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This article is about fibroblast growth factor-1. For the internal ribosome entry site, see FGF-1 internal ribosome entry site (IRES).
Fibroblast growth factor 1 (acidic)
Protein FGF1 PDB 1afc.png
PDB rendering based on 1afc.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols FGF1 ; AFGF; ECGF; ECGF-beta; ECGFA; ECGFB; FGF-1; FGF-alpha; FGFA; GLIO703; HBGF-1; HBGF1
External IDs OMIM131220 MGI95515 HomoloGene625 ChEMBL: 2120 GeneCards: FGF1 Gene
RNA expression pattern
PBB GE FGF1 205117 at tn.png
PBB GE FGF1 208240 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2246 14164
Ensembl ENSG00000113578 ENSMUSG00000036585
UniProt P05230 P61148
RefSeq (mRNA) NM_000800 NM_010197
RefSeq (protein) NP_000791 NP_034327
Location (UCSC) Chr 5:
142.59 – 142.7 Mb
Chr 18:
38.84 – 38.93 Mb
PubMed search [1] [2]

Heparin-binding growth factor 1 is a protein that in humans is encoded by the FGF1 gene.[1][2]


The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, 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- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described.[3]

In mice with diet-induced diabetes, the equivalent of type 2 diabetes in humans, a single injection of the protein FGF1 is enough to restore blood sugar levels to a healthy range for > 2 days.[4]


FGF1 has been shown to interact with:

See also[edit]


  1. ^ Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (Sep 1990). "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors". The EMBO Journal 9 (9): 2685–92. PMC 551973. PMID 1697263. 
  2. ^ Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN (Aug 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". Science 233 (4763): 541–5. doi:10.1126/science.3523756. PMID 3523756. 
  3. ^ "Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)". 
  4. ^ 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 (Sep 2014). "Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer". Nature 513 (7518): 436–9. doi:10.1038/nature13540. PMID 25043058. Lay summarySalk Institute. 
  5. ^ a b c Skjerpen CS, Nilsen T, Wesche J, Olsnes S (Aug 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". The EMBO Journal 21 (15): 4058–69. doi:10.1093/emboj/cdf402. PMC 126148. PMID 12145206. 
  6. ^ Kolpakova E, Wiedłocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S (Nov 1998). "Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor". The Biochemical Journal 336 (1): 213–22. doi:10.1042/bj3360213. PMC 1219860. PMID 9806903. 
  7. ^ Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M (Sep 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Molecular Cell 6 (3): 743–50. doi:10.1016/s1097-2765(00)00073-3. PMID 11030354. 
  8. ^ a b c Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM (Jan 1996). "Expression and biological activity of mouse fibroblast growth factor-9". The Journal of Biological Chemistry 271 (3): 1726–31. doi:10.1074/jbc.271.3.1726. PMID 8576175. 
  9. ^ Stauber DJ, DiGabriele AD, Hendrickson WA (Jan 2000). "Structural interactions of fibroblast growth factor receptor with its ligands". Proceedings of the National Academy of Sciences of the United States of America 97 (1): 49–54. doi:10.1073/pnas.97.1.49. PMC 26614. PMID 10618369. 
  10. ^ Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL (Oct 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". Nature 407 (6807): 1029–34. doi:10.1038/35039551. PMID 11069186. 
  11. ^ Chellaiah A, Yuan W, Chellaiah M, Ornitz DM (Dec 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". The Journal of Biological Chemistry 274 (49): 34785–94. doi:10.1074/jbc.274.49.34785. PMID 10574949. 
  12. ^ 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:10.1016/S1357-2725(99)00145-4. PMID 10736564. 
  13. ^ 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". The Journal of Biological Chemistry 274 (22): 15947–52. doi:10.1074/jbc.274.22.15947. PMID 10336501. 
  14. ^ Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (Oct 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". The Biochemical Journal 343 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314. 
  15. ^ Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (Aug 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". The Journal of Biological Chemistry 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. PMID 9712836. 
  16. ^ Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (Jul 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". The Journal of Biological Chemistry 276 (27): 25549–57. doi:10.1074/jbc.M102925200. PMID 11432880. 

Further reading[edit]