GP5

This article is about the glycoprotein V. For the GP5 computer chip, see GP5 chip.
GP5
Identifiers
Aliases GP5, CD42d, GPV, glycoprotein V platelet
External IDs MGI: 1096363 HomoloGene: 74523 GeneCards: GP5
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

2814

14729

Ensembl

ENSG00000178732

ENSMUSG00000047953

UniProt

P40197

O08742

RefSeq (mRNA)

NM_004488

NM_008148

RefSeq (protein)

NP_004479.1

n/a

Location (UCSC) Chr 3: 194.39 – 194.4 Mb Chr 16: 30.31 – 30.31 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene.[3]

Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 193400) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder.[supplied by OMIM][3]

See also

References

Further reading

  • 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. 
  • Shimomura T, Fujimura K, Maehama S, et al. (1990). "Rapid purification and characterization of human platelet glycoprotein V: the amino acid sequence contains leucine-rich repetitive modules as in glycoprotein Ib.". Blood. 75 (12): 2349–56. PMID 2350580. 
  • Roth GJ, Church TA, McMullen BA, Williams SA (1990). "Human platelet glycoprotein V: a surface leucine-rich glycoprotein related to adhesion.". Biochem. Biophys. Res. Commun. 170 (1): 153–61. doi:10.1016/0006-291X(90)91253-O. PMID 2372284. 
  • Hickey MJ, Hagen FS, Yagi M, Roth GJ (1993). "Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins.". Proc. Natl. Acad. Sci. U.S.A. 90 (18): 8327–31. doi:10.1073/pnas.90.18.8327. PMC 47349Freely accessible. PMID 7690959. 
  • Meyer SC, Fox JE (1995). "Interaction of platelet glycoprotein V with glycoprotein Ib-IX regulates expression of the glycoproteins and binding of von Willebrand factor to glycoprotein Ib-IX in transfected cells.". J. Biol. Chem. 270 (24): 14693–9. doi:10.1074/jbc.270.24.14693. PMID 7782333. 
  • Takafuta T, Fujimura K, Kawano H, et al. (1995). "Expression of platelet membrane glycoprotein V in human megakaryocytes and megakaryocytic cell lines: a study using a novel monoclonal antibody against GPV.". Thromb. Haemost. 72 (5): 762–9. PMID 7900083. 
  • Lanza F, Morales M, de La Salle C, et al. (1993). "Cloning and characterization of the gene encoding the human platelet glycoprotein V. A member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation.". J. Biol. Chem. 268 (28): 20801–7. PMID 8407908. 
  • Yagi M, Edelhoff S, Disteche CM, Roth GJ (1996). "Human platelet glycoproteins V and IX: mapping of two leucine-rich glycoprotein genes to chromosome 3 and analysis of structures.". Biochemistry. 34 (49): 16132–7. doi:10.1021/bi00049a028. PMID 8519770. 
  • Berger G, Massé JM, Cramer EM (1996). "Alpha-granule membrane mirrors the platelet plasma membrane and contains the glycoproteins Ib, IX, and V.". Blood. 87 (4): 1385–95. PMID 8608228. 
  • Ravanat C, Morales M, Azorsa DO, et al. (1997). "Gene cloning of rat and mouse platelet glycoprotein V: identification of megakaryocyte-specific promoters and demonstration of functional thrombin cleavage.". Blood. 89 (9): 3253–62. PMID 9129030. 
  • Bradford HN, Dela Cadena RA, Kunapuli SP, et al. (1997). "Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex.". Blood. 90 (4): 1508–15. PMID 9269768. 
  • Wu G, Essex DW, Meloni FJ, et al. (1997). "Human endothelial cells in culture and in vivo express on their surface all four components of the glycoprotein Ib/IX/V complex.". Blood. 90 (7): 2660–9. PMID 9326233. 
  • Andrews RK, Harris SJ, McNally T, Berndt MC (1998). "Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex.". Biochemistry. 37 (2): 638–47. doi:10.1021/bi970893g. PMID 9425086. 
  • Longhurst CM, White MM, Wilkinson DA, Jennings LK (1999). "A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states.". Eur. J. Biochem. 263 (1): 104–11. doi:10.1046/j.1432-1327.1999.00467.x. PMID 10429193. 
  • Dicker IB, Pedicord DL, Seiffert DA, et al. (2002). "Both the high affinity thrombin receptor (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin-induced platelet procoagulant activity.". Thromb. Haemost. 86 (4): 1065–9. PMID 11686325. 
  • Rabie T, Strehl A, Ludwig A, Nieswandt B (2005). "Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V.". J. Biol. Chem. 280 (15): 14462–8. doi:10.1074/jbc.M500041200. PMID 15691827. 
  • Aktas B, Pozgajova M, Bergmeier W, et al. (2006). "Aspirin induces platelet receptor shedding via ADAM17 (TACE).". J. Biol. Chem. 280 (48): 39716–22. doi:10.1074/jbc.M507762200. PMID 16179345. 
  • Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.". Mol. Cell Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699. 

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


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