Fibrinogen alpha chain

Fibrinogen alpha chain

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

PBB_Summary
section_title =
summary_text = 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. [cite web | title = Entrez Gene: FGA fibrinogen alpha chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2243| accessdate = ]

ee also

*Fibrinogen
*Fibrinogen gamma chain

References

Further reading

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

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