The human platelet membrane glycoprotein IIb/IIIa complex: a multi functional adhesion receptor

Abstract

The glycoprotein GPIIb/IIIa complex is a major constituent of the platelet membrane; it plays an important role in platelet adhesion and aggregation. The complex is a member of the integrin superfamily. Integrins are related membrane receptors which mediate the adhesive interactions of a variety of cells; they specifically recognize the arginine-glycine-aspartic acid (RGD) sequence present in several adhesive proteins. The GPIIb/IIIa complex of activated platelets can bind fibrinogen, von Willebrand factor, fibronectin, vitronectin and thrombospondin. Platelets are activated by a variety of signals including extracellular matrix molecules and soluble factors; upon platelet activation the complex undergoes a conformational change, thus permitting the macromolecular ligands access to their binding sites. In turn, fibrinogen binding results in a receptor modification and neoantigens exposure; such events may participate in signal transduction. The adhesive proteins compete reciprocally for binding to GPIIb/IIIa, and the complex binds to different domains of them, thus creating multiple interactions with the ligands.