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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/01 12:37:38」(JST)

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

Function

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]

Interactions

FGF1 has been shown to interact with:

CSNK2A2,^[5]
CSNK2B,^[5]
CSNK2A1,^[5]
FIBP,^[6]
FGFR1,^[7]^[8]
FGFR2^[8]^[9]^[10]
FGFR3,^[8]^[11]
FGFR4,^[12]^[13]
HSPA9,^[14] and
S100A13.^[15]^[16]

References

^ 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.
^ 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.
^ "Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)".
^ 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 summary – Salk Institute.
^ ^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.
^ 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.
^ 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.
^ ^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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.

UpToDate Contents

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English Journal

Therapeutic foam scaffolds incorporating biopolymer-shelled mesoporous nanospheres with growth factors.

Kim TH1, Eltohamy M1, Kim M1, Perez RA1, Kim JH1, Yun YR1, Jang JH2, Lee EJ1, Knowles JC3, Kim HW4.
Acta biomaterialia.Acta Biomater.2014 Jun;10(6):2612-21. doi: 10.1016/j.actbio.2014.02.005. Epub 2014 Feb 11.
A novel therapeutic scaffolding system of engineered nanocarriers within a foam matrix for the long-term and sequential delivery of growth factors is reported. Mesoporous silica nanospheres were first functionalized to have an enlarged mesopore size (12.2nm) and aminated surface, which was then shel
PMID 24530558

Development and application of site mapping methods for the design of glycosaminoglycans.

Agostino M1, Gandhi NS1, Mancera RL2.
Glycobiology.Glycobiology.2014 May 23. pii: cwu045. [Epub ahead of print]
Glycosaminoglycans (GAGs) are complex polysaccharides involved in a wide range of biological signaling events, as well as being important as biological structural materials. Despite the ubiquity and importance of GAG-protein interactions in biological systems and potentially as therapeutic targets,
PMID 24859723

Proteome array identification of bioactive soluble proteins/peptides in Matrigel: relevance to stem cell responses.

Talbot NC1, Caperna TJ.
Cytotechnology.Cytotechnology.2014 Apr 18. [Epub ahead of print]
Matrigel and similar commercial products are extracts of the Engelbreth-Holm-Swarm sarcoma that provide a basement-membrane-like attachment substrate or gel that is used to grow cells on or in, respectively. To ascertain further what proteins may be present in Matrigel, besides its major basement-me
PMID 24744128

Japanese Journal

3P-1177 CORYNEX(R)を用いた活性型ヒトaFGF及びbFGFの高分泌生産(6a生物化学工学,一般講演,生物化学工学,伝統の技と先端科学技術の融合)

別府春樹,竹中康浩,吉良郁夫,菊池慶実
日本生物工学会大会講演要旨集平成22年度, 102, 2010-09-25
NAID 110008084733

Combined Use of Acid Fibroblast Growth Factor, Granulocyte Colony-stimulating Factor and Zinc Sulphate Accelerates Diabetic Ulcer Healing

Lin Shaoqiang,Xu Hengwu,Xiao Jian [他],Liu Yanlong,Zhang Yi,Cai Lu,Li Xiaokun,Tan Yi
JOURNAL OF HEALTH SCIENCE 55(6), 910-922, 2009
… Our previous studies demonstrated that topic application of recombinant human acid fibroblast growth factor (aFGF) significantly, but still not completely, improved in diabetic ulcer healing. … To obtain a maximal therapy for diabetic ulcer healing, a combined protocol containing aFGF, anti-oxidative reagent zinc (Zn) and stem cell stimulator granulocyte colony-stimulating factor (G-CSF), i.e.: aFGF/G-CSF/zinc sulphate (ZnSO4), was explored in the present study. …
NAID 130000127987

Co-expression of aFGF and FGFR-1 is predictive of a poor prognosis in patients with esophageal squamous cell carcinoma

杉浦功一
慶應医学 84(2), 56, 2007-06-00
号外
NAID 120000801952

Related Pictures

★リンクテーブル★

リンク元	「酸性線維芽細胞成長因子」「acidic fibroblast growth factor」
関連記事	「aF」

「酸性線維芽細胞成長因子」

Fibroblast growth factor 1 (acidic)
	PDB rendering based on 1afc.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1AXM, 1DJS, 1DZC, 1DZD, 1E0O, 1EVT, 1HKN, 1JQZ, 1JT3, 1JT4, 1JT5, 1JT7, 1JTC, 1JY0, 1K5U, 1K5V, 1M16, 1NZK, 1P63, 1PZZ, 1Q03, 1Q04, 1QCT, 1RG8, 1RML, 1RY7, 1YTO, 1Z2V, 1Z4S, 2AFG, 2AQZ, 2AXM, 2ERM, 2HW9, 2HWA, 2HWM, 2HZ9, 2K43, 2K4A, 2K8R, 2KI4, 2KI6, 2LDN, 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, 4QO3
Identifiers
Symbols	FGF1 ; AFGF; ECGF; ECGF-beta; ECGFA; ECGFB; FGF-1; FGF-alpha; FGFA; GLIO703; HBGF-1; HBGF1
External IDs	OMIM: 131220 MGI: 95515 HomoloGene: 625 ChEMBL: 2120 GeneCards: FGF1 Gene
Gene ontology
Molecular function	• fibroblast growth factor receptor binding; • protein binding; • growth factor activity; • heparin binding; • S100 protein binding;
Cellular component	• extracellular region; • proteinaceous extracellular matrix; • extracellular space; • nucleoplasm; • cytosol; • cell cortex;
Biological process	• angiogenesis; • organ induction; • signal transduction; • epidermal growth factor receptor signaling pathway; • multicellular organismal development; • positive regulation of cell proliferation; • insulin receptor signaling pathway; • fibroblast growth factor receptor signaling pathway; • anatomical structure morphogenesis; • lung development; • positive regulation of cell migration; • cellular response to heat; • Fc-epsilon receptor signaling pathway; • positive regulation of MAP kinase activity; • innate immune response; • positive regulation of cholesterol biosynthetic process; • positive regulation of angiogenesis; • positive regulation of transcription from RNA polymerase II promoter; • neurotrophin TRK receptor signaling pathway; • phosphatidylinositol-mediated signaling; • positive regulation of epithelial cell proliferation; • positive regulation of cell division; • branch elongation involved in ureteric bud branching; • positive regulation of ERK1 and ERK2 cascade; • mesonephric epithelium development; • positive regulation of intracellular signal transduction; • regulation of endothelial cell chemotaxis to fibroblast growth factor;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;