Fibrinogen beta chain

From Wikipedia, the free encyclopedia

PDB rendering based on 1fza.

Available structures: 1fza, 1fzb, 1fzc, 1fze, 1fzf, 1fzg, 1lt9, 1ltj, 1n86, 1n8e, 1re3, 1re4, 1rf0, 1rf1, 2a45, 2ffd, 2h43, 2hod, 2hpc, 2oyh, 2oyi

Identifiers

Symbol(s)

FGB; MGC104327; MGC120405

External IDs

OMIM: 134830 MGI: 99501 HomoloGene: 3772

Gene ontology
Molecular Function:	• receptor binding • protein binding, bridging
Cellular Component:	• extracellular region • fibrinogen complex • soluble fraction
Biological Process:	• signal transduction • blood pressure regulation • positive regulation of cell proliferation • platelet activation • protein polymerization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005141 (mRNA)
NP_005132 (protein)

NM_181849 (mRNA)
NP_862897 (protein)

Location

Chr 4: 155.7 - 155.71 Mb

Chr 3: 83.13 - 83.14 Mb

Pubmed search

[1]

[2]

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.^[1]

[edit] See also

Fibrin

[edit] References

^ Entrez Gene: FGB fibrinogen beta chain.

[edit] 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.
Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen.". Int. J. Biochem. Cell Biol. 31 (7): 741-6. PMID 10467729.
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.
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.
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.
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.
Watt KW, Takagi T, Doolittle RF (1979). "Amino acid sequence of the beta chain of human fibrinogen.". Biochemistry 18 (1): 68-76. PMID 420779.
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.
Blombäck B, Hessel B, Hogg D (1976). "Disulfide bridges in nh2 -terminal part of human fibrinogen.". Thromb. Res. 8 (5): 639-58. PMID 936108.
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.
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.
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.
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.
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.
Berg K, Kierulf P (1989). "DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration.". Clin. Genet. 36 (4): 229-35. PMID 2572363.