Glycoprotein V (platelet) (GP5) also known asCD42d (Cluster ofDifferentiation42d), is a humangene.[5]
Human platelet glycoprotein V (GP5) is a part of theIb-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][5]
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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.PMID11686325.