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词条 GP5
释义

  1. See also

  2. References

  3. Further reading

  4. External links

{{about|the glycoprotein V| the GP5 computer chip |GP5 chip | the Soviet-era civilian gas mask |GP-5 gas mask }}{{Infobox_gene}}Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene.[1]

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][1]

See also

  • Cluster of differentiation

References

1. ^1 {{cite web | title = Entrez Gene: GP5 glycoprotein V (platelet)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2814| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE |title=Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 364–9 |year= 1992 |pmid= 1730602 |doi= }}
  • {{cite journal |vauthors=Shimomura T, Fujimura K, Maehama S |title=Rapid purification and characterization of human platelet glycoprotein V: the amino acid sequence contains leucine-rich repetitive modules as in glycoprotein Ib. |journal=Blood |volume=75 |issue= 12 |pages= 2349–56 |year= 1990 |pmid= 2350580 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Roth GJ, Church TA, McMullen BA, Williams SA |title=Human platelet glycoprotein V: a surface leucine-rich glycoprotein related to adhesion. |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 1 |pages= 153–61 |year= 1990 |pmid= 2372284 |doi=10.1016/0006-291X(90)91253-O }}
  • {{cite journal |vauthors=Hickey MJ, Hagen FS, Yagi M, Roth GJ |title=Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 18 |pages= 8327–31 |year= 1993 |pmid= 7690959 |doi=10.1073/pnas.90.18.8327 | pmc=47349 }}
  • {{cite journal |vauthors=Meyer SC, Fox JE |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14693–9 |year= 1995 |pmid= 7782333 |doi=10.1074/jbc.270.24.14693 }}
  • {{cite journal |vauthors=Takafuta T, Fujimura K, Kawano H |title=Expression of platelet membrane glycoprotein V in human megakaryocytes and megakaryocytic cell lines: a study using a novel monoclonal antibody against GPV. |journal=Thromb. Haemost. |volume=72 |issue= 5 |pages= 762–9 |year= 1995 |pmid= 7900083 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Lanza F, Morales M, de La Salle C |title=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. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 20801–7 |year= 1993 |pmid= 8407908 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Yagi M, Edelhoff S, Disteche CM, Roth GJ |title=Human platelet glycoproteins V and IX: mapping of two leucine-rich glycoprotein genes to chromosome 3 and analysis of structures. |journal=Biochemistry |volume=34 |issue= 49 |pages= 16132–7 |year= 1996 |pmid= 8519770 |doi=10.1021/bi00049a028 }}
  • {{cite journal |vauthors=Berger G, Massé JM, Cramer EM |title=Alpha-granule membrane mirrors the platelet plasma membrane and contains the glycoproteins Ib, IX, and V. |journal=Blood |volume=87 |issue= 4 |pages= 1385–95 |year= 1996 |pmid= 8608228 |doi= }}
  • {{cite journal |vauthors=Ravanat C, Morales M, Azorsa DO |title=Gene cloning of rat and mouse platelet glycoprotein V: identification of megakaryocyte-specific promoters and demonstration of functional thrombin cleavage. |journal=Blood |volume=89 |issue= 9 |pages= 3253–62 |year= 1997 |pmid= 9129030 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Bradford HN, Dela Cadena RA, Kunapuli SP |title=Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex. |journal=Blood |volume=90 |issue= 4 |pages= 1508–15 |year= 1997 |pmid= 9269768 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Wu G, Essex DW, Meloni FJ |title=Human endothelial cells in culture and in vivo express on their surface all four components of the glycoprotein Ib/IX/V complex. |journal=Blood |volume=90 |issue= 7 |pages= 2660–9 |year= 1997 |pmid= 9326233 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Andrews RK, Harris SJ, McNally T, Berndt MC |title=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. |journal=Biochemistry |volume=37 |issue= 2 |pages= 638–47 |year= 1998 |pmid= 9425086 |doi= 10.1021/bi970893g }}
  • {{cite journal |vauthors=Longhurst CM, White MM, Wilkinson DA, Jennings LK |title=A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states. |journal=Eur. J. Biochem. |volume=263 |issue= 1 |pages= 104–11 |year= 1999 |pmid= 10429193 |doi=10.1046/j.1432-1327.1999.00467.x }}
  • {{cite journal |vauthors=Dicker IB, Pedicord DL, Seiffert DA |title=Both the high affinity thrombin receptor (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin-induced platelet procoagulant activity. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1065–9 |year= 2002 |pmid= 11686325 |doi= |display-authors=etal}}
  • {{cite journal |vauthors=Rabie T, Strehl A, Ludwig A, Nieswandt B |title=Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V. |journal=J. Biol. Chem. |volume=280 |issue= 15 |pages= 14462–8 |year= 2005 |pmid= 15691827 |doi= 10.1074/jbc.M500041200 }}
  • {{cite journal |vauthors=Aktas B, Pozgajova M, Bergmeier W |title=Aspirin induces platelet receptor shedding via ADAM17 (TACE). |journal=J. Biol. Chem. |volume=280 |issue= 48 |pages= 39716–22 |year= 2006 |pmid= 16179345 |doi= 10.1074/jbc.M507762200 |display-authors=etal}}
  • {{cite journal |vauthors=Lewandrowski U, Moebius J, Walter U, Sickmann A |title=Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. |journal=Mol. Cell. Proteomics |volume=5 |issue= 2 |pages= 226–33 |year= 2006 |pmid= 16263699 |doi= 10.1074/mcp.M500324-MCP200 }}
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External links

  • {{MeshName|GP5+protein,+human}}
{{NLM content}}{{Clusters of differentiation}}{{membrane-protein-stub}}

1 : Clusters of differentiation
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