FGF1

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Fibroblast growth factor 1 (acidic)
Protein FGF1 PDB 1afc.png
PDB rendering based on 1afc.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
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
Orthologs
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:
141.97 – 142.08 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]

Interactions[edit]

FGF1 has been shown to interact with CSNK2B,[4] CSNK2A2,[4] HSPA9,[5] S100A13,[6][7] Casein kinase 2, alpha 1,[4] Fibroblast growth factor receptor 1,[8][9] FIBP,[10] Fibroblast growth factor receptor 4,[11][12] Fibroblast growth factor receptor 2[9][13][14] and Fibroblast growth factor receptor 3.[9][15]

See also[edit]

References[edit]

  1. ^ Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (October 1990). "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors". EMBO J 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 (August 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. ^ a b c Skjerpen, Camilla Skiple; Nilsen Trine; Wesche Jørgen; Olsnes Sjur (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. (England) 21 (15): 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206. 
  5. ^ Mizukoshi, E; Suzuki M; Loupatov A; Uruno T; Hayashi H; Misono T; Kaul S C; Wadhwa R; Imamura T (October 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. (ENGLAND) 343 (2): 461–6. doi:10.1042/0264-6021:3430461. ISSN 0264-6021. PMC 1220575. PMID 10510314. 
  6. ^ Mouta Carreira, C; LaVallee T M; Tarantini F; Jackson A; Lathrop J T; Hampton B; Burgess W H; Maciag T (August 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". J. Biol. Chem. (UNITED STATES) 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. ISSN 0021-9258. PMID 9712836. 
  7. ^ 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". J. Biol. Chem. (United States) 276 (27): 25549–57. doi:10.1074/jbc.M102925200. ISSN 0021-9258. PMID 11432880. 
  8. ^ Schlessinger, J; Plotnikov A N; Ibrahimi O A; Eliseenkova A V; Yeh B K; Yayon A; Linhardt R J; Mohammadi M (September 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Mol. Cell (UNITED STATES) 6 (3): 743–50. doi:10.1016/S1097-2765(00)00073-3. ISSN 1097-2765. PMID 11030354. 
  9. ^ a b c Santos-Ocampo, S; Colvin J S; Chellaiah A; Ornitz D M (January 1996). "Expression and biological activity of mouse fibroblast growth factor-9". J. Biol. Chem. (UNITED STATES) 271 (3): 1726–31. doi:10.1074/jbc.271.3.1726. ISSN 0021-9258. PMID 8576175. 
  10. ^ Kolpakova, E; Wiedłocha A; Stenmark H; Klingenberg O; Falnes P O; Olsnes S (November 1998). "Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor". Biochem. J. (ENGLAND) 336 (Pt 1): 213–22. ISSN 0264-6021. PMC 1219860. PMID 9806903. 
  11. ^ Loo, B B; Darwish K K; Vainikka S S; Saarikettu J J; Vihko P P; Hermonen J J; Goldman A A; Alitalo K K; Jalkanen M M (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". Int. J. Biochem. Cell Biol. (ENGLAND) 32 (5): 489–97. doi:10.1016/S1357-2725(99)00145-4. ISSN 1357-2725. PMID 10736564. 
  12. ^ Kan, M; Wu X; Wang F; McKeehan W L (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". J. Biol. Chem. (UNITED STATES) 274 (22): 15947–52. doi:10.1074/jbc.274.22.15947. ISSN 0021-9258. PMID 10336501. 
  13. ^ Stauber, D J; DiGabriele A D; Hendrickson W A (January 2000). "Structural interactions of fibroblast growth factor receptor with its ligands". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (1): 49–54. doi:10.1073/pnas.97.1.49. ISSN 0027-8424. PMC 26614. PMID 10618369. 
  14. ^ Pellegrini, L; Burke D F; von Delft F; Mulloy B; Blundell T L (October 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". Nature (ENGLAND) 407 (6807): 1029–34. doi:10.1038/35039551. ISSN 0028-0836. PMID 11069186. 
  15. ^ Chellaiah, A; Yuan W; Chellaiah M; Ornitz D M (December 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". J. Biol. Chem. (UNITED STATES) 274 (49): 34785–94. doi:10.1074/jbc.274.49.34785. ISSN 0021-9258. PMID 10574949. 

Further reading[edit]