Biology:Fibrinogen alpha chain

Short description: Protein-coding gene in the species Homo sapiens

Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene.

Function

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.^[1]

Interactions

Fibrinogen alpha chain has been shown to interact with tissue plasminogen activator.^[2]^[3]

References

↑ "Entrez Gene: FGA fibrinogen alpha chain". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2243.
↑ "Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains". Biochemistry 40 (3): 801–808. Jan 2001. doi:10.1021/bi001789t. PMID 11170397.
↑ "Localization of the binding site of tissue-type plasminogen activator to fibrin". The Journal of Clinical Investigation 78 (1): 163–169. Jul 1986. doi:10.1172/JCI112546. PMID 3088041.

"Fibrinogen and fibrin". Annual Review of Biochemistry 53: 195–229. 1984. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
"Inherited dysfibrinogenemia: emerging abnormal structure associations with pathologic and nonpathologic dysfunctions". Seminars in Thrombosis and Hemostasis 19 (4): 386–395. 1994. doi:10.1055/s-2007-993290. PMID 8140431.
"Fibrinogen". The International Journal of Biochemistry & Cell Biology 31 (7): 741–746. Jul 1999. doi:10.1016/S1357-2725(99)00032-1. PMID 10467729.
"Platelet-fibrinogen interactions". Annals of the New York Academy of Sciences 936 (1): 340–354. 2001. doi:10.1111/j.1749-6632.2001.tb03521.x. PMID 11460491. Bibcode: 2001NYASA.936..340B.
"Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion". Annals of the New York Academy of Sciences 936: 480–495. 2001. doi:10.1111/j.1749-6632.2001.tb03535.x. PMID 11460506.
"Structure and function of human fibrinogen inferred from dysfibrinogens". International Journal of Hematology 76 Suppl 1: 352–60. August 2002. doi:10.1007/bf03165284. PMID 12430881.
"New insights into fibrin (ogen) structure and function". Vox Sanguinis 83 Suppl 1: 375–82. August 2002. doi:10.1111/j.1423-0410.2002.tb05338.x. PMID 12617173.
"Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease". Arteriosclerosis, Thrombosis, and Vascular Biology 24 (9): 1558–1566. September 2004. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804.
"Fibrinogen and fibrin: scaffold proteins in hemostasis". Current Opinion in Hematology 14 (3): 236–241. May 2007. doi:10.1097/MOH.0b013e3280dce58c. PMID 17414213.
"Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites". Biochemistry 18 (24): 5405–5410. November 1979. doi:10.1021/bi00591a023. PMID 518845.
"Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence". Biochemistry 18 (24): 5410–5416. November 1979. doi:10.1021/bi00591a024. PMID 518846.
"Localization of the alpha-chain cross-link acceptor sites of human fibrin". The Journal of Biological Chemistry 253 (7): 2184–95. Apr 1978. doi:10.1016/S0021-9258(17)38057-2. PMID 632262.
"Disulfide bridges in nh2 -terminal part of human fibrinogen". Thrombosis Research 8 (5): 639–658. May 1976. doi:10.1016/0049-3848(76)90245-0. PMID 936108.
"Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA-->stop TAA)". Blood 80 (8): 1972–9. Oct 1992. doi:10.1182/blood.V80.8.1972.1972. PMID 1391954.
"Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits". Biochemistry 31 (48): 11968–11972. December 1992. doi:10.1021/bi00163a002. PMID 1457396.
"The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution". The Journal of Biological Chemistry 267 (11): 7911–20. Apr 1992. doi:10.1016/S0021-9258(18)42599-9. PMID 1560020.
"The interaction of thrombin with fibrinogen. A structural basis for its specificity". European Journal of Biochemistry 206 (1): 187–195. May 1992. doi:10.1111/j.1432-1033.1992.tb16916.x. PMID 1587268.
"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". The Journal of Clinical Investigation 90 (1): 67–76. Jul 1992. doi:10.1172/JCI115857. PMID 1634621.
"An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation". The Journal of Biological Chemistry 266 (18): 11575–81. Jun 1991. doi:10.1016/S0021-9258(18)98995-7. PMID 1675636.
"Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains". The Journal of Biological Chemistry 266 (28): 18802–7. Oct 1991. doi:10.1016/S0021-9258(18)55134-6. PMID 1680863.