Fibrinogen beta chain

Fibrinogen beta 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​, 1fze​, 1fzf​, 1fzg​, 1lt9​, 1ltj​, 1n86​, 1n8e​, 1re3​, 1re4​, 1rf0​, 1rf1​, 2a45​, 2ffd​, 2h43​, 2hod​, 2hpc​, 2oyh​, 2oyi​
Identifiers
Symbols	FGB ; MGC104327; MGC120405
External IDs	Template:OMIM5 Template:MGI HomoloGene: 3772
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 beta chain, also known as FGB, is a human gene.

The protein encoded by this gene is the beta 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 afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.

See also

• Fibrin

Further reading

• Doolittle RF (1984). "Fibrinogen and fibrin". Annu. Rev. Biochem. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
• Vasse M, Paysant J, Soria J; et al. (1997). "Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk". Haemostasis. 26 Suppl 4: 331–9. PMID 8979138.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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)
• 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.
• Brennan SO, Fellowes AP, George PM (2001). "Molecular mechanisms of hypo- and afibrinogenemia". Ann. N. Y. Acad. Sci. 936: 91–100. PMID 11460528.CS1 maint: Multiple names: authors list (link)
• 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.
• Chen XC, Xu MT, Zhou W; et al. (2007). "A meta-analysis of relationship between beta-fibrinogen gene -148C/T polymorphism and susceptibility to cerebral infarction in Han Chinese". Chin. Med. J. 120 (13): 1198–202. PMID 17637253.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tarakhovskiĭ IuS, Galushchenko IV, Boroviagin VL; et al. (1979). "[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones]". Biokhimiia. 44 (5): 897–902. PMID 156564.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Watt KW, Takagi T, Doolittle RF (1979). "Amino acid sequence of the beta chain of human fibrinogen". Biochemistry. 18 (1): 68–76. PMID 420779.CS1 maint: Multiple names: authors list (link)
• Gårdlund B, Hessel B, Marguerie G; et al. (1977). "Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments". Eur. J. Biochem. 77 (3): 595–610. PMID 891553.CS1 maint: Explicit use of et al. (link) 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). "Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3478–82. PMID 1565641.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Koopman J, Haverkate F, Lord ST; et al. (1992). "Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr". J. Clin. Invest. 90 (1): 238–44. PMID 1634610.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.
• Yoshida N, Wada H, Morita K; et al. (1991). "A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine". Blood. 77 (9): 1958–63. PMID 2018836.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chung DW, Harris JE, Davie EW (1991). "Nucleotide sequences of the three genes coding for human fibrinogen". Adv. Exp. Med. Biol. 281: 39–48. PMID 2102623.CS1 maint: Multiple names: authors list (link)
• Danishefsky K, Hartwig R, Banerjee D, Redman C (1990). "Intracellular fate of fibrinogen B beta chain expressed in COS cells". Biochim. Biophys. Acta. 1048 (2–3): 202–8. PMID 2322576.CS1 maint: Multiple names: authors list (link)
• Berg K, Kierulf P (1989). "DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration". Clin. Genet. 36 (4): 229–35. PMID 2572363.