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]
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↑ 8.08.18.2Santos-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. PMID8576175.
↑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. PMID11069186.
↑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. PMID10574949.
↑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. PMID10736564.
↑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. PMID10336501.
↑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. PMID9712836.
↑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. PMID11432880.
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Wang WP, Quick D, Balcerzak SP, Needleman SW, Chiu IM (Sep 1991). "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients". Oncogene. 6 (9): 1521–9. PMID1717925.
Wu DQ, Kan MK, Sato GH, Okamoto T, Sato JD (Sep 1991). "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors". The Journal of Biological Chemistry. 266 (25): 16778–85. PMID1885605.
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Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (Jul 1986). "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor". Biochemical and Biophysical Research Communications. 138 (2): 611–7. doi:10.1016/S0006-291X(86)80540-X. PMID3527167.
Gautschi P, Fràter-Schröder M, Böhlen P (Aug 1986). "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors". FEBS Letters. 204 (2): 203–7. doi:10.1016/0014-5793(86)80812-2. PMID3732516.
Gautschi-Sova P, Müller T, Böhlen P (Nov 1986). "Amino acid sequence of human acidic fibroblast growth factor". Biochemical and Biophysical Research Communications. 140 (3): 874–80. doi:10.1016/0006-291X(86)90716-3. PMID3778488.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (Mar 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:10.1016/0006-291X(86)90028-8. PMID3964259.
Zhao XM, Yeoh TK, Hiebert M, Frist WH, Miller GG (Nov 1993). "The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells". Transplantation. 56 (5): 1177–82. doi:10.1097/00007890-199311000-00025. PMID7504343.
Pineda-Lucena A, Jiménez MA, Nieto JL, Santoro J, Rico M, Giménez-Gallego G (Sep 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:10.1006/jmbi.1994.1558. PMID7521397.
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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)
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).