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GP1BA  -  glycoprotein Ib (platelet), alpha polypeptide

Homo sapiens

Synonyms: Antigen CD42b-alpha, BDPLT1, BDPLT3, BSS, CD42B, ...
 
 
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Disease relevance of GP1BA

 

High impact information on GP1BA

 

Chemical compound and disease context of GP1BA

 

Biological context of GP1BA

 

Anatomical context of GP1BA

 

Associations of GP1BA with chemical compounds

  • While relative frequencies of the GP1BA Kozak alleles were comparable across groups, the methionine allele (HPA-2b) showed a higher frequency in Africa (0.26) than in the other groups [1].
  • Neither GPIbalpha nor heparin increased the cleavage of substrate A2A3 that lacks domain A1 [21].
  • Surface-labeling of the platelets and two-dimensional gel electrophoresis showed reduced but detectable amounts of glycoprotein (GP) Ib-IX-V present;however, there was markedly less GPIX (2% +/- 1% of normal) than GPIb alpha, Ib beta, or V (7% +/- 2% of normal) [22].
  • The inhibitory effect of antibody against GPIb alpha (GUR83-35) on liposome adhesion was greater at higher shear rates [23].
  • Raised levels of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate, as well as membrane-permeable calcium chelators, inhibited these [Ca(++)](i) oscillations and prevented stable adhesion without affecting the dynamic characteristics of the typical platelet translocation on VWF mediated by GPIbalpha [16].
 

Physical interactions of GP1BA

 

Regulatory relationships of GP1BA

  • Digestion of A1A2A3 by plasma ADAMTS13 was enhanced to a similar extent by a recombinant mutant fragment of platelet GPIbalpha that binds with high affinity to domain A1 or by heparin [21].
  • To begin, we examined filamin binding to GpIbalpha in Chinese hamster ovary cells coexpressing mutant human GpIb-IX and wild-type human filamin A [25].
  • All leucine-rich repeat (LRR) peptides derived from glycoprotein Ibalpha were able to inhibit FXI binding to activated platelets in the following order of decreasing potency: LRR7, LRR1, LRR4, LRR5, LRR6, LRR3, and LRR2 [27].
  • Exposure of platelets for 3 min at 37 degrees C to CG at a concentration that induces full cell activation resulted in an extensive cleavage of the N-terminal region of the extracellular domain of GPIb alpha, the largest (relative molecular mass, M(r), 143,000) of the three subunits constituting the GPIb-IX complex [28].
  • The expression of CD61 did not alter during storage and the percentage of platelets expressing CD42b was > 88% in all units on day 7 [29].
 

Other interactions of GP1BA

  • The results suggest that vWF domain A1 inhibits the cleavage of domain A2, and that inhibition can be relieved by interaction of domain A1 with platelet GPIbalpha or certain glycosaminoglycans [21].
  • Recent results with an adhesion blocking antibody (RAM.1) against GPIb beta, which is disulfide linked to GPIb alpha, have suggested a novel function of this subunit in regulating VWF-mediated platelet adhesion, possibly involving its intracellular face [30].
  • DNA-sequence analysis revealed normal sequences for GPIb alpha and GPIX [24].
  • Removal of the Mr 45,000 amino-terminal part of GPIb alpha by treatment with elastase did not abrogate association of GPV with GPIb-IX, showing that the leucine-rich repeat sequences in GPIb alpha are not required for complex formation [31].
  • However, a synthetic glycoprotein Ibalpha peptide, Asp269-Asp287, containing a thrombin binding site had no effect on the binding of FXI to activated platelets [27].
 

Analytical, diagnostic and therapeutic context of GP1BA

References

  1. Platelet glycoprotein I(b)alpha and integrin alpha2 beta1 polymorphisms: gene frequencies and linkage disequilibrium in a population diversity panel. Di Paola, J., Jugessur, A., Goldman, T., Reiland, J., Tallman, D., Sayago, C., Murray, J.C. J. Thromb. Haemost. (2005) [Pubmed]
  2. Macrothrombocytopenia with abnormal demarcation membranes in megakaryocytes and neutropenia with a complete lack of sialyl-Lewis-X antigen in leukocytes--a new syndrome? Willig, T.B., Breton-Gorius, J., Elbim, C., Mignotte, V., Kaplan, C., Mollicone, R., Pasquier, C., Filipe, A., Miélot, F., Cartron, J.P., Gougerot-Pocidalo, M.A., Debili, N., Guichard, J., Dommergues, J.P., Mohandas, N., Tchernia, G. Blood (2001) [Pubmed]
  3. Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations. Dumas, J.J., Kumar, R., McDonagh, T., Sullivan, F., Stahl, M.L., Somers, W.S., Mosyak, L. J. Biol. Chem. (2004) [Pubmed]
  4. Molecular abnormalities in Glanzmann's thrombasthenia, Bernard-Soulier syndrome, and platelet-type von Willebrand's disease. Clemetson, K.J., Clemetson, J.M. Curr. Opin. Hematol. (1994) [Pubmed]
  5. The variable number of tandem repeat polymorphism of platelet glycoprotein Ibalpha and risk of coronary heart disease. Afshar-Kharghan, V., Matijevic-Aleksic, N., Ahn, C., Boerwinkle, E., Wu, K.K., López, J.A. Blood (2004) [Pubmed]
  6. Targeting platelet-leukocyte interactions: identification of the integrin Mac-1 binding site for the platelet counter receptor glycoprotein Ibalpha. Ehlers, R., Ustinov, V., Chen, Z., Zhang, X., Rao, R., Luscinskas, F.W., Lopez, J., Plow, E., Simon, D.I. J. Exp. Med. (2003) [Pubmed]
  7. Platelet glycoprotein ibalpha is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18). Simon, D.I., Chen, Z., Xu, H., Li, C.Q., Dong, J., McIntire, L.V., Ballantyne, C.M., Zhang, L., Furman, M.I., Berndt, M.C., López, J.A. J. Exp. Med. (2000) [Pubmed]
  8. Distinct mechanisms of platelet aggregation as a consequence of different shearing flow conditions. Goto, S., Ikeda, Y., Saldívar, E., Ruggeri, Z.M. J. Clin. Invest. (1998) [Pubmed]
  9. Complementary DNA cloning of the alternatively expressed endothelial cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb beta gene to chromosome 22. Kelly, M.D., Essex, D.W., Shapiro, S.S., Meloni, F.J., Druck, T., Huebner, K., Konkle, B.A. J. Clin. Invest. (1994) [Pubmed]
  10. Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease. Matsubara, Y., Murata, M., Sugita, K., Ikeda, Y. J. Thromb. Haemost. (2003) [Pubmed]
  11. Bernard-Soulier syndrome Kagoshima: Ser 444-->stop mutation of glycoprotein (GP) Ib alpha resulting in circulating truncated GPIb alpha and surface expression of GPIb beta and GPIX. Kunishima, S., Miura, H., Fukutani, H., Yoshida, H., Osumi, K., Kobayashi, S., Ohno, R., Naoe, T. Blood (1994) [Pubmed]
  12. The von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. Characterization by monoclonal antibodies and partial amino acid sequence analysis of proteolytic fragments. Handa, M., Titani, K., Holland, L.Z., Roberts, J.R., Ruggeri, Z.M. J. Biol. Chem. (1986) [Pubmed]
  13. Trp207Gly in platelet glycoprotein Ibalpha is a novel mutation that disrupts the connection between the leucine-rich repeat domain and the disulfide loop structure and causes Bernard-Soulier syndrome. Rosenberg, N., Lalezari, S., Landau, M., Shenkman, B., Seligsohn, U., Izraeli, S. J. Thromb. Haemost. (2007) [Pubmed]
  14. Amino acid requirement of adenovirus multiplication. Wigand, R., Kümel, G. J. Gen. Virol. (1978) [Pubmed]
  15. Neutrophil cathepsin G modulates the platelet surface expression of the glycoprotein (GP) Ib-IX complex by proteolysis of the von Willebrand factor binding site on GPIb alpha and by a cytoskeletal-mediated redistribution of the remainder of the complex. LaRosa, C.A., Rohrer, M.J., Benoit, S.E., Barnard, M.R., Michelson, A.D. Blood (1994) [Pubmed]
  16. Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Ibalpha mechanoreceptor. Mazzucato, M., Pradella, P., Cozzi, M.R., De Marco, L., Ruggeri, Z.M. Blood (2002) [Pubmed]
  17. 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. Miller, J.L., Lyle, V.A., Cunningham, D. Blood (1992) [Pubmed]
  18. High molecular weight kininogen regulates platelet-leukocyte interactions by bridging Mac-1 and glycoprotein Ib. Chavakis, T., Santoso, S., Clemetson, K.J., Sachs, U.J., Isordia-Salas, I., Pixley, R.A., Nawroth, P.P., Colman, R.W., Preissner, K.T. J. Biol. Chem. (2003) [Pubmed]
  19. Influence of monoclonal antiplatelet glycoprotein antibodies on in vitro human megakaryocyte colony formation and proplatelet formation. Takahashi, R., Sekine, N., Nakatake, T. Blood (1999) [Pubmed]
  20. Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site. Dong, J.F., Sae-Tung, G., López, J.A. Blood (1997) [Pubmed]
  21. Binding of platelet glycoprotein Ibalpha to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS13. Nishio, K., Anderson, P.J., Zheng, X.L., Sadler, J.E. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  22. Variant Bernard-Soulier syndrome associated with a homozygous mutation in the leucine-rich domain of glycoprotein IX. Clemetson, J.M., Kyrle, P.A., Brenner, B., Clemetson, K.J. Blood (1994) [Pubmed]
  23. Reconstitution of adhesive properties of human platelets in liposomes carrying both recombinant glycoproteins Ia/IIa and Ib alpha under flow conditions: specific synergy of receptor-ligand interactions. Nishiya, T., Kainoh, M., Murata, M., Handa, M., Ikeda, Y. Blood (2002) [Pubmed]
  24. Surface expression of glycoprotein ib alpha is dependent on glycoprotein ib beta: evidence from a novel mutation causing Bernard-Soulier syndrome. Moran, N., Morateck, P.A., Deering, A., Ryan, M., Montgomery, R.R., Fitzgerald, D.J., Kenny, D. Blood (2000) [Pubmed]
  25. Filamin A binding to the cytoplasmic tail of glycoprotein Ibalpha regulates von Willebrand factor-induced platelet activation. Feng, S., Reséndiz, J.C., Lu, X., Kroll, M.H. Blood (2003) [Pubmed]
  26. Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha. Takafuta, T., Wu, G., Murphy, G.F., Shapiro, S.S. J. Biol. Chem. (1998) [Pubmed]
  27. Factor XI interacts with the leucine-rich repeats of glycoprotein Ibalpha on the activated platelet. Baglia, F.A., Shrimpton, C.N., Emsley, J., Kitagawa, K., Ruggeri, Z.M., López, J.A., Walsh, P.N. J. Biol. Chem. (2004) [Pubmed]
  28. Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit. Pidard, D., Renesto, P., Berndt, M.C., Rabhi, S., Clemetson, K.J., Chignard, M. Biochem. J. (1994) [Pubmed]
  29. In vitro function of platelet concentrates prepared after filtration of whole blood or buffy coat pools. Turner, C.P., Sutherland, J., Wadhwa, M., Dilger, P., Cardigan, R. Vox Sang. (2005) [Pubmed]
  30. Role of the intracellular domains of GPIb in controlling the adhesive properties of the platelet GPIb/V/IX complex. Perrault, C., Mangin, P., Santer, M., Baas, M.J., Moog, S., Cranmer, S.L., Pikovski, I., Williamson, D., Jackson, S.P., Cazenave, J.P., Lanza, F. Blood (2003) [Pubmed]
  31. Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane. Modderman, P.W., Admiraal, L.G., Sonnenberg, A., von dem Borne, A.E. J. Biol. Chem. (1992) [Pubmed]
  32. Impaired megakaryocytopoiesis in type 2B von Willebrand disease with severe thrombocytopenia. Nurden, P., Debili, N., Vainchenker, W., Bobe, R., Bredoux, R., Corvazier, E., Combrie, R., Fressinaud, E., Meyer, D., Nurden, A.T., Enouf, J. Blood (2006) [Pubmed]
  33. Glycoprotein VI is associated with GPIb-IX-V on the membrane of resting and activated platelets. Arthur, J.F., Gardiner, E.E., Matzaris, M., Taylor, S.G., Wijeyewickrema, L., Ozaki, Y., Kahn, M.L., Andrews, R.K., Berndt, M.C. Thromb. Haemost. (2005) [Pubmed]
  34. The effect of air and nitrox divings on platelet activation tested by flow cytometry. Baj, Z., Olszański, R., Majewska, E., Konarski, M. Aviation, space, and environmental medicine. (2000) [Pubmed]
  35. Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness. Murata, M., Furihata, K., Ishida, F., Russell, S.R., Ware, J., Ruggeri, Z.M. Blood (1992) [Pubmed]
 
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