Fibrinogen alpha chain is a protein that in humans is encoded by the FGAgene.
The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein composed 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 that vary in the carboxy-terminus.
Matsuda M, Sugo T (2003). "Structure and function of human fibrinogen inferred from dysfibrinogens". Int. J. Hematol. 76 Suppl 1: 352–60. PMID12430881.
Everse SJ (2003). "New insights into fibrin (ogen) structure and function". Vox Sang. 83 Suppl 1: 375–82. PMID12617173.
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): 1558–1566. doi:10.1161/01.ATV.0000136649.83297.bf. PMID15217804.
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)". Blood80 (8): 1972–9. PMID1391954.
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". Biochemistry31 (48): 11968–11972. doi:10.1021/bi00163a002. PMID1457396.
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. PMID1560020.
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. doi:10.1172/JCI115857. PMC443064. PMID1634621.
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. PMID1675636.
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. PMID1680863.