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Glycoprotein Ib (platelet), alpha polypeptide

PDB rendering based on 1gwb.
Available structures
1gwb, 1m0z, 1m10, 1ook, 1p8v, 1p9a, 1qyy, 1sq0, 1u0n
Symbols GP1BA; BSS; CD42B; CD42b-alpha; GP1B; MGC34595
External IDs OMIM606672 MGI1333744 HomoloGene143 GeneCards: GP1BA Gene
RNA expression pattern
PBB GE GP1BA 207389 at tn.png
More reference expression data
Species Human Mouse
Entrez 2811 14723
Ensembl ENSG00000185245 ENSMUSG00000050675
UniProt P07359 O35930
RefSeq (mRNA) NM_000173 NM_010326
RefSeq (protein) NP_000164 NP_034456
Location (UCSC) Chr 17:
4.78 - 4.78 Mb
Chr 11:
70.46 - 70.46 Mb
PubMed search [1] [2]

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]



GP1BA has been shown to interact with YWHAZ[2][3][4] and FLNB.[5]

See also


  1. ^ "Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide".  
  2. ^ Calverley, D C; Kavanagh T J, Roth G J (Feb. 1998). "Human signaling protein 14-3-3zeta interacts with platelet glycoprotein Ib subunits Ibalpha and Ibbeta". Blood (UNITED STATES) 91 (4): 1295–303. ISSN 0006-4971. PMID 9454760.  
  3. ^ Du, X; Fox J E, Pei S (Mar. 1996). "Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha". J. Biol. Chem. (UNITED STATES) 271 (13): 7362–7. ISSN 0021-9258. PMID 8631758.  
  4. ^ Feng, S; Christodoulides N, Reséndiz J C, Berndt M C, Kroll M H (Jan. 2000). "Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to GpIb/IX/V". Blood (UNITED STATES) 95 (2): 551–7. ISSN 0006-4971. PMID 10627461.  
  5. ^ Takafuta, T; Wu G, Murphy G F, Shapiro S S (Jul. 1998). "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha". J. Biol. Chem. (UNITED STATES) 273 (28): 17531–8. ISSN 0021-9258. PMID 9651345.  

Further reading

  • Kunishima S, Kamiya T, Saito H (2003). "Genetic abnormalities of Bernard-Soulier syndrome.". Int. J. Hematol. 76 (4): 319–27. doi:10.1007/BF02982690. 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. doi:10.1073/pnas.88.11.4761. 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. doi:10.1111/j.1432-1033.1991.tb16135.x. 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. doi:10.1021/bi00447a009. 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. doi:10.1016/0378-1119(89)90446-0. 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. doi:10.1016/S0006-291X(88)80853-2. 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. doi:10.1111/j.1432-1033.1985.tb09259.x. 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. doi:10.1073/pnas.84.16.5615. 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. doi:10.1073/pnas.85.7.2135. 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. doi:10.1073/pnas.84.16.5610. 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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