GP5 (gene)

This article is about the glycoprotein V. For the GP5 computer chip, see GP5 chip. For the Soviet-era civilian gas mask, see GP-5 gas mask.

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

GP5
Identifiers
Aliases	GP5, CD42d, GPV, glycoprotein V platelet
External IDs	OMIM: 173511; MGI: 1096363; HomoloGene: 74523; GeneCards: GP5; OMA:GP5 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q29 Start 194,394,821 bp End 194,399,266 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16|16 B2 Start 30,126,503 bp End 30,129,597 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte trabecular bone right uterine tube bronchial epithelial cell granulocyte lymph node blood appendix bone marrow gallbladder Top expressed in tibiofemoral joint blood morula blastocyst embryo spleen embryo yolk sac abdominal wall bone marrow More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component integral component of membrane plasma membrane integral component of plasma membrane extracellular exosome membrane extracellular space Biological process platelet activation blood coagulation, intrinsic pathway hemostasis cell adhesion blood coagulation axonogenesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2814 14729 Ensembl ENSG00000178732 ENSMUSG00000047953 UniProt P40197 O08742 Q9QZU3 RefSeq (mRNA) NM_004488 NM_008148 RefSeq (protein) NP_004479 NP_032174 Location (UCSC) Chr 3: 194.39 – 194.4 Mb Chr 16: 30.13 – 30.13 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

• 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. doi:10.1016/S0021-9258(18)48503-1. 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. doi:10.1182/blood.V75.12.2349.2349. 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. Bibcode:1993PNAS...90.8327H. doi:10.1073/pnas.90.18.8327. PMC 47349. 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 7950083.
• 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. doi:10.1016/S0021-9258(19)36855-3. 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. doi:10.1182/blood.V87.4.1385.bloodjournal8741385. 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. doi:10.1182/blood.V89.9.3253. 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. doi:10.1182/blood.V90.4.1508. 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. doi:10.1182/blood.V90.7.2660. 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" (PDF). Mol. Cell. Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699. S2CID 7856143.

External links

• GP5 protein, human at the U.S. 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.