Platelet glycoprotein V (GP5)

Platelet glycoprotein V (GP5, CD42d) is a membrane glycoprotein that forms part of the GPIb-V-IX receptor complex on platelet surfaces, primarily serving as a regulatory component within the broader receptor for von Willebrand factor (VWF)[1][2]. This complex mediates platelet adhesion to injured vascular surfaces—an essential first step in hemostasis[1][2]. GP5 is cleaved by thrombin during platelet activation, and the shed soluble form (sGPV) specifically limits thrombin-dependent fibrin formation, spatially and temporally restricting thrombus growth at vascular injury sites[3]. Mutations in the GPIb-V-IX complex (though not GP5 alone) can cause Bernard-Soulier syndrome, a rare bleeding disorder[1][2]. GP5's modulation of thrombin activity at sites of injury means it may represent a future therapeutic target for selectively enhancing hemostatic fibrin formation where platelet function is deficient, with research ongoing to exploit this without increasing the risk of systemic thrombosis or bleeding[3].

Other names

Platelet glycoprotein VGP5CD42dGPVGlycoprotein 5glycoprotein V plateletplatelet glycoprotein 5

Experimental blockade of thrombin-mediated shedding of GP5 enhances local fibrin formation and hemostasis in models with platelet function defects[3].\nRecombinant GP5 can limit thrombin-mediated fibrin generation and potentially reduce thrombo-inflammatory damage without increasing bleeding risk[3].