Fibrinogen alpha chain

Fibrinogen alpha chain
PDB rendering based on 1fza.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1fza​, 1fzb​, 1fzc​, 1fzd​, 1fze​, 1fzf​, 1fzg​, 1lt9​, 1ltj​, 1n86​, 1n8e​, 1re3​, 1re4​, 1rf0​, 1rf1​, 2a45​, 2ffd​, 2h43​, 2hod​, 2hpc​, 2oyh​, 2oyi​
Identifiers
Symbols	FGA ; Fib2; MGC119422; MGC119423; MGC119425
External IDs	Template:OMIM5 Template:MGI HomoloGene: 428
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Fibrinogen alpha chain, also known as FGA, is a human gene.

The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus.

See also

• Fibrinogen
• Fibrinogen gamma chain

Further reading

• Doolittle RF (1984). "Fibrinogen and fibrin". Annu. Rev. Biochem. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
• Galanakis DK (1994). "Inherited dysfibrinogenemia: emerging abnormal structure associations with pathologic and nonpathologic dysfunctions". Semin. Thromb. Hemost. 19 (4): 386–95. PMID 8140431.
• Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen". Int. J. Biochem. Cell Biol. 31 (7): 741–6. PMID 10467729.CS1 maint: Multiple names: authors list (link)
• Bennett JS (2001). "Platelet-fibrinogen interactions". Ann. N. Y. Acad. Sci. 936: 340–54. PMID 11460491.
• Redman CM, Xia H (2001). "Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion". Ann. N. Y. Acad. Sci. 936: 480–95. PMID 11460506.
• Matsuda M, Sugo T (2003). "Structure and function of human fibrinogen inferred from dysfibrinogens". Int. J. Hematol. 76 Suppl 1: 352–60. PMID 12430881.
• Everse SJ (2003). "New insights into fibrin (ogen) structure and function". Vox Sang. 83 Suppl 1: 375–82. PMID 12617173.
• Scott EM, Ariëns RA, Grant PJ (2005). "Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1558–66. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804.CS1 maint: Multiple names: authors list (link)
• Lord ST (2007). "Fibrinogen and fibrin: scaffold proteins in hemostasis". Curr. Opin. Hematol. 14 (3): 236–41. doi:10.1097/MOH.0b013e3280dce58c. PMID 17414213.
• Cottrell BA, Strong DD, Watt KW, Doolittle RF (1980). "Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites". Biochemistry. 18 (24): 5405–10. PMID 518845.CS1 maint: Multiple names: authors list (link)
• Watt KW, Cottrell BA, Strong DD, Doolittle RF (1980). "Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence". Biochemistry. 18 (24): 5410–6. PMID 518846.CS1 maint: Multiple names: authors list (link)
• Fretto LJ, Ferguson EW, Steinman HM, McKee PA (1978). "Localization of the alpha-chain cross-link acceptor sites of human fibrin". J. Biol. Chem. 253 (7): 2184–95. PMID 632262.CS1 maint: Multiple names: authors list (link)
• Blombäck B, Hessel B, Hogg D (1976). "Disulfide bridges in nh2 -terminal part of human fibrinogen". Thromb. Res. 8 (5): 639–58. PMID 936108.CS1 maint: Multiple names: authors list (link)
• Koopman J, Haverkate F, Grimbergen J; et al. (1992). "Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA-->stop TAA)". Blood. 80 (8): 1972–9. PMID 1391954.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fu Y, Weissbach L, Plant PW; et al. (1993). "Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits". Biochemistry. 31 (48): 11968–72. PMID 1457396.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Martin PD, Robertson W, Turk D; et al. (1992). "The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution". J. Biol. Chem. 267 (11): 7911–20. PMID 1560020.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Stubbs MT, Oschkinat H, Mayr I; et al. (1992). "The interaction of thrombin with fibrinogen. A structural basis for its specificity". Eur. J. Biochem. 206 (1): 187–95. PMID 1587268.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Maekawa H, Yamazumi K, Muramatsu S; et al. (1992). "Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator". J. Clin. Invest. 90 (1): 67–76. PMID 1634621.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Maekawa H, Yamazumi K, Muramatsu S; et al. (1991). "An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation". J. Biol. Chem. 266 (18): 11575–81. PMID 1675636.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wu C, Chung AE (1991). "Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains". J. Biol. Chem. 266 (28): 18802–7. PMID 1680863.