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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{about|fibroblast growth factor-1|the internal ribosome entry site|FGF-1 internal ribosome entry site (IRES)}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Heparin-binding growth factor 1''' is a [[protein]] that in humans is encoded by the ''FGF1'' [[gene]].<ref name="pmid1697263">{{cite journal | vauthors = Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J | title = Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors | journal = The EMBO Journal | volume = 9 | issue = 9 | pages = 2685–92 | date = Sep 1990 | pmid = 1697263 | pmc = 551973 | doi =  }}</ref><ref name="pmid3523756">{{cite journal | vauthors = Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN | title = Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization | journal = Science | volume = 233 | issue = 4763 | pages = 541–5 | date = Aug 1986 | pmid = 3523756 | pmc = | doi = 10.1126/science.3523756 }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_FGF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1afc.
| PDB = {{PDB2|1afc}}, {{PDB2|1axm}}, {{PDB2|1bar}}, {{PDB2|1djs}}, {{PDB2|1dzc}}, {{PDB2|1dzd}}, {{PDB2|1e0o}}, {{PDB2|1evt}}, {{PDB2|1hkn}}, {{PDB2|1jqz}}, {{PDB2|1jt3}}, {{PDB2|1jt4}}, {{PDB2|1jt5}}, {{PDB2|1jt7}}, {{PDB2|1jtc}}, {{PDB2|1jy0}}, {{PDB2|1k5u}}, {{PDB2|1k5v}}, {{PDB2|1m16}}, {{PDB2|1nzk}}, {{PDB2|1p63}}, {{PDB2|1pzz}}, {{PDB2|1q03}}, {{PDB2|1q04}}, {{PDB2|1rg8}}, {{PDB2|1rml}}, {{PDB2|1ry7}}, {{PDB2|1yto}}, {{PDB2|1z2v}}, {{PDB2|1z4s}}, {{PDB2|2afg}}, {{PDB2|2aqz}}, {{PDB2|2axm}}, {{PDB2|2erm}}, {{PDB2|2j3p}}
| Name = Fibroblast growth factor 1 (acidic)
| HGNCid = 3665
| Symbol = FGF1
| AltSymbols =; AFGF; ECGF; ECGF-beta; ECGFA; ECGFB; FGF-alpha; FGFA; GLIO703; HBGF1
| OMIM = 131220
| ECnumber = 
| Homologene = 625
| MGIid = 95515
| GeneAtlas_image1 = PBB_GE_FGF1_205117_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGF1_208240_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001759 |text = induction of an organ}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030324 |text = lung development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2246
    | Hs_Ensembl = ENSG00000113578
    | Hs_RefseqProtein = NP_000791
    | Hs_RefseqmRNA = NM_000800
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 141951927
    | Hs_GenLoc_end = 142046134
    | Hs_Uniprot = P05230
    | Mm_EntrezGene = 14164
    | Mm_Ensembl = ENSMUSG00000036585
    | Mm_RefseqmRNA = NM_010197
    | Mm_RefseqProtein = NP_034327
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 38965154
    | Mm_GenLoc_end = 39044673
    | Mm_Uniprot = Q6ZWS1
  }}
}}
'''Fibroblast growth factor 1 (acidic)''', also known as '''FGF1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref>{{cite web | title = Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2246| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2246| accessdate = }}</ref>
}}


==See also==
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.<ref>{{cite journal | vauthors = 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 | title = Endocrinization of FGF1 produces a neomorphic and potent insulin sensitizer | journal = Nature | volume = 513 | issue = 7518 | date = Sep 2014 | pmid = 25043058 | doi = 10.1038/nature13540 | laysummary = http://www.salk.edu/news/pressrelease_details.php?press_id=2037 | laysource = Salk Institute | pages=436–9 | pmc=4184286}}</ref>
 
== Interactions ==
 
FGF1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[CSNK2A2]],<ref name = pmid12145206/>
* [[CSNK2B]],<ref name = pmid12145206>{{cite journal | vauthors = Skjerpen CS, Nilsen T, Wesche J, Olsnes S | title = Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity | journal = The EMBO Journal | volume = 21 | issue = 15 | pages = 4058–69 | date = Aug 2002 | pmid = 12145206 | pmc = 126148 | doi = 10.1093/emboj/cdf402 }}</ref>
* [[Casein kinase 2, alpha 1|CSNK2A1]],<ref name = pmid12145206/>
* [[FIBP]],<ref name = pmid9806903>{{cite journal | vauthors = Kolpakova E, Wiedłocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S | title = Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor | journal = The Biochemical Journal | volume = 336 | issue = 1 | pages = 213–22 | date = Nov 1998 | pmid = 9806903 | pmc = 1219860 | doi =  10.1042/bj3360213}}</ref>
* [[Fibroblast growth factor receptor 1|FGFR1]],<ref name = pmid11030354>{{cite journal | vauthors = Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M | title = Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization | journal = Molecular Cell | volume = 6 | issue = 3 | pages = 743–50 | date = Sep 2000 | pmid = 11030354 | doi = 10.1016/s1097-2765(00)00073-3 }}</ref><ref name = pmid8576175>{{cite journal | vauthors = Santos-Ocampo S, Colvin JS, Chellaiah A, Ornitz DM | title = Expression and biological activity of mouse fibroblast growth factor-9 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 3 | pages = 1726–31 | date = Jan 1996 | pmid = 8576175 | doi = 10.1074/jbc.271.3.1726 }}</ref>
* [[Fibroblast growth factor receptor 2|FGFR2]]<ref name = pmid8576175/><ref name = pmid10618369>{{cite journal | vauthors = Stauber DJ, DiGabriele AD, Hendrickson WA | title = Structural interactions of fibroblast growth factor receptor with its ligands | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 1 | pages = 49–54 | date = Jan 2000 | pmid = 10618369 | pmc = 26614 | doi = 10.1073/pnas.97.1.49 }}</ref><ref name = pmid11069186>{{cite journal | vauthors = Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL | title = Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin | journal = Nature | volume = 407 | issue = 6807 | pages = 1029–34 | date = Oct 2000 | pmid = 11069186 | doi = 10.1038/35039551 }}</ref>
* [[Fibroblast growth factor receptor 3|FGFR3]],<ref name = pmid8576175/><ref name = pmid10574949>{{cite journal | vauthors = Chellaiah A, Yuan W, Chellaiah M, Ornitz DM | title = Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity | journal = The Journal of Biological Chemistry | volume = 274 | issue = 49 | pages = 34785–94 | date = Dec 1999 | pmid = 10574949 | doi = 10.1074/jbc.274.49.34785 }}</ref>
* [[Fibroblast growth factor receptor 4|FGFR4]],<ref name = pmid10736564>{{cite journal | vauthors = Loo BB, Darwish KK, Vainikka SS, Saarikettu JJ, Vihko PP, Hermonen JJ, Goldman AA, Alitalo KK, Jalkanen MM | title = Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4 | journal = The International Journal of Biochemistry & Cell Biology | volume = 32 | issue = 5 | pages = 489–97 | date = May 2000 | pmid = 10736564 | doi = 10.1016/S1357-2725(99)00145-4 }}</ref><ref name = pmid10336501>{{cite journal | vauthors = Kan M, Wu X, Wang F, McKeehan WL | title = Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 22 | pages = 15947–52 | date = May 1999 | pmid = 10336501 | doi = 10.1074/jbc.274.22.15947 }}</ref>
* [[HSPA9]],<ref name = pmid10510314>{{cite journal | vauthors = Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T | title = Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin | journal = The Biochemical Journal | volume = 343 | issue = 2 | pages = 461–6 | date = Oct 1999 | pmid = 10510314 | pmc = 1220575 | doi = 10.1042/0264-6021:3430461 }}</ref>  and
* [[S100A13]].<ref name = pmid9712836>{{cite journal | vauthors = Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T | title = S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro | journal = The Journal of Biological Chemistry | volume = 273 | issue = 35 | pages = 22224–31 | date = Aug 1998 | pmid = 9712836 | doi = 10.1074/jbc.273.35.22224 }}</ref><ref name = pmid11432880>{{cite journal | vauthors = Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T | title = Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress | journal = The Journal of Biological Chemistry | volume = 276 | issue = 27 | pages = 25549–57 | date = Jul 2001 | pmid = 11432880 | doi = 10.1074/jbc.M102925200 }}</ref>
{{Div col end}}
 
== See also ==
* [[Fibroblast growth factor]]
* [[Fibroblast growth factor]]


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Yu YL, Kha H, Golden JA, Migchielsen AA, Goetzl EJ, Turck CW | title = An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist | journal = The Journal of Experimental Medicine | volume = 175 | issue = 4 | pages = 1073–80 | date = Apr 1992 | pmid = 1372643 | pmc = 2119192 | doi = 10.1084/jem.175.4.1073 }}
| citations =
* {{cite journal | vauthors = Chiu IM, Wang WP, Lehtoma K | title = Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1 | journal = Oncogene | volume = 5 | issue = 5 | pages = 755–62 | date = May 1990 | pmid = 1693186 | doi =  }}
*{{cite journal | author=Yu YL, Kha H, Golden JA, ''et al.'' |title=An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist. |journal=J. Exp. Med. |volume=175 |issue= 4 |pages= 1073-80 |year= 1992 |pmid= 1372643 |doi= }}
* {{cite journal | vauthors = Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, Hsu BT, Rees DC | title = Three-dimensional structures of acidic and basic fibroblast growth factors | journal = Science | volume = 251 | issue = 4989 | pages = 90–3 | date = Jan 1991 | pmid = 1702556 | doi = 10.1126/science.1702556 }}
*{{cite journal | author=Chiu IM, Wang WP, Lehtoma K |title=Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1. |journal=Oncogene |volume=5 |issue= 5 |pages= 755-62 |year= 1990 |pmid= 1693186 |doi=  }}
* {{cite journal | vauthors = Wang WP, Quick D, Balcerzak SP, Needleman SW, Chiu IM | title = Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients | journal = Oncogene | volume = 6 | issue = 9 | pages = 1521–9 | date = Sep 1991 | pmid = 1717925 | doi =  }}
*{{cite journal | author=Zhu X, Komiya H, Chirino A, ''et al.'' |title=Three-dimensional structures of acidic and basic fibroblast growth factors. |journal=Science |volume=251 |issue= 4989 |pages= 90-3 |year= 1991 |pmid= 1702556 |doi= }}
* {{cite journal | vauthors = Wu DQ, Kan MK, Sato GH, Okamoto T, Sato JD | title = Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors | journal = The Journal of Biological Chemistry | volume = 266 | issue = 25 | pages = 16778–85 | date = Sep 1991 | pmid = 1885605 | doi =  }}
*{{cite journal | author=Wang WP, Quick D, Balcerzak SP, ''et al.'' |title=Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients. |journal=Oncogene |volume=6 |issue= 9 |pages= 1521-9 |year= 1991 |pmid= 1717925 |doi=  }}
* {{cite journal | vauthors = Crumley G, Dionne CA, Jaye M | title = The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon | journal = Biochemical and Biophysical Research Communications | volume = 171 | issue = 1 | pages = 7–13 | date = Aug 1990 | pmid = 2393407 | doi = 10.1016/0006-291X(90)91348-V }}
*{{cite journal | author=Wu DQ, Kan MK, Sato GH, ''et al.'' |title=Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors. |journal=J. Biol. Chem. |volume=266 |issue= 25 |pages= 16778-85 |year= 1991 |pmid= 1885605 |doi=  }}
* {{cite journal | vauthors = Harper JW, Strydom DJ, Lobb RR | title = Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor | journal = Biochemistry | volume = 25 | issue = 14 | pages = 4097–103 | date = Jul 1986 | pmid = 2427112 | doi = 10.1021/bi00362a017 }}
*{{cite journal | author=Crumley G, Dionne CA, Jaye M |title=The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 1 |pages= 7-13 |year= 1990 |pmid= 2393407 |doi= }}
* {{cite journal | vauthors = Winkles JA, Friesel R, Burgess WH, Howk R, Mehlman T, Weinstein R, Maciag T | title = Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 20 | pages = 7124–8 | date = Oct 1987 | pmid = 2444975 | pmc = 299242 | doi = 10.1073/pnas.84.20.7124 }}
*{{cite journal | author=Harper JW, Strydom DJ, Lobb RR |title=Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor. |journal=Biochemistry |volume=25 |issue= 14 |pages= 4097-103 |year= 1986 |pmid= 2427112 |doi= }}
* {{cite journal | vauthors = Wang WP, Lehtoma K, Varban ML, Krishnan I, Chiu IM | title = Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues | journal = Molecular and Cellular Biology | volume = 9 | issue = 6 | pages = 2387–95 | date = Jun 1989 | pmid = 2474753 | pmc = 362312 | doi =  }}
*{{cite journal | author=Winkles JA, Friesel R, Burgess WH, ''et al.'' |title=Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 20 |pages= 7124-8 |year= 1987 |pmid= 2444975 |doi= }}
* {{cite journal | vauthors = Mergia A, Tischer E, Graves D, Tumolo A, Miller J, Gospodarowicz D, Abraham JA, Shipley GD, Fiddes JC | title = Structural analysis of the gene for human acidic fibroblast growth factor | journal = Biochemical and Biophysical Research Communications | volume = 164 | issue = 3 | pages = 1121–9 | date = Nov 1989 | pmid = 2590193 | doi = 10.1016/0006-291X(89)91785-3 }}
*{{cite journal | author=Wang WP, Lehtoma K, Varban ML, ''et al.'' |title=Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues. |journal=Mol. Cell. Biol. |volume=9 |issue= 6 |pages= 2387-95 |year= 1989 |pmid= 2474753 |doi=  }}
* {{cite journal | vauthors = Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA | title = The complete amino acid sequence of human brain-derived acidic fibroblast growth factor | journal = Biochemical and Biophysical Research Communications | volume = 138 | issue = 2 | pages = 611–7 | date = Jul 1986 | pmid = 3527167 | doi = 10.1016/S0006-291X(86)80540-X }}
*{{cite journal | author=Mergia A, Tischer E, Graves D, ''et al.'' |title=Structural analysis of the gene for human acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 3 |pages= 1121-9 |year= 1989 |pmid= 2590193 |doi= }}
* {{cite journal | vauthors = Gautschi P, Fràter-Schröder M, Böhlen P | title = Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors | journal = FEBS Letters | volume = 204 | issue = 2 | pages = 203–7 | date = Aug 1986 | pmid = 3732516 | doi = 10.1016/0014-5793(86)80812-2 }}
*{{cite journal | author=Jaye M, Howk R, Burgess W, ''et al.'' |title=Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization. |journal=Science |volume=233 |issue= 4763 |pages= 541-5 |year= 1986 |pmid= 3523756 |doi= }}
* {{cite journal | vauthors = Gautschi-Sova P, Müller T, Böhlen P | title = Amino acid sequence of human acidic fibroblast growth factor | journal = Biochemical and Biophysical Research Communications | volume = 140 | issue = 3 | pages = 874–80 | date = Nov 1986 | pmid = 3778488 | doi = 10.1016/0006-291X(86)90716-3 }}
*{{cite journal | author=Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA |title=The complete amino acid sequence of human brain-derived acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=138 |issue= 2 |pages= 611-7 |year= 1986 |pmid= 3527167 |doi= }}
* {{cite journal | vauthors = Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA | title = Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities | journal = Biochemical and Biophysical Research Communications | volume = 135 | issue = 2 | pages = 541–8 | date = Mar 1986 | pmid = 3964259 | doi = 10.1016/0006-291X(86)90028-8 }}
*{{cite journal | author=Gautschi P, Fràter-Schröder M, Böhlen P |title=Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors. |journal=FEBS Lett. |volume=204 |issue= 2 |pages= 203-7 |year= 1986 |pmid= 3732516 |doi= }}
* {{cite journal | vauthors = Zhao XM, Yeoh TK, Hiebert M, Frist WH, Miller GG | title = The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells | journal = Transplantation | volume = 56 | issue = 5 | pages = 1177–82 | date = Nov 1993 | pmid = 7504343 | doi = 10.1097/00007890-199311000-00025 }}
*{{cite journal | author=Gautschi-Sova P, Müller T, Böhlen P |title=Amino acid sequence of human acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=140 |issue= 3 |pages= 874-80 |year= 1986 |pmid= 3778488 |doi= }}
* {{cite journal | vauthors = Pineda-Lucena A, Jiménez MA, Nieto JL, Santoro J, Rico M, Giménez-Gallego G | title = 1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate | journal = Journal of Molecular Biology | volume = 242 | issue = 1 | pages = 81–98 | date = Sep 1994 | pmid = 7521397 | doi = 10.1006/jmbi.1994.1558 }}
*{{cite journal | author=Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA |title=Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 2 |pages= 541-8 |year= 1986 |pmid= 3964259 |doi= }}
* {{cite journal | vauthors = Chotani MA, Payson RA, Winkles JA, Chiu IM | title = 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 | journal = Nucleic Acids Research | volume = 23 | issue = 3 | pages = 434–41 | date = Feb 1995 | pmid = 7533902 | pmc = 306694 | doi = 10.1093/nar/23.3.434 }}
*{{cite journal | author=Zhao XM, Yeoh TK, Hiebert M, ''et al.'' |title=The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells. |journal=Transplantation |volume=56 |issue= 5 |pages= 1177-82 |year= 1993 |pmid= 7504343 |doi= }}
* {{cite journal | vauthors = Opalenik SR, Shin JT, Wehby JN, Mahesh VK, Thompson JA | title = The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor | journal = The Journal of Biological Chemistry | volume = 270 | issue = 29 | pages = 17457–67 | date = Jul 1995 | pmid = 7542239 | doi = 10.1074/jbc.270.29.17457 }}
*{{cite journal | author=Pineda-Lucena A, Jiménez MA, Nieto JL, ''et al.'' |title=1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate. |journal=J. Mol. Biol. |volume=242 |issue= 1 |pages= 81-98 |year= 1994 |pmid= 7521397 |doi= 10.1006/jmbi.1994.1558 }}
* {{cite journal | vauthors = Myers RL, Payson RA, Chotani MA, Deaven LL, Chiu IM | title = Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts | journal = Oncogene | volume = 8 | issue = 2 | pages = 341–9 | date = Feb 1993 | pmid = 7678925 | doi =  }}
*{{cite journal | author=Chotani MA, Payson RA, Winkles JA, Chiu IM |title=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. |journal=Nucleic Acids Res. |volume=23 |issue= 3 |pages= 434-41 |year= 1995 |pmid= 7533902 |doi= }}
*{{cite journal | author=Opalenik SR, Shin JT, Wehby JN, ''et al.'' |title=The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17457-67 |year= 1995 |pmid= 7542239 |doi=  }}
*{{cite journal  | author=Myers RL, Payson RA, Chotani MA, ''et al.'' |title=Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts. |journal=Oncogene |volume=8 |issue= 2 |pages= 341-9 |year= 1993 |pmid= 7678925 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=2246}}
{{Growth factors}}
{{Intercellular signaling peptides and proteins}}
{{Intercellular signaling peptides and proteins}}
{{WikiDoc Sources}}
{{Growth factor receptor modulators}}

Revision as of 04:46, 31 August 2017

This article is about fibroblast growth factor-1. For the internal ribosome entry site, see FGF-1 internal ribosome entry site (IRES).
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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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:

See also

References

  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. PMC 4184286. PMID 25043058. Lay summary – Salk Institute.
  5. ↑ 5.0 5.1 5.2 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. ↑ 8.0 8.1 8.2 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

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