- GP1BA
Glycoprotein Ib (platelet), alpha polypeptide (GP1BA) also known as CD42b (Cluster of Differentiation 42b), is a human
gene .PBB_Summary
section_title =
summary_text = 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 ofBernard-Soulier syndrome s and platelet-typevon Willebrand disease . [cite web | title = Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2811| accessdate = ]ee also
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Cluster of differentiation References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Kunishima S, Kamiya T, Saito H |title=Genetic abnormalities of Bernard-Soulier syndrome. |journal=Int. J. Hematol. |volume=76 |issue= 4 |pages= 319–27 |year= 2003 |pmid= 12463594 |doi=
*cite journal | author=Du X |title=Signaling and regulation of the platelet glycoprotein Ib-IX-V complex. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 262–9 |year= 2007 |pmid= 17414217 |doi= 10.1097/MOH.0b013e3280dce51a
*cite journal | author=Clemetson KJ |title=A short history of platelet glycoprotein Ib complex. |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 63–8 |year= 2007 |pmid= 17597992 |doi=
*cite journal | author=López JA, Ludwig EH, McCarthy BJ |title=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. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 10055–61 |year= 1992 |pmid= 1577776 |doi=
*cite journal | author=Murata M, Furihata K, Ishida F, "et al." |title=Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness. |journal=Blood |volume=79 |issue= 11 |pages= 3086–90 |year= 1992 |pmid= 1586750 |doi=
*cite journal | author=Girma JP, Takahashi Y, Yoshioka A, "et al." |title=Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib. |journal=Thromb. Haemost. |volume=64 |issue= 2 |pages= 326–32 |year= 1991 |pmid= 1702906 |doi=
*cite journal | author=Miller JL, Lyle VA, Cunningham D |title=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. |journal=Blood |volume=79 |issue= 2 |pages= 439–46 |year= 1992 |pmid= 1730088 |doi=
*cite journal | author=Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE |title=Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 364–9 |year= 1992 |pmid= 1730602 |doi=
*cite journal | author=Miller JL, Cunningham D, Lyle VA, Finch CN |title=Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4761–5 |year= 1991 |pmid= 2052556 |doi=
*cite journal | author=Hess D, Schaller J, Rickli EE, Clemetson KJ |title=Identification of the disulphide bonds in human platelet glycocalicin. |journal=Eur. J. Biochem. |volume=199 |issue= 2 |pages= 389–93 |year= 1991 |pmid= 2070794 |doi=
*cite journal | author=Du X, Beutler L, Ruan C, "et al." |title=Glycoprotein Ib and glycoprotein IX are fully complexed in the intact platelet membrane. |journal=Blood |volume=69 |issue= 5 |pages= 1524–7 |year= 1987 |pmid= 2436691 |doi=
*cite journal | author=Andrews RK, Booth WJ, Gorman JJ, "et al." |title=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. |journal=Biochemistry |volume=28 |issue= 21 |pages= 8317–26 |year= 1990 |pmid= 2557900 |doi=
*cite journal | author=Wenger RH, Wicki AN, Kieffer N, "et al." |title=The 5' flanking region and chromosomal localization of the gene encoding human platelet membrane glycoprotein Ib alpha. |journal=Gene |volume=85 |issue= 2 |pages= 517–24 |year= 1990 |pmid= 2628181 |doi=
*cite journal | author=Wenger RH, Kieffer N, Wicki AN, Clemetson KJ |title=Structure of the human blood platelet membrane glycoprotein Ib alpha gene. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 389–95 |year= 1988 |pmid= 2845978 |doi=
*cite journal | author=Wicki AN, Clemetson KJ |title=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. |journal=Eur. J. Biochem. |volume=153 |issue= 1 |pages= 1–11 |year= 1985 |pmid= 2933256 |doi=
*cite journal | author=Adelman B, Michelson AD, Greenberg J, Handin RI |title=Proteolysis of platelet glycoprotein Ib by plasmin is facilitated by plasmin lysine-binding regions. |journal=Blood |volume=68 |issue= 6 |pages= 1280–4 |year= 1987 |pmid= 2946332 |doi=
*cite journal | author=Lopez JA, Chung DW, Fujikawa K, "et al." |title=Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5615–9 |year= 1987 |pmid= 3303030 |doi=
*cite journal | author=Lopez JA, Chung DW, Fujikawa K, "et al." |title=The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 7 |pages= 2135–9 |year= 1988 |pmid= 3353370 |doi=
*cite journal | author=Titani K, Takio K, Handa M, Ruggeri ZM |title=Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5610–4 |year= 1987 |pmid= 3497398 |doi=
*cite journal | author=Harmon JT, Jamieson GA |title=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. |journal=J. Biol. Chem. |volume=261 |issue= 28 |pages= 13224–9 |year= 1986 |pmid= 3759960 |doi=External links
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