GP1BA

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Glycoprotein Ib (platelet), alpha polypeptide
PDB rendering based on 1gwb.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols GP1BA ; BSS; CD42B; CD42b-alpha; GP1B; MGC34595
External IDs Template:OMIM5 Template:MGI HomoloGene143
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

Glycoprotein Ib (platelet), alpha polypeptide (GP1BA) also known as CD42b (Cluster of Differentiation 42b), is a human gene.

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard-Soulier syndromes and platelet-type von Willebrand disease.[1]

See also

References

  1. "Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide".

Further reading

  • Kunishima S, Kamiya T, Saito H (2003). "Genetic abnormalities of Bernard-Soulier syndrome". Int. J. Hematol. 76 (4): 319–27. PMID 12463594.
  • Du X (2007). "Signaling and regulation of the platelet glycoprotein Ib-IX-V complex". Curr. Opin. Hematol. 14 (3): 262–9. doi:10.1097/MOH.0b013e3280dce51a. PMID 17414217.
  • Clemetson KJ (2007). "A short history of platelet glycoprotein Ib complex". Thromb. Haemost. 98 (1): 63–8. PMID 17597992.
  • López JA, Ludwig EH, McCarthy BJ (1992). "Polymorphism of human glycoprotein Ib alpha results from a variable number of tandem repeats of a 13-amino acid sequence in the mucin-like macroglycopeptide region. Structure/function implications". J. Biol. Chem. 267 (14): 10055–61. PMID 1577776.
  • Murata M, Furihata K, Ishida F; et al. (1992). "Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness". Blood. 79 (11): 3086–90. PMID 1586750.
  • Girma JP, Takahashi Y, Yoshioka A; et al. (1991). "Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib". Thromb. Haemost. 64 (2): 326–32. PMID 1702906.
  • Miller JL, Lyle VA, Cunningham D (1992). "Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease". Blood. 79 (2): 439–46. PMID 1730088.
  • Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE (1992). "Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane". J. Biol. Chem. 267 (1): 364–9. PMID 1730602.
  • Miller JL, Cunningham D, Lyle VA, Finch CN (1991). "Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease". Proc. Natl. Acad. Sci. U.S.A. 88 (11): 4761–5. PMID 2052556.
  • Hess D, Schaller J, Rickli EE, Clemetson KJ (1991). "Identification of the disulphide bonds in human platelet glycocalicin". Eur. J. Biochem. 199 (2): 389–93. PMID 2070794.
  • Du X, Beutler L, Ruan C; et al. (1987). "Glycoprotein Ib and glycoprotein IX are fully complexed in the intact platelet membrane". Blood. 69 (5): 1524–7. PMID 2436691.
  • Andrews RK, Booth WJ, Gorman JJ; et al. (1990). "Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex". Biochemistry. 28 (21): 8317–26. PMID 2557900.
  • Wenger RH, Wicki AN, Kieffer N; et al. (1990). "The 5' flanking region and chromosomal localization of the gene encoding human platelet membrane glycoprotein Ib alpha". Gene. 85 (2): 517–24. PMID 2628181.
  • Wenger RH, Kieffer N, Wicki AN, Clemetson KJ (1988). "Structure of the human blood platelet membrane glycoprotein Ib alpha gene". Biochem. Biophys. Res. Commun. 156 (1): 389–95. PMID 2845978.
  • Wicki AN, Clemetson KJ (1985). "Structure and function of platelet membrane glycoproteins Ib and V. Effects of leukocyte elastase and other proteases on platelets response to von Willebrand factor and thrombin". Eur. J. Biochem. 153 (1): 1–11. PMID 2933256.
  • Adelman B, Michelson AD, Greenberg J, Handin RI (1987). "Proteolysis of platelet glycoprotein Ib by plasmin is facilitated by plasmin lysine-binding regions". Blood. 68 (6): 1280–4. PMID 2946332.
  • Lopez JA, Chung DW, Fujikawa K; et al. (1987). "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein". Proc. Natl. Acad. Sci. U.S.A. 84 (16): 5615–9. PMID 3303030.
  • Lopez JA, Chung DW, Fujikawa K; et al. (1988). "The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence". Proc. Natl. Acad. Sci. U.S.A. 85 (7): 2135–9. PMID 3353370.
  • Titani K, Takio K, Handa M, Ruggeri ZM (1987). "Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib". Proc. Natl. Acad. Sci. U.S.A. 84 (16): 5610–4. PMID 3497398.
  • Harmon JT, Jamieson GA (1986). "The glycocalicin portion of platelet glycoprotein Ib expresses both high and moderate affinity receptor sites for thrombin. A soluble radioreceptor assay for the interaction of thrombin with platelets". J. Biol. Chem. 261 (28): 13224–9. PMID 3759960.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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