblastgrowthfactor pages 3-5, liu2021fgfmechanismof pages 4-5) |
| Localization and mode of action | FGF10 enters the ER–Golgi pathway, is secreted, and functions predominantly in the extracellular/pericellular matrix. It is commonly produced by mesenchymal or stromal cells and acts on adjacent FGFR2b-positive epithelial cells. | The principal site of function is outside the producing cell, at the HS-rich surface and matrix surrounding target cells; this is classic mesenchyme-to-epithelium paracrine signaling. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8, baran2025fibroblastgrowthfactors pages 5-7, baran2025fibroblastgrowthfactors pages 7-8, ornitz2022newdevelopmentsin pages 59-60) |
| Lung branching morphogenesis | In developing lung, mesenchymal FGF10 signals to epithelial FGFR2b to direct epithelial growth, migration/outgrowth, survival, branching, and proximal–distal patterning. Genetic loss of Fgf10 or Fgfr2b causes severe growth failure or lung agenesis; conditional inhibition after bud initiation impairs branching. | Lung development supplies the strongest mechanistic model for FGF10: a spatially restricted mesenchymal cue organizes a branching epithelial organ. | (sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 7-8, baran2025fibroblastgrowthfactors pages 5-7, yin2020fgf9andfgf10 pages 1-2) |
| Lung progenitor and lineage regulation | FGF10 helps maintain distal SOX9⁺/ID2⁺ progenitors, activates β-catenin-associated programs, and influences BMP4, SOX9, SOX2, basal-cell fate, alveolar type 2-cell behavior, and later alveolar formation. SHH provides negative feedback that spatially restrains FGF10. | FGF10 is both mitogenic and instructive, but its effects depend on dose, location, and developmental stage; sustained excess can suppress normal branching and produce cyst-like epithelial expansion. | (baran2025fibroblastgrowthfactors pages 7-8, sedighi2021theroleof pages 20-23, baran2025fibroblastgrowthfactors pages 5-7) |
| Other organogenesis | FGF10–FGFR2b signaling contributes to lacrimal and salivary gland formation, tooth and facial development, neural guidance, gastrointestinal morphogenesis, liver growth, and other epithelial organs. In the gut, loss disrupts stomach, duodenum, cecum, and colon development; in liver, null embryos show reduced hepatoblast proliferation/survival and smaller livers. | These phenotypes generalize the same core mechanism: mesenchymal FGF10 controls the survival, expansion, patterning, or branching of adjacent epithelia. | (bzdega2022phenotypicspectrumof pages 3-5, edirisinghe2025pathologyandtherapeutic pages 8-10, edirisinghe2024decodingfgffgfrsignaling pages 7-8, ornitz2022newdevelopmentsin pages 59-60) |
| Human genetic evidence | Heterozygous pathogenic FGF10 variants cause aplasia of the lacrimal and salivary glands (ALSG) and contribute to lacrimo-auriculo-dento-digital syndrome (LADD), demonstrating dosage sensitivity in human glandular development. | Human Mendelian disease strongly corroborates animal and tissue-model evidence that FGF10 is essential for epithelial gland morphogenesis. | (edirisinghe2024decodingfgffgfrsignaling pages 7-8, edirisinghe2025pathologyandtherapeutic pages 8-10, sedighi2021theroleof pages 20-23) |
| Tissue repair and regeneration | Experimental FGF10 promotes epithelial survival and regeneration in lung, intestine, kidney, lacrimal gland, and skin models. Reported effects include intestinal epithelial repair through FGFR2b, reduced injury-associated stress in kidney, and enhanced keratinocyte proliferation and wound healing. | Developmental signaling is redeployed after injury, making FGF10 a candidate regenerative agonist; most evidence remains preclinical. | (chen2022rolesofthe pages 8-10, chen2022rolesofthe pages 10-11) |
| COPD and emphysema evidence | A 2023 study found reduced FGF10 in COPD alveolar walls and interstitial fibroblasts. Partial impairment of Fgf10/Fgfr2b signaling in mice produced emphysema and pulmonary-hypertension features, whereas FGF10 overexpression after cigarette-smoke- or elastase-induced disease restored alveolar and vascular structure. | This provides loss-of-function and therapeutic-rescue evidence that inadequate FGF10 signaling contributes to failed alveolar maintenance and that pathway restoration can be disease-modifying in models. | (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 1-2, hadzic2023fibroblastgrowthfactor pages 3-4) |
| Human translational lung models | Recombinant FGF10 increased alveolar type 2-cell numbers in precision-cut lung slices from people with COPD; mouse and human ex-vivo responses implicated canonical β-catenin-associated epithelial repair. | Human tissue data improve translational relevance but do not establish clinical efficacy, optimal dose, delivery route, or long-term safety. | (hadzic2023fibroblastgrowthfactor pages 14-15, hadzic2023fibroblastgrowthfactor pages 13-14) |
| Endothelial and glycocalyx repair | In smoke-exposure models, FGF10 reduced endothelial apoptosis and glycocalyx shedding through an FGFR1–ERK–SOX9–HS6ST1 mechanism, helping preserve heparan sulfate, chondroitin sulfate, and syndecan-1. | This illustrates a context in which FGFR1-associated activity complements the canonical epithelial FGFR2b axis and may contribute to pulmonary vascular protection. | (baran2025fibroblastgrowthfactors pages 13-14, jiang2022fibroblastgrowthfactor pages 1-2) |
| Current application status | Recombinant FGF10, gene delivery, stabilized variants, and downstream-pathway stimulation are being investigated for emphysema, pulmonary hypertension, lung injury, wound repair, organoids, and regenerative medicine. No cited evidence establishes an approved FGF10 medicine or proven patient benefit. | Major translational barriers include short protein stability, HS-dependent tissue distribution, delivery and dosing, unwanted ectopic growth, context-dependent receptor use, and possible pro-tumorigenic signaling. | (chen2025fgfbaseddrugdiscovery pages 2-4, hadzic2023fibroblastgrowthfactor pages 14-15, baran2025fibroblastgrowthfactors pages 10-12, baran2025fibroblastgrowthfactors pages 14-16) |
Table: This table integrates FGF10 structure, localization, receptor specificity, signaling pathways, developmental roles, and recent regenerative applications. It distinguishes well-established molecular functions from context-dependent receptor activity and preclinical therapeutic findings.
FGF10 (UniProt O15520) is a secreted paracrine signaling molecule belonging to the FGF7 subfamily of heparin-binding growth factors. It functions primarily through binding to FGFR2b (and to a lesser extent FGFR1b) on epithelial cells, with heparan sulfate proteoglycans serving as essential cofactors. Upon receptor engagement, FGF10 activates multiple downstream pathways including MAPK/ERK, PI3K/AKT, PLCγ, and STAT signaling.
The protein's primary and best-characterized biological function is directing lung branching morphogenesis during development, where mesenchymal FGF10 coordinates epithelial growth, patterning, survival, and differentiation. Genetic loss of FGF10 or FGFR2b results in lung agenesis, establishing its essential developmental role. Beyond the lung, FGF10 is critical for development of lacrimal and salivary glands, gastrointestinal organs, liver, and other tissues, as evidenced by human genetic syndromes caused by FGF10 mutations.
Recent 2023 research has established FGF10 as a promising therapeutic target for COPD and emphysema, with preclinical studies demonstrating that FGF10 overexpression can reverse established disease in mouse models and activate regenerative responses in human lung tissue. These findings represent a significant advance in understanding FGF10's regenerative potential and suggest future clinical applications, though substantial translational challenges remain before therapeutic use in patients can be realized.
References
(edirisinghe2024decodingfgffgfrsignaling pages 7-8): Oshadi Edirisinghe, Gaëtane Ternier, Zeina Alraawi, and Thallapuranam Krishnaswamy Suresh Kumar. Decoding fgf/fgfr signaling: insights into biological functions and disease relevance. Biomolecules, 14:1622, Dec 2024. URL: https://doi.org/10.3390/biom14121622, doi:10.3390/biom14121622. This article has 67 citations.
(bzdega2022phenotypicspectrumof pages 3-5): Katarzyna Bzdęga and Justyna A. Karolak. Phenotypic spectrum of fgf10-related disorders: a systematic review. PeerJ, Sep 2022. URL: https://doi.org/10.7717/peerj.14003, doi:10.7717/peerj.14003. This article has 14 citations and is from a peer-reviewed journal.
(edirisinghe2024decodingfgffgfrsignaling pages 5-7): Oshadi Edirisinghe, Gaëtane Ternier, Zeina Alraawi, and Thallapuranam Krishnaswamy Suresh Kumar. Decoding fgf/fgfr signaling: insights into biological functions and disease relevance. Biomolecules, 14:1622, Dec 2024. URL: https://doi.org/10.3390/biom14121622, doi:10.3390/biom14121622. This article has 67 citations.
(edirisinghe2025pathologyandtherapeutic pages 8-10): Oshadi Edirisinghe, Gaëtane Ternier, and Thallapuranam Krishnaswamy Suresh Kumar. Pathology and therapeutic significance of fibroblast growth factors. Targets, 3:5, Feb 2025. URL: https://doi.org/10.3390/targets3010005, doi:10.3390/targets3010005. This article has 6 citations.
(bzdega2022phenotypicspectrumof pages 1-3): Katarzyna Bzdęga and Justyna A. Karolak. Phenotypic spectrum of fgf10-related disorders: a systematic review. PeerJ, Sep 2022. URL: https://doi.org/10.7717/peerj.14003, doi:10.7717/peerj.14003. This article has 14 citations and is from a peer-reviewed journal.
(baran2025fibroblastgrowthfactors pages 5-7): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.
(baran2025fibroblastgrowthfactors pages 7-8): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.
(ornitz2022newdevelopmentsin pages 59-60): D. Ornitz and N. Itoh. New developments in the biology of fibroblast growth factors. WIREs mechanisms of disease, pages e1549, Feb 2022. URL: https://doi.org/10.1002/wsbm.1549, doi:10.1002/wsbm.1549. This article has 171 citations.
(yin2020fgf9andfgf10 pages 8-9): Yongjun Yin and David M. Ornitz. Fgf9 and fgf10 activate distinct signaling pathways to direct lung epithelial specification and branching. Science Signaling, Mar 2020. URL: https://doi.org/10.1126/scisignal.aay4353, doi:10.1126/scisignal.aay4353. This article has 64 citations and is from a domain leading peer-reviewed journal.
(chen2025fgfbaseddrugdiscovery pages 2-4): Gaozhi Chen, Lingfeng Chen, Xiaokun Li, and Moosa Mohammadi. Fgf-based drug discovery: advances and challenges. Nature reviews. Drug discovery, Jan 2025. URL: https://doi.org/10.1038/s41573-024-01125-w, doi:10.1038/s41573-024-01125-w. This article has 52 citations.
(ferguson2021fibroblastgrowthfactor pages 2-3): Harriet R. Ferguson, Michael P. Smith, and Chiara Francavilla. Fibroblast growth factor receptors (fgfrs) and noncanonical partners in cancer signaling. Cells, 10:1201, May 2021. URL: https://doi.org/10.3390/cells10051201, doi:10.3390/cells10051201. This article has 150 citations.
(francavilla2022fibroblastgrowthfactor pages 3-4): Chiara Francavilla and Ciara S. O'Brien. Fibroblast growth factor receptor signalling dysregulation and targeting in breast cancer. Open Biology, Feb 2022. URL: https://doi.org/10.1098/rsob.210373, doi:10.1098/rsob.210373. This article has 63 citations and is from a peer-reviewed journal.
(edirisinghe2024decodingfgffgfrsignaling pages 8-10): Oshadi Edirisinghe, Gaëtane Ternier, Zeina Alraawi, and Thallapuranam Krishnaswamy Suresh Kumar. Decoding fgf/fgfr signaling: insights into biological functions and disease relevance. Biomolecules, 14:1622, Dec 2024. URL: https://doi.org/10.3390/biom14121622, doi:10.3390/biom14121622. This article has 67 citations.
(farooq2021theroleof pages 5-6): Mariya Farooq, Abdul Waheed Khan, Moon Suk Kim, and Sangdun Choi. The role of fibroblast growth factor (fgf) signaling in tissue repair and regeneration. Cells, 10:3242, Nov 2021. URL: https://doi.org/10.3390/cells10113242, doi:10.3390/cells10113242. This article has 446 citations.
(chen2022rolesofthe pages 3-4): Keyang Chen, Zhiheng Rao, Siyang Dong, Yajing Chen, Xulan Wang, Yongde Luo, Fanghua Gong, and Xiaokun Li. Roles of the fibroblast growth factor signal transduction system in tissue injury repair. Burns & Trauma, Mar 2022. URL: https://doi.org/10.1093/burnst/tkac005, doi:10.1093/burnst/tkac005. This article has 57 citations and is from a peer-reviewed journal.
(ferguson2021fibroblastgrowthfactor pages 3-5): Harriet R. Ferguson, Michael P. Smith, and Chiara Francavilla. Fibroblast growth factor receptors (fgfrs) and noncanonical partners in cancer signaling. Cells, 10:1201, May 2021. URL: https://doi.org/10.3390/cells10051201, doi:10.3390/cells10051201. This article has 150 citations.
(francavilla2022fibroblastgrowthfactor pages 2-3): Chiara Francavilla and Ciara S. O'Brien. Fibroblast growth factor receptor signalling dysregulation and targeting in breast cancer. Open Biology, Feb 2022. URL: https://doi.org/10.1098/rsob.210373, doi:10.1098/rsob.210373. This article has 63 citations and is from a peer-reviewed journal.
(liu2021fgfmechanismof pages 4-5): Yiqiu Liu, Junyu Deng, Ye Liu, Wei Li, and Xuqiang Nie. Fgf, mechanism of action, role in parkinson’s disease, and therapeutics. Frontiers in Pharmacology, Jun 2021. URL: https://doi.org/10.3389/fphar.2021.675725, doi:10.3389/fphar.2021.675725. This article has 62 citations.
(liu2026fgffamilyin pages 3-4): Xiaoyu Liu, Meiling Jing, Yueyi Yang, Qiaoqiao Jin, B. Feng, Pengfei Zhang, Chenguang Niu, Xuchen Hu, and Zheng-Wei Huang. Fgf family in health and disease. Molecular Biomedicine, Mar 2026. URL: https://doi.org/10.1186/s43556-026-00429-0, doi:10.1186/s43556-026-00429-0. This article has 10 citations and is from a peer-reviewed journal.
(yin2020fgf9andfgf10 pages 9-9): Yongjun Yin and David M. Ornitz. Fgf9 and fgf10 activate distinct signaling pathways to direct lung epithelial specification and branching. Science Signaling, Mar 2020. URL: https://doi.org/10.1126/scisignal.aay4353, doi:10.1126/scisignal.aay4353. This article has 64 citations and is from a domain leading peer-reviewed journal.
(yin2020fgf9andfgf10 pages 1-2): Yongjun Yin and David M. Ornitz. Fgf9 and fgf10 activate distinct signaling pathways to direct lung epithelial specification and branching. Science Signaling, Mar 2020. URL: https://doi.org/10.1126/scisignal.aay4353, doi:10.1126/scisignal.aay4353. This article has 64 citations and is from a domain leading peer-reviewed journal.
(yin2020fgf9andfgf10 pages 7-8): Yongjun Yin and David M. Ornitz. Fgf9 and fgf10 activate distinct signaling pathways to direct lung epithelial specification and branching. Science Signaling, Mar 2020. URL: https://doi.org/10.1126/scisignal.aay4353, doi:10.1126/scisignal.aay4353. This article has 64 citations and is from a domain leading peer-reviewed journal.
(ferguson2021fibroblastgrowthfactor pages 5-7): Harriet R. Ferguson, Michael P. Smith, and Chiara Francavilla. Fibroblast growth factor receptors (fgfrs) and noncanonical partners in cancer signaling. Cells, 10:1201, May 2021. URL: https://doi.org/10.3390/cells10051201, doi:10.3390/cells10051201. This article has 150 citations.
(wang2021fgffgfrsignalingin pages 2-4): Yijun Wang, Danfei Liu, Tongyue Zhang, and Limin Xia. Fgf/fgfr signaling in hepatocellular carcinoma: from carcinogenesis to recent therapeutic intervention. Cancers, 13:1360, Mar 2021. URL: https://doi.org/10.3390/cancers13061360, doi:10.3390/cancers13061360. This article has 80 citations.
(sedighi2021theroleof pages 20-23): The role of Fgf10/Fgfr2b signaling during lung development This article has 0 citations.
(baran2025fibroblastgrowthfactors pages 18-19): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.
(baran2025fibroblastgrowthfactors pages 10-12): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.
(chen2022rolesofthe pages 8-10): Keyang Chen, Zhiheng Rao, Siyang Dong, Yajing Chen, Xulan Wang, Yongde Luo, Fanghua Gong, and Xiaokun Li. Roles of the fibroblast growth factor signal transduction system in tissue injury repair. Burns & Trauma, Mar 2022. URL: https://doi.org/10.1093/burnst/tkac005, doi:10.1093/burnst/tkac005. This article has 57 citations and is from a peer-reviewed journal.
(chen2022rolesofthe pages 10-11): Keyang Chen, Zhiheng Rao, Siyang Dong, Yajing Chen, Xulan Wang, Yongde Luo, Fanghua Gong, and Xiaokun Li. Roles of the fibroblast growth factor signal transduction system in tissue injury repair. Burns & Trauma, Mar 2022. URL: https://doi.org/10.1093/burnst/tkac005, doi:10.1093/burnst/tkac005. This article has 57 citations and is from a peer-reviewed journal.
(hadzic2023fibroblastgrowthfactor pages 1-2): Stefan Hadzic, Cheng-Yu Wu, Marija Gredic, Oleg Pak, Edma Loku, Simone Kraut, Baktybek Kojonazarov, Jochen Wilhelm, Monika Brosien, Mariola Bednorz, Michael Seimetz, Andreas Günther, Djuro Kosanovic, Natascha Sommer, David Warburton, Xiaokun Li, Friedrich Grimminger, Hossein A. Ghofrani, Ralph T. Schermuly, Werner Seeger, Elie El Agha, Saverio Bellusci, and Norbert Weissmann. Fibroblast growth factor 10 reverses cigarette smoke- and elastase-induced emphysema and pulmonary hypertension in mice. European Respiratory Journal, 62:2201606, Oct 2023. URL: https://doi.org/10.1183/13993003.01606-2022, doi:10.1183/13993003.01606-2022. This article has 36 citations and is from a highest quality peer-reviewed journal.
(hadzic2023fibroblastgrowthfactor pages 3-4): Stefan Hadzic, Cheng-Yu Wu, Marija Gredic, Oleg Pak, Edma Loku, Simone Kraut, Baktybek Kojonazarov, Jochen Wilhelm, Monika Brosien, Mariola Bednorz, Michael Seimetz, Andreas Günther, Djuro Kosanovic, Natascha Sommer, David Warburton, Xiaokun Li, Friedrich Grimminger, Hossein A. Ghofrani, Ralph T. Schermuly, Werner Seeger, Elie El Agha, Saverio Bellusci, and Norbert Weissmann. Fibroblast growth factor 10 reverses cigarette smoke- and elastase-induced emphysema and pulmonary hypertension in mice. European Respiratory Journal, 62:2201606, Oct 2023. URL: https://doi.org/10.1183/13993003.01606-2022, doi:10.1183/13993003.01606-2022. This article has 36 citations and is from a highest quality peer-reviewed journal.
(hadzic2023fibroblastgrowthfactor pages 14-15): Stefan Hadzic, Cheng-Yu Wu, Marija Gredic, Oleg Pak, Edma Loku, Simone Kraut, Baktybek Kojonazarov, Jochen Wilhelm, Monika Brosien, Mariola Bednorz, Michael Seimetz, Andreas Günther, Djuro Kosanovic, Natascha Sommer, David Warburton, Xiaokun Li, Friedrich Grimminger, Hossein A. Ghofrani, Ralph T. Schermuly, Werner Seeger, Elie El Agha, Saverio Bellusci, and Norbert Weissmann. Fibroblast growth factor 10 reverses cigarette smoke- and elastase-induced emphysema and pulmonary hypertension in mice. European Respiratory Journal, 62:2201606, Oct 2023. URL: https://doi.org/10.1183/13993003.01606-2022, doi:10.1183/13993003.01606-2022. This article has 36 citations and is from a highest quality peer-reviewed journal.
(hadzic2023fibroblastgrowthfactor pages 13-14): Stefan Hadzic, Cheng-Yu Wu, Marija Gredic, Oleg Pak, Edma Loku, Simone Kraut, Baktybek Kojonazarov, Jochen Wilhelm, Monika Brosien, Mariola Bednorz, Michael Seimetz, Andreas Günther, Djuro Kosanovic, Natascha Sommer, David Warburton, Xiaokun Li, Friedrich Grimminger, Hossein A. Ghofrani, Ralph T. Schermuly, Werner Seeger, Elie El Agha, Saverio Bellusci, and Norbert Weissmann. Fibroblast growth factor 10 reverses cigarette smoke- and elastase-induced emphysema and pulmonary hypertension in mice. European Respiratory Journal, 62:2201606, Oct 2023. URL: https://doi.org/10.1183/13993003.01606-2022, doi:10.1183/13993003.01606-2022. This article has 36 citations and is from a highest quality peer-reviewed journal.
(baran2025fibroblastgrowthfactors pages 13-14): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.
(jiang2022fibroblastgrowthfactor pages 1-2): Tian Jiang, Weiping Hu, Shaoyuan Zhang, Changhao Ren, Siyun Lin, Zhenyu Zhou, Hao Wu, Jun Yin, and Lijie Tan. Fibroblast growth factor 10 attenuates chronic obstructive pulmonary disease by protecting against glycocalyx impairment and endothelial apoptosis. Respiratory Research, Oct 2022. URL: https://doi.org/10.1186/s12931-022-02193-5, doi:10.1186/s12931-022-02193-5. This article has 29 citations and is from a domain leading peer-reviewed journal.
(baran2025fibroblastgrowthfactors pages 14-16): Karolina Baran, Kamila Skrzynska, Aleksandra A. Czyrek, Adrianna Wittek, Daniel Krowarsch, Anna Szlachcic, Malgorzata Zakrzewska, and Julia Chudzian. Fibroblast growth factors in lung development and regeneration: mechanisms and therapeutic potential. Cells, 14:1256, Aug 2025. URL: https://doi.org/10.3390/cells14161256, doi:10.3390/cells14161256. This article has 11 citations.