Biology:GP5 (gene)

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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

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]

See also

• Cluster of differentiation

Further reading

• "Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane.". J. Biol. Chem. 267 (1): 364–9. 1992. doi:10.1016/S0021-9258(18)48503-1. PMID 1730602. 
• "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. 1990. doi:10.1182/blood.V75.12.2349.2349. PMID 2350580. 
• "Human platelet glycoprotein V: a surface leucine-rich glycoprotein related to adhesion.". Biochem. Biophys. Res. Commun. 170 (1): 153–61. 1990. doi:10.1016/0006-291X(90)91253-O. PMID 2372284. 
• "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. 1993. doi:10.1073/pnas.90.18.8327. PMID 7690959. Bibcode: 1993PNAS...90.8327H. 
• "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. 1995. doi:10.1074/jbc.270.24.14693. PMID 7782333. 
• "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. 1995. PMID 7900083. 
• "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. 1993. doi:10.1016/S0021-9258(19)36855-3. PMID 8407908. 
• "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. 1996. doi:10.1021/bi00049a028. PMID 8519770. 
• "Alpha-granule membrane mirrors the platelet plasma membrane and contains the glycoproteins Ib, IX, and V.". Blood 87 (4): 1385–95. 1996. doi:10.1182/blood.V87.4.1385.bloodjournal8741385. PMID 8608228. 
• "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. 1997. doi:10.1182/blood.V89.9.3253. PMID 9129030. 
• "Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex.". Blood 90 (4): 1508–15. 1997. doi:10.1182/blood.V90.4.1508. PMID 9269768. 
• "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. 1997. doi:10.1182/blood.V90.7.2660. PMID 9326233. 
• "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. 1998. doi:10.1021/bi970893g. PMID 9425086. 
• "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. 1999. doi:10.1046/j.1432-1327.1999.00467.x. PMID 10429193. 
• "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. 2002. PMID 11686325. 
• "Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V.". J. Biol. Chem. 280 (15): 14462–8. 2005. doi:10.1074/jbc.M500041200. PMID 15691827. 
• "Aspirin induces platelet receptor shedding via ADAM17 (TACE).". J. Biol. Chem. 280 (48): 39716–22. 2006. doi:10.1074/jbc.M507762200. PMID 16179345. 
• "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.". Mol. Cell. Proteomics 5 (2): 226–33. 2006. doi:10.1074/mcp.M500324-MCP200. PMID 16263699. http://www.mcponline.org/content/5/2/226.full.pdf. 

External links

• GP5+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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