# Fibroblast growth factor 1

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Protein-coding gene in the species Homo sapiens

This article is about fibroblast growth factor-1. For the internal ribosome entry site, see [FGF-1 internal ribosome entry site (IRES)](/source/FGF-1_internal_ribosome_entry_site_(IRES)).

FGF1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4QO3, 1AXM, 1DJS, 1DZC, 1DZD, 1E0O, 1EVT, 1HKN, 1JQZ, 1JT3, 1JT4, 1JT5, 1JT7, 1JTC, 1JY0, 1K5U, 1K5V, 1M16, 1NZK, 1P63, 1PZZ, 1Q03, 1Q04, 1RG8, 1RML, 1RY7, 1YTO, 1Z2V, 1Z4S, 2AFG, 2AQZ, 2AXM, 2ERM, 2HW9, 2HWA, 2HWM, 2HZ9, 2K43, 2K4A, 2K8R, 2KI4, 2KI6, 2NTD, 2Q9X, 2RQ9, 3B9U, 3BA4, 3BA5, 3BA7, 3BAD, 3BAG, 3BAH, 3BAO, 3BAQ, 3BAU, 3BAV, 3BB2, 3CQA, 3CRG, 3CRH, 3CRI, 3CU1, 3FGM, 3FJ8, 3FJ9, 3FJA, 3FJB, 3FJC, 3FJD, 3FJE, 3FJF, 3FJH, 3FJI, 3FJJ, 3FJK, 3HOM, 3JUT, 3K1X, 3O3Q, 3OJ2, 3OJM, 3OJV, 3UD7, 3UD8, 3UD9, 3UDA, 4J23, 4Q91, 4Q9G, 4Q9P, 4QAL, 4QBC, 4QBV, 4QC4, 4XKI, 4YOL Identifiers Aliases FGF1, AFGF, ECGF, ECGF-beta, ECGFA, ECGFB, FGF-1, FGF-alpha, FGFA, GLIO703, HBGF-1, HBGF1, fibroblast growth factor 1 External IDs OMIM: 131220; MGI: 95515; HomoloGene: 625; GeneCards: FGF1; OMA:FGF1 - orthologs Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q31.3 Start 142,592,178 bp[1] End 142,698,070 bp[1] Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18 B3|18 20.74 cM Start 38,971,726 bp[2] End 39,062,525 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in glomerulus metanephric glomerulus inferior ganglion of vagus nerve corpus callosum optic nerve external globus pallidus internal globus pallidus medulla oblongata inferior olivary nucleus olfactory bulb Top expressed in deep cerebellar nuclei pontine nuclei medial vestibular nucleus habenula facial motor nucleus dorsal tegmental nucleus anterior horn of spinal cord right lung myocardium of ventricle right ventricle More reference expression data BioGPS More reference expression data Gene ontology Molecular function S100 protein binding protein binding growth factor activity protein tyrosine kinase activity phosphatidylinositol-4,5-bisphosphate 3-kinase activity fibroblast growth factor receptor binding integrin binding 1-phosphatidylinositol-3-kinase activity heparin binding Hsp70 protein binding Cellular component cytoplasm cytosol extracellular region cell cortex nucleolus nucleus extracellular space extracellular matrix Biological process cell differentiation cellular response to heat positive regulation of protein phosphorylation positive regulation of MAP kinase activity organ induction lung development positive regulation of epithelial cell proliferation anatomical structure morphogenesis positive regulation of intracellular signal transduction branch elongation involved in ureteric bud branching positive regulation of angiogenesis MAPK cascade multicellular organism development mesonephric epithelium development angiogenesis regulation of endothelial cell chemotaxis to fibroblast growth factor positive regulation of cholesterol biosynthetic process cell population proliferation positive regulation of cell division positive regulation of transcription by RNA polymerase II signal transduction phosphatidylinositol phosphate biosynthetic process peptidyl-tyrosine phosphorylation positive regulation of sprouting angiogenesis fibroblast growth factor receptor signaling pathway positive regulation of cell population proliferation phosphatidylinositol-3-phosphate biosynthetic process regulation of endothelial tube morphogenesis positive regulation of cell migration positive regulation of endothelial cell migration activation of protein kinase B activity regulation of signaling receptor activity positive regulation of protein kinase B signaling Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 2246 14164 Ensembl ENSG00000113578 ENSMUSG00000036585 UniProt P05230 P61148 RefSeq (mRNA) NM_000800 NM_001144892 NM_001144934 NM_001144935 NM_001257205 NM_001257206 NM_001257207 NM_001257208 NM_001257209 NM_001257210 NM_001257211 NM_001257212 NM_033136 NM_033137 NM_001354955 NM_001354956 NM_001354957 NM_001354958 NM_001354959 NM_001354961 NM_001354963 NM_001354964 NM_001354951 NM_001354952 NM_001354953 NM_001354954 NM_001354962 NM_010197 RefSeq (protein) NP_000791 NP_001138364 NP_001138406 NP_001138407 NP_001244134 NP_001244135 NP_001244136 NP_001244137 NP_001244138 NP_001244139 NP_001244140 NP_001244141 NP_149127 NP_149128 NP_001341884 NP_001341885 NP_001341886 NP_001341887 NP_001341888 NP_001341890 NP_001341892 NP_001341893 NP_001341880 NP_001341881 NP_001341882 NP_001341883 NP_001341891 NP_034327 Location (UCSC) Chr 5: 142.59 – 142.7 Mb Chr 18: 38.97 – 39.06 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Fibroblast growth factor 1** **(FGF-1)** also known as **acidic fibroblast growth factor** (**aFGF**)[5], is a [growth factor](/source/Growth_factor) and [signaling protein](/source/Signaling_protein) encoded by the *FGF1* [gene](/source/Gene).[6][7] It is synthesized as a 155 amino acid polypeptide, whose mature form is a non-[glycosylated](/source/Glycosylated) 17-18 kDa protein. [Fibroblast growth factor](/source/Fibroblast_growth_factor) protein was first purified in 1975, but soon afterwards others using different conditions isolated acidic FGF, Heparin-binding growth factor-1, and [Endothelial cell growth factor-1](/source/ECGF1).[8] Gene sequencing revealed that this group was actually the same growth factor and that FGF1 was a member of a [family of FGF](/source/Fibroblast_growth_factor) proteins.

FGF-1 has no definitive signal sequence and thus is not secreted through classical pathways, but it does appear to form a disulfide linked dimer inside cells that associate with a complex of proteins at the cell membrane (including [S100A13](/source/S100A13) and [Syt1](/source/Synaptotagmin_1)) which then help flip it through the membrane to the exterior of the cell.[9][10] Once in the reducing conditions of the surrounding tissue, the dimer dissociates into [monomeric](/source/Monomer) FGF1 that can enter systemic circulation or be sequestered in tissues binding to [heparan sulfate proteoglycans](/source/Heparan_sulfate_proteoglycan) of the [extracellular matrix](/source/Extracellular_matrix). FGF1 can then bind to and exert its effects via specific [fibroblast growth factor receptor (FGFR)](/source/Fibroblast_growth_factor_receptor) proteins which themselves constitute a family of closely related molecules.[11]

In addition to its extracellular activity, FGF1 can also function intracellularly. The protein has a [nuclear localization sequence](/source/Nuclear_localization_sequence) (NLS) but the route that FGF1 takes to get to the nucleus is unclear and it appears that some sort of cell surface receptor binding is necessary, followed by its internalization and translocation to the nucleus whereupon it can interact with nuclear isoforms of FGFRs.[11] This is different from [FGF2](/source/FGF2) which also can activate nuclear FGFRs but has splicing variants of the protein that never leave the cell and go directly to the nucleus.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

## Function

FGF family members possess broad [mitogenic](/source/Mitogenic) and cell survival activities, and are involved in a variety of biological processes, including [embryonic development](/source/Embryonic_development), [cell growth](/source/Cell_growth), [morphogenesis](/source/Morphogenesis), [tissue repair](/source/Tissue_repair), tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of [mesoderm](/source/Mesoderm)- and neuroectoderm-derived cells in vitro, thus is thought to be involved in [organogenesis](/source/Organogenesis). Three alternatively spliced variants encoding different isoforms have been described.[12]

FGF1 is multifunctional with many reported effects. For one example, in mice with diet-induced diabetes that is an experimental equivalent of type 2 diabetes in humans, a single injection of the FGF1 protein is enough to restore blood sugar levels to a healthy range for > 2 days.[13]

## Interactions

FGF1 has been shown to [interact](/source/Protein-protein_interaction) with:

- [CSNK2A2](/source/CSNK2A2)[14]

- [CSNK2B](/source/CSNK2B)[14]

- [CSNK2A1](/source/Casein_kinase_2%2C_alpha_1)[14]

- [FIBP](/source/FIBP)[15]

- [FGFR1](/source/Fibroblast_growth_factor_receptor_1)[16][17]

- [FGFR2](/source/Fibroblast_growth_factor_receptor_2)[17][18][19]

- [FGFR3](/source/Fibroblast_growth_factor_receptor_3)[17][20]

- [FGFR4](/source/Fibroblast_growth_factor_receptor_4)[21][22]

- [HSPA9](/source/HSPA9)[23] and

- [S100A13](/source/S100A13)[10][24][25]

- [Synaptotagmin 1 (SYT1)](/source/Synaptotagmin_1)[10][24]

## See also

- [Fibroblast growth factor](/source/Fibroblast_growth_factor)

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000113578](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000113578) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000036585](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000036585) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=2246). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=14164). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-5)** Lawrence E. "aFGF". *Henderson's Dictionary of Biological Terms* (10th ed.). p. 1. [ISBN](/source/ISBN_(identifier)) [0-470-21446-5](https://en.wikipedia.org/wiki/Special:BookSources/0-470-21446-5).

1. **[^](#cite_ref-pmid1697263_6-0)** Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (September 1990). ["Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC551973). *The EMBO Journal*. **9** (9): 2685–92. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1990.tb07454.x](https://doi.org/10.1002%2Fj.1460-2075.1990.tb07454.x). [PMC](/source/PMC_(identifier)) [551973](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC551973). [PMID](/source/PMID_(identifier)) [1697263](https://pubmed.ncbi.nlm.nih.gov/1697263).

1. **[^](#cite_ref-pmid3523756_7-0)** Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN (August 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". *Science*. **233** (4763): 541–5. [Bibcode](/source/Bibcode_(identifier)):[1986Sci...233..541J](https://ui.adsabs.harvard.edu/abs/1986Sci...233..541J). [doi](/source/Doi_(identifier)):[10.1126/science.3523756](https://doi.org/10.1126%2Fscience.3523756). [PMID](/source/PMID_(identifier)) [3523756](https://pubmed.ncbi.nlm.nih.gov/3523756).

1. **[^](#cite_ref-8)** Burgess WH, Maciag T (1989). "The heparin-binding (fibroblast) growth factor family of proteins". *Annual Review of Biochemistry*. **58**: 575–606. [doi](/source/Doi_(identifier)):[10.1146/annurev.bi.58.070189.003043](https://doi.org/10.1146%2Fannurev.bi.58.070189.003043). [PMID](/source/PMID_(identifier)) [2549857](https://pubmed.ncbi.nlm.nih.gov/2549857).

1. **[^](#cite_ref-9)** Tarantini F, Gamble S, Jackson A, Maciag T (December 1995). ["The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding"](http://www.jbc.org/content/270/49/29039.long). *The Journal of Biological Chemistry*. **270** (49): 29039–42. [doi](/source/Doi_(identifier)):[10.1074/jbc.270.49.29039](https://doi.org/10.1074%2Fjbc.270.49.29039). [PMID](/source/PMID_(identifier)) [7493920](https://pubmed.ncbi.nlm.nih.gov/7493920).

1. ^ [***a***](#cite_ref-Prudovsky&Maciag_10-0) [***b***](#cite_ref-Prudovsky&Maciag_10-1) [***c***](#cite_ref-Prudovsky&Maciag_10-2) Prudovsky I, Bagala C, Tarantini F, Mandinova A, Soldi R, Bellum S, Maciag T (July 2002). ["The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export"](http://jcb.rupress.org/content/158/2/201.long). *The Journal of Cell Biology*. **158** (2): 201–8. [doi](/source/Doi_(identifier)):[10.1083/jcb.200203084](https://doi.org/10.1083%2Fjcb.200203084). [PMC](/source/PMC_(identifier)) [2173119](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173119). [PMID](/source/PMID_(identifier)) [12135982](https://pubmed.ncbi.nlm.nih.gov/12135982).

1. ^ [***a***](#cite_ref-pmid_24780002_11-0) [***b***](#cite_ref-pmid_24780002_11-1) Coleman SJ, Bruce C, Chioni AM, Kocher HM, Grose RP (August 2014). "The ins and outs of fibroblast growth factor receptor signalling". *Clinical Science*. **127** (4): 217–31. [doi](/source/Doi_(identifier)):[10.1042/CS20140100](https://doi.org/10.1042%2FCS20140100). [PMID](/source/PMID_(identifier)) [24780002](https://pubmed.ncbi.nlm.nih.gov/24780002).

1. **[^](#cite_ref-12)** ["Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=2246).

1. **[^](#cite_ref-13)** Suh JM, Jonker JW, Ahmadian M, Goetz R, Lackey D, Osborn O, Huang Z, Liu W, Yoshihara E, van Dijk TH, Havinga R, Fan W, Yin YQ, Yu RT, Liddle C, Atkins AR, Olefsky JM, Mohammadi M, Downes M, Evans RM (September 2014). ["Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4184286). *Nature*. **513** (7518): 436–9. [Bibcode](/source/Bibcode_(identifier)):[2014Natur.513..436S](https://ui.adsabs.harvard.edu/abs/2014Natur.513..436S). [doi](/source/Doi_(identifier)):[10.1038/nature13540](https://doi.org/10.1038%2Fnature13540). [PMC](/source/PMC_(identifier)) [4184286](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4184286). [PMID](/source/PMID_(identifier)) [25043058](https://pubmed.ncbi.nlm.nih.gov/25043058).*Lay summary in: ["One injection stops diabetes in its tracks"](http://www.salk.edu/news/pressrelease_details.php?press_id=2037). *Salk Institute*. July 16, 2014.

1. ^ [***a***](#cite_ref-pmid12145206_14-0) [***b***](#cite_ref-pmid12145206_14-1) [***c***](#cite_ref-pmid12145206_14-2) Skjerpen CS, Nilsen T, Wesche J, Olsnes S (August 2002). ["Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC126148). *The EMBO Journal*. **21** (15): 4058–69. [doi](/source/Doi_(identifier)):[10.1093/emboj/cdf402](https://doi.org/10.1093%2Femboj%2Fcdf402). [PMC](/source/PMC_(identifier)) [126148](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC126148). [PMID](/source/PMID_(identifier)) [12145206](https://pubmed.ncbi.nlm.nih.gov/12145206).

1. **[^](#cite_ref-pmid9806903_15-0)** Kolpakova E, Wiedłocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S (November 1998). ["Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219860). *The Biochemical Journal*. **336** (1): 213–22. [doi](/source/Doi_(identifier)):[10.1042/bj3360213](https://doi.org/10.1042%2Fbj3360213). [PMC](/source/PMC_(identifier)) [1219860](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219860). [PMID](/source/PMID_(identifier)) [9806903](https://pubmed.ncbi.nlm.nih.gov/9806903).

1. **[^](#cite_ref-pmid11030354_16-0)** Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M (September 2000). ["Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization"](https://doi.org/10.1016%2Fs1097-2765%2800%2900073-3). *Molecular Cell*. **6** (3): 743–50. [doi](/source/Doi_(identifier)):[10.1016/s1097-2765(00)00073-3](https://doi.org/10.1016%2Fs1097-2765%2800%2900073-3). [PMID](/source/PMID_(identifier)) [11030354](https://pubmed.ncbi.nlm.nih.gov/11030354).

1. ^ [***a***](#cite_ref-pmid8576175_17-0) [***b***](#cite_ref-pmid8576175_17-1) [***c***](#cite_ref-pmid8576175_17-2) Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (January 1996). ["Expression and biological activity of mouse fibroblast growth factor-9"](https://doi.org/10.1074%2Fjbc.271.3.1726). *The Journal of Biological Chemistry*. **271** (3): 1726–31. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.3.1726](https://doi.org/10.1074%2Fjbc.271.3.1726). [PMID](/source/PMID_(identifier)) [8576175](https://pubmed.ncbi.nlm.nih.gov/8576175).

1. **[^](#cite_ref-pmid10618369_18-0)** Stauber DJ, DiGabriele AD, Hendrickson WA (January 2000). ["Structural interactions of fibroblast growth factor receptor with its ligands"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC26614). *Proceedings of the National Academy of Sciences of the United States of America*. **97** (1): 49–54. [Bibcode](/source/Bibcode_(identifier)):[2000PNAS...97...49S](https://ui.adsabs.harvard.edu/abs/2000PNAS...97...49S). [doi](/source/Doi_(identifier)):[10.1073/pnas.97.1.49](https://doi.org/10.1073%2Fpnas.97.1.49). [PMC](/source/PMC_(identifier)) [26614](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC26614). [PMID](/source/PMID_(identifier)) [10618369](https://pubmed.ncbi.nlm.nih.gov/10618369).

1. **[^](#cite_ref-pmid11069186_19-0)** Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL (October 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". *Nature*. **407** (6807): 1029–34. [Bibcode](/source/Bibcode_(identifier)):[2000Natur.407.1029P](https://ui.adsabs.harvard.edu/abs/2000Natur.407.1029P). [doi](/source/Doi_(identifier)):[10.1038/35039551](https://doi.org/10.1038%2F35039551). [PMID](/source/PMID_(identifier)) [11069186](https://pubmed.ncbi.nlm.nih.gov/11069186). [S2CID](/source/S2CID_(identifier)) [4418272](https://api.semanticscholar.org/CorpusID:4418272).

1. **[^](#cite_ref-pmid10574949_20-0)** Chellaiah A, Yuan W, Chellaiah M, Ornitz DM (December 1999). ["Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity"](https://doi.org/10.1074%2Fjbc.274.49.34785). *The Journal of Biological Chemistry*. **274** (49): 34785–94. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.49.34785](https://doi.org/10.1074%2Fjbc.274.49.34785). [PMID](/source/PMID_(identifier)) [10574949](https://pubmed.ncbi.nlm.nih.gov/10574949).

1. **[^](#cite_ref-pmid10736564_21-0)** Loo BB, Darwish KK, Vainikka SS, Saarikettu JJ, Vihko PP, Hermonen JJ, Goldman AA, Alitalo KK, Jalkanen MM (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". *The International Journal of Biochemistry & Cell Biology*. **32** (5): 489–97. [doi](/source/Doi_(identifier)):[10.1016/S1357-2725(99)00145-4](https://doi.org/10.1016%2FS1357-2725%2899%2900145-4). [PMID](/source/PMID_(identifier)) [10736564](https://pubmed.ncbi.nlm.nih.gov/10736564).

1. **[^](#cite_ref-pmid10336501_22-0)** Kan M, Wu X, Wang F, McKeehan WL (May 1999). ["Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase"](https://doi.org/10.1074%2Fjbc.274.22.15947). *The Journal of Biological Chemistry*. **274** (22): 15947–52. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.22.15947](https://doi.org/10.1074%2Fjbc.274.22.15947). [PMID](/source/PMID_(identifier)) [10336501](https://pubmed.ncbi.nlm.nih.gov/10336501).

1. **[^](#cite_ref-pmid10510314_23-0)** Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (October 1999). ["Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220575). *The Biochemical Journal*. **343** (2): 461–6. [doi](/source/Doi_(identifier)):[10.1042/0264-6021:3430461](https://doi.org/10.1042%2F0264-6021%3A3430461). [PMC](/source/PMC_(identifier)) [1220575](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220575). [PMID](/source/PMID_(identifier)) [10510314](https://pubmed.ncbi.nlm.nih.gov/10510314).

1. ^ [***a***](#cite_ref-pmid9712836_24-0) [***b***](#cite_ref-pmid9712836_24-1) Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (August 1998). ["S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro"](https://doi.org/10.1074%2Fjbc.273.35.22224). *The Journal of Biological Chemistry*. **273** (35): 22224–31. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.35.22224](https://doi.org/10.1074%2Fjbc.273.35.22224). [hdl](/source/Hdl_(identifier)):[2158/26736](https://hdl.handle.net/2158%2F26736). [PMID](/source/PMID_(identifier)) [9712836](https://pubmed.ncbi.nlm.nih.gov/9712836).

1. **[^](#cite_ref-pmid11432880_25-0)** Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (July 2001). ["Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress"](https://doi.org/10.1074%2Fjbc.M102925200). *The Journal of Biological Chemistry*. **276** (27): 25549–57. [doi](/source/Doi_(identifier)):[10.1074/jbc.M102925200](https://doi.org/10.1074%2Fjbc.M102925200). [PMID](/source/PMID_(identifier)) [11432880](https://pubmed.ncbi.nlm.nih.gov/11432880).

## Further reading

- Yu YL, Kha H, Golden JA, Migchielsen AA, Goetzl EJ, Turck CW (April 1992). ["An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119192). *The Journal of Experimental Medicine*. **175** (4): 1073–80. [doi](/source/Doi_(identifier)):[10.1084/jem.175.4.1073](https://doi.org/10.1084%2Fjem.175.4.1073). [PMC](/source/PMC_(identifier)) [2119192](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119192). [PMID](/source/PMID_(identifier)) [1372643](https://pubmed.ncbi.nlm.nih.gov/1372643).

- Chiu IM, Wang WP, Lehtoma K (May 1990). "Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1". *Oncogene*. **5** (5): 755–62. [PMID](/source/PMID_(identifier)) [1693186](https://pubmed.ncbi.nlm.nih.gov/1693186).

- Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, Hsu BT, Rees DC (January 1991). "Three-dimensional structures of acidic and basic fibroblast growth factors". *Science*. **251** (4989): 90–3. [Bibcode](/source/Bibcode_(identifier)):[1991Sci...251...90Z](https://ui.adsabs.harvard.edu/abs/1991Sci...251...90Z). [doi](/source/Doi_(identifier)):[10.1126/science.1702556](https://doi.org/10.1126%2Fscience.1702556). [PMID](/source/PMID_(identifier)) [1702556](https://pubmed.ncbi.nlm.nih.gov/1702556).

- Wang WP, Quick D, Balcerzak SP, Needleman SW, Chiu IM (September 1991). "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients". *Oncogene*. **6** (9): 1521–9. [PMID](/source/PMID_(identifier)) [1717925](https://pubmed.ncbi.nlm.nih.gov/1717925).

- Wu DQ, Kan MK, Sato GH, Okamoto T, Sato JD (September 1991). ["Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors"](https://doi.org/10.1016%2FS0021-9258%2818%2955368-0). *The Journal of Biological Chemistry*. **266** (25): 16778–85. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)55368-0](https://doi.org/10.1016%2FS0021-9258%2818%2955368-0). [PMID](/source/PMID_(identifier)) [1885605](https://pubmed.ncbi.nlm.nih.gov/1885605).

- Crumley G, Dionne CA, Jaye M (August 1990). "The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon". *Biochemical and Biophysical Research Communications*. **171** (1): 7–13. [doi](/source/Doi_(identifier)):[10.1016/0006-291X(90)91348-V](https://doi.org/10.1016%2F0006-291X%2890%2991348-V). [PMID](/source/PMID_(identifier)) [2393407](https://pubmed.ncbi.nlm.nih.gov/2393407).

- Harper JW, Strydom DJ, Lobb RR (July 1986). "Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor". *Biochemistry*. **25** (14): 4097–103. [doi](/source/Doi_(identifier)):[10.1021/bi00362a017](https://doi.org/10.1021%2Fbi00362a017). [PMID](/source/PMID_(identifier)) [2427112](https://pubmed.ncbi.nlm.nih.gov/2427112).

- Winkles JA, Friesel R, Burgess WH, Howk R, Mehlman T, Weinstein R, Maciag T (October 1987). ["Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor)"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299242). *Proceedings of the National Academy of Sciences of the United States of America*. **84** (20): 7124–8. [Bibcode](/source/Bibcode_(identifier)):[1987PNAS...84.7124W](https://ui.adsabs.harvard.edu/abs/1987PNAS...84.7124W). [doi](/source/Doi_(identifier)):[10.1073/pnas.84.20.7124](https://doi.org/10.1073%2Fpnas.84.20.7124). [PMC](/source/PMC_(identifier)) [299242](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299242). [PMID](/source/PMID_(identifier)) [2444975](https://pubmed.ncbi.nlm.nih.gov/2444975).

- Wang WP, Lehtoma K, Varban ML, Krishnan I, Chiu IM (June 1989). ["Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362312). *Molecular and Cellular Biology*. **9** (6): 2387–95. [doi](/source/Doi_(identifier)):[10.1128/mcb.9.6.2387](https://doi.org/10.1128%2Fmcb.9.6.2387). [PMC](/source/PMC_(identifier)) [362312](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362312). [PMID](/source/PMID_(identifier)) [2474753](https://pubmed.ncbi.nlm.nih.gov/2474753).

- Mergia A, Tischer E, Graves D, Tumolo A, Miller J, Gospodarowicz D, Abraham JA, Shipley GD, Fiddes JC (November 1989). "Structural analysis of the gene for human acidic fibroblast growth factor". *Biochemical and Biophysical Research Communications*. **164** (3): 1121–9. [doi](/source/Doi_(identifier)):[10.1016/0006-291X(89)91785-3](https://doi.org/10.1016%2F0006-291X%2889%2991785-3). [PMID](/source/PMID_(identifier)) [2590193](https://pubmed.ncbi.nlm.nih.gov/2590193).

- Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (July 1986). "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor". *Biochemical and Biophysical Research Communications*. **138** (2): 611–7. [doi](/source/Doi_(identifier)):[10.1016/S0006-291X(86)80540-X](https://doi.org/10.1016%2FS0006-291X%2886%2980540-X). [PMID](/source/PMID_(identifier)) [3527167](https://pubmed.ncbi.nlm.nih.gov/3527167).

- Gautschi P, Fràter-Schröder M, Böhlen P (August 1986). ["Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors"](https://doi.org/10.1016%2F0014-5793%2886%2980812-2). *FEBS Letters*. **204** (2): 203–7. [Bibcode](/source/Bibcode_(identifier)):[1986FEBSL.204..203G](https://ui.adsabs.harvard.edu/abs/1986FEBSL.204..203G). [doi](/source/Doi_(identifier)):[10.1016/0014-5793(86)80812-2](https://doi.org/10.1016%2F0014-5793%2886%2980812-2). [PMID](/source/PMID_(identifier)) [3732516](https://pubmed.ncbi.nlm.nih.gov/3732516). [S2CID](/source/S2CID_(identifier)) [22617694](https://api.semanticscholar.org/CorpusID:22617694).

- Gautschi-Sova P, Müller T, Böhlen P (November 1986). "Amino acid sequence of human acidic fibroblast growth factor". *Biochemical and Biophysical Research Communications*. **140** (3): 874–80. [doi](/source/Doi_(identifier)):[10.1016/0006-291X(86)90716-3](https://doi.org/10.1016%2F0006-291X%2886%2990716-3). [PMID](/source/PMID_(identifier)) [3778488](https://pubmed.ncbi.nlm.nih.gov/3778488).

- Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (March 1986). "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities". *Biochemical and Biophysical Research Communications*. **135** (2): 541–8. [doi](/source/Doi_(identifier)):[10.1016/0006-291X(86)90028-8](https://doi.org/10.1016%2F0006-291X%2886%2990028-8). [PMID](/source/PMID_(identifier)) [3964259](https://pubmed.ncbi.nlm.nih.gov/3964259).

- Zhao XM, Yeoh TK, Hiebert M, Frist WH, Miller GG (November 1993). ["The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells"](https://doi.org/10.1097%2F00007890-199311000-00025). *Transplantation*. **56** (5): 1177–82. [doi](/source/Doi_(identifier)):[10.1097/00007890-199311000-00025](https://doi.org/10.1097%2F00007890-199311000-00025). [PMID](/source/PMID_(identifier)) [7504343](https://pubmed.ncbi.nlm.nih.gov/7504343).

- Pineda-Lucena A, Jiménez MA, Nieto JL, Santoro J, Rico M, Giménez-Gallego G (September 1994). "1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate". *Journal of Molecular Biology*. **242** (1): 81–98. [doi](/source/Doi_(identifier)):[10.1006/jmbi.1994.1558](https://doi.org/10.1006%2Fjmbi.1994.1558). [PMID](/source/PMID_(identifier)) [7521397](https://pubmed.ncbi.nlm.nih.gov/7521397).

- Chotani MA, Payson RA, Winkles JA, Chiu IM (February 1995). ["Human fibroblast growth factor 1 gene expression in vascular smooth muscle cells is modulated via an alternate promoter in response to serum and phorbol ester"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC306694). *Nucleic Acids Research*. **23** (3): 434–41. [doi](/source/Doi_(identifier)):[10.1093/nar/23.3.434](https://doi.org/10.1093%2Fnar%2F23.3.434). [PMC](/source/PMC_(identifier)) [306694](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC306694). [PMID](/source/PMID_(identifier)) [7533902](https://pubmed.ncbi.nlm.nih.gov/7533902).

- Opalenik SR, Shin JT, Wehby JN, Mahesh VK, Thompson JA (July 1995). ["The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor"](https://doi.org/10.1074%2Fjbc.270.29.17457). *The Journal of Biological Chemistry*. **270** (29): 17457–67. [doi](/source/Doi_(identifier)):[10.1074/jbc.270.29.17457](https://doi.org/10.1074%2Fjbc.270.29.17457). [PMID](/source/PMID_(identifier)) [7542239](https://pubmed.ncbi.nlm.nih.gov/7542239).

- Myers RL, Payson RA, Chotani MA, Deaven LL, Chiu IM (February 1993). "Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts". *Oncogene*. **8** (2): 341–9. [PMID](/source/PMID_(identifier)) [7678925](https://pubmed.ncbi.nlm.nih.gov/7678925).

v t e PDB gallery 1afc: STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR 1axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR 1bar: THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST GROWTH FACTORS 1djs: LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1 1dzc: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR. MUTANT FGF-4-ALA-(23-154), 24 NMR STRUCTURES 1dzd: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR (27-154), 24 NMR STRUCTURES 1e0o: CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX 1evt: CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1) 1hkn: A COMPLEX BETWEEN ACIDIC FIBROBLAST GROWTH FACTOR AND 5-AMINO-2-NAPHTHALENESULFONATE 1jqz: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag. 1jt3: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Histidine Tag AND LEU 73 REPLACED BY VAL (L73V) 1jt4: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND VAL 109 REPLACED BY LEU (V109L) 1jt5: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L73V/V109L) 1jt7: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L44F/L73V/V109L) 1jtc: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE (L44F) 1jy0: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag and Cys 117 replaced with Val (C117V). 1k5u: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G). 1k5v: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G). 1m16: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V). 1nzk: Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic Fibroblast Growth Factor 1p63: Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I) 1pzz: Crystal structure of FGF-1, V51N mutant 1q03: Crystal structure of FGF-1, S50G/V51G mutant 1q04: Crystal structure of FGF-1, S50E/V51N 1rg8: Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form) 1rml: NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHALENE TRISULPHONATE, 26 STRUCTURES 1ry7: Crystal Structure of the 3 Ig form of FGFR3c in complex with FGF1 1yto: Crystal Structure of Gly19 deletion Mutant of Human Acidic Fibroblast Growth Factor 1z2v: Crystal Structure of Glu60 deletion Mutant of Human Acidic Fibroblast Growth Factor 1z4s: Crystal Structure of Gly19 and Glu60 deletion mutant of Human Acidic Fibroblast Growth Factor 2afg: 2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR 2aqz: Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant 2axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR 2erm: Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue 2j3p: CRYSTAL STRUCTURE OF RAT FGF1 AT 1.4 A

v t e Growth factors Fibroblast FGF receptor ligands: FGF1/FGF2/FGF5 FGF3/FGF4/FGF6 KGF FGF7/FGF10/FGF22 FGF8/FGF17/FGF18 FGF9/FGF16/FGF20 FGF homologous factors: FGF11(FHF3) FGF12(FHF1) FGF13(FHF2) FGF14(FHF4) hormone-like: FGF15/19 FGF15 FGF19 FGF21 FGF23 EGF-like domain TGFα EGF HB-EGF TGFβ pathway TGFβ TGFβ1 TGFβ2 TGFβ3 Insulin/IGF/ Relaxin family Insulin and Insulin-like growth factor IGF1 IGF2 Relaxin family peptide hormones INSL3 INSL4 INSL5 INSL6 Relaxin 1 2 3 Platelet-derived PDGFA PDGFB PDGFC PDGFD Vascular endothelial VEGF-A VEGF-B VEGF-C VEGF-D PGF Other Nerve Hepatocyte

v t e Intercellular signaling peptides and proteins / ligands Growth factors Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily Vascular endothelial growth factor Ephrin EFNA1 EFNA2 EFNA3 EFNA4 EFNA5 EFNB1 EFNB2 EFNB3 Other Adipokine Agouti-related peptide Agouti-signaling protein Angiogenic protein CCN intercellular signaling protein Cysteine-rich protein 61 Connective tissue growth factor Nephroblastoma overexpressed protein Cytokine Endothelin EDN1 EDN2 EDN3 Hedgehog protein Interferon Kinin Parathyroid hormone-related protein Semaphorin Somatomedin Tolloid-like metalloproteinase Tumor necrosis factor Wnt protein see also extracellular ligand disorders

v t e Growth factor receptor modulators Angiopoietin Agonists: Angiopoietin 1 Angiopoietin 4 Antagonists: Angiopoietin 2 Angiopoietin 3 Kinase inhibitors: Altiratinib CE-245677 Rebastinib Antibodies: Evinacumab (against angiopoietin 3) Nesvacumab (against angiopoietin 2) CNTF Agonists: Axokine CNTF Dapiclermin EGF (ErbB) EGF (ErbB1/HER1) Agonists: Amphiregulin Betacellulin EGF (urogastrone) Epigen Epiregulin Heparin-binding EGF-like growth factor (HB-EGF) Murodermin Nepidermin Transforming growth factor alpha (TGFα) Kinase inhibitors: Afatinib Agerafenib Brigatinib Canertinib Dacomitinib Erlotinib Gefitinib Grandinin Icotinib Lapatinib Neratinib Osimertinib Vandetanib WHI-P 154 Antibodies: Cetuximab Depatuxizumab Depatuxizumab mafodotin Futuximab Imgatuzumab Matuzumab Necitumumab Nimotuzumab Panitumumab Zalutumumab ErbB2/HER2 Agonists: Unknown/none Antibodies: Ertumaxomab Pertuzumab Trastuzumab Trastuzumab deruxtecan Trastuzumab duocarmazine Trastuzumab emtansine Kinase inhibitors: Afatinib Lapatinib Mubritinib Neratinib Tucatinib ErbB3/HER3 Agonists: Neuregulins (heregulins) (1, 2, 6 (neuroglycan C)) Antibodies: Duligotuzumab Patritumab Seribantumab ErbB4/HER4 Agonists: Betacellulin Epigen Heparin-binding EGF-like growth factor (HB-EGF) Neuregulins (heregulins) (1, 2, 3, 4, 5 (tomoregulin, TMEFF)) FGF FGFR1 Agonists: Ersofermin FGF (1, 2 (bFGF), 3, 4, 5, 6, 8, 10 (KGF2), 20) Repifermin Selpercatinib Trafermin Velafermin FGFR2 Agonists: Ersofermin FGF (1, 2 (bFGF), 3, 4, 5, 6, 7 (KGF), 8, 9, 10 (KGF2), 17, 18, 22) Palifermin Repifermin Selpercatinib Sprifermin Trafermin Antibodies: Aprutumab Aprutumab ixadotin Kinase inhibitors: Infigratinib FGFR3 Agonists: Ersofermin FGF (1, 2 (bFGF), 4, 8, 9, 18, 23) Selpercatinib Sprifermin Trafermin Antibodies: Burosumab (against FGF23) FGFR4 Agonists: Ersofermin FGF (1, 2 (bFGF), 4, 6, 8, 9, 19) Trafermin Unsorted Agonists: FGF15/19 HGF (c-Met) Agonists: Fosgonimeton Hepatocyte growth factor Potentiators: Dihexa (PNB-0408) Kinase inhibitors: Altiratinib AM7 AMG-458 Amuvatinib BMS-777607 Cabozantinib Capmatinib Crizotinib Foretinib Golvatinib INCB28060 JNJ-38877605 K252a MK-2461 PF-04217903 PF-2341066 PHA-665752 Savolitinib SU-11274 Tivantinib Antibodies: Emibetuzumab Ficlatuzumab Flanvotumab Onartuzumab Rilotumumab Telisotuzumab Telisotuzumab vedotin IGF IGF-1 Agonists: des(1-3)IGF-1 Insulin-like growth factor-1 (somatomedin C) IGF-1 LR3 Insulin-like growth factor-2 (somatomedin A) Insulin Mecasermin Mecasermin rinfabate Kinase inhibitors: BMS-754807 Linsitinib NVP-ADW742 NVP-AEW541 OSl-906 Antibodies: AVE-1642 Cixutumumab Dalotuzumab Figitumumab Ganitumab Robatumumab R1507 Teprotumumab Xentuzumab (against IGF-1 and IGF-2) IGF-2 Agonists: Insulin-like growth factor-2 (somatomedin A) Antibodies: Dusigitumab Xentuzumab (against IGF-1 and IGF-2) Others Binding proteins: IGFBP (1, 2, 3, 4, 5, 6, 7) Cleavage products/derivatives with unknown target: Glypromate (GPE, (1-3)IGF-1) Trofinetide LNGF (p75NTR) Agonists: BDNF BNN-20 BNN-27 Cenegermin DHEA DHEA-S NGF NT-3 NT-4 Antagonists: ALE-0540 Dexamethasone EVT-901 (SAR-127963) Testosterone Antibodies: Against NGF: ABT-110 (PG110) ASP-6294 Fasinumab Frunevetmab Fulranumab MEDI-578 Ranevetmab Tanezumab Aptamers: Against NGF: RBM-004 Decoy receptors: LEVI-04 (p75NTR-Fc) PDGF Agonists: Becaplermin Platelet-derived growth factor (A, B, C, D) Kinase inhibitors: Agerafenib Avapritinib Axitinib Crenolanib Imatinib Lenvatinib Masitinib Motesanib Nintedanib Pazopanib Radotinib Quizartinib Ripretinib Sunitinib Sorafenib Toceranib Antibodies: Olaratumab Ramucirumab Tovetumab RET (GFL) GFRα1 Agonists: Glial cell line-derived neurotrophic factor (GDNF) Liatermin Kinase inhibitors: Vandetanib GFRα2 Agonists: Neurturin (NRTN) Kinase inhibitors: Vandetanib GFRα3 Agonists: Artemin (ARTN) Kinase inhibitors: Vandetanib GFRα4 Agonists: Persephin (PSPN) Kinase inhibitors: Vandetanib Unsorted Kinase inhibitors: Agerafenib SCF (c-Kit) Agonists: Ancestim Stem cell factor Kinase inhibitors: Agerafenib Axitinib Dasatinib Imatinib Masitinib Nilotinib Pazopanib Quizartinib Sorafenib Sunitinib Toceranib TGFβ See here instead. Trk TrkA Agonists: Amitriptyline BNN-20 BNN-27 Cenegermin DHEA DHEA-S Gambogic amide NGF Tavilermide Antagonists: ALE-0540 Dexamethasone FX007 Testosterone Positive allosteric modulators: AC26845 (AC‑0026845) ACD856 ACD857 E2511 Ponazuril (ACD855) Toltrazuril Negative allosteric modulators: VM-902A Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib Milciclib ONO-4474 ONO-5390556 PLX-7486 Rebastinib SNA-120 (pegylated K252a)) Antibodies: Against TrkA: GBR-900; Against NGF: ABT-110 (PG110) ASP-6294 Fasinumab Frunevetmab Fulranumab MEDI-578 Ranevetmab Tanezumab Aptamers: Against NGF: RBM-004 Decoy receptors: ReN-1820 (TrkAd5) TrkB Agonists: 3,7-DHF 3,7,8,2'-THF 4'-DMA-7,8-DHF 7,3'-DHF 7,8-DHF 7,8,2'-THF 7,8,3'-THF Amitriptyline Braegen-02 BDNF BNN-20 Deoxygedunin Diosmetin DMAQ-B1 HIOC LM22A-4 N-Acetylserotonin NT-3 NT-4 Norwogonin (5,7,8-THF) R7 R13 (BrAD-R13, Braegen-01) SPV-400 TDP6 Antagonists: ANA-12 Cyclotraxin B Gossypetin (3,5,7,8,3',4'-HHF) Ligands: DHEA Positive allosteric modulators: AC26845 (AC‑0026845) ACD856 ACD857 Ponazuril (ACD855) Toltrazuril Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib ONO-4474 ONO-5390556 PLX-7486 TrkC Agonists: BNN-20 DHEA NT-3 Positive allosteric modulators: AC26845 (AC‑0026845) ACD856 Kinase inhibitors: Altiratinib AZD-6918 CE-245677 CH-7057288 DS-6051 Entrectinib GZ-389988 K252a Larotrectinib Lestaurtinib ONO-4474 ONO-5390556 PLX-7486 VEGF Agonists: Placental growth factor (PGF) Ripretinib Telbermin VEGF (A, B, C, D (FIGF)) Allosteric modulators: Cyclotraxin B Kinase inhibitors: Agerafenib Altiratinib Axitinib Cabozantinib Cediranib Fruquintinib Lapatinib Lenvatinib Motesanib Nintedanib Pazopanib Pegaptanib Rebastinib Regorafenib Semaxanib Sorafenib Sunitinib Toceranib Tivozanib Vandetanib WHI-P 154 Antibodies: Alacizumab pegol Bevacizumab Icrucumab Ramucirumab Ranibizumab Decoy receptors: Aflibercept Others Additional growth factors: Adrenomedullin Colony-stimulating factors (see here instead) Connective tissue growth factor (CTGF) Ephrins (A1, A2, A3, A4, A5, B1, B2, B3) Erythropoietin (see here instead) Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF) Glia maturation factor (GMF) Hepatoma-derived growth factor (HDGF) Interleukins/T-cell growth factors (see here instead) Leukemia inhibitory factor (LIF) Macrophage-stimulating protein (MSP; HLP, HGFLP) Midkine (NEGF2) Migration-stimulating factor (MSF; PRG4) Oncomodulin Pituitary adenylate cyclase-activating peptide (PACAP) Pleiotrophin Renalase Thrombopoietin (see here instead) Wnt signaling proteins Additional growth factor receptor modulators: Cerebrolysin (neurotrophin mixture)

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Adapted from the Wikipedia article [Fibroblast growth factor 1](https://en.wikipedia.org/wiki/Fibroblast_growth_factor_1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Fibroblast_growth_factor_1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.