In biochemistry and medicine, glycoprotein IIb/IIIa (GPIIb/IIIa, also known as integrin αIIbβ3) is an integrin complex found on platelets. It is a transmembrane receptor for fibrinogen[1] and von Willebrand factor, and aids platelet activation. The complex is formed via calcium-dependent association of gpIIb and gpIIIa, a required step in normal platelet aggregation and endothelial adherence.[2][3] Platelet activation by ADP (blocked by clopidogrel) leads to the aforementioned conformational change in platelet gpIIb/IIIa receptors that induces binding to fibrinogen.[1] The gpIIb/IIIa receptor is a target of several drugs including abciximab, eptifibatide, and tirofiban.
^ abVickers JD (July 1999). "Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin". Platelets. 10 (4): 228–37. doi:10.1080/09537109976077. PMID16801097.
^Calvete JJ (April 1995). "On the structure and function of platelet integrin alpha IIb beta 3, the fibrinogen receptor". Proceedings of the Society for Experimental Biology and Medicine. 208 (4): 346–60. doi:10.3181/00379727-208-43863a. PMID7535429. S2CID9298838.
^Shattil SJ (August 1999). "Signaling through platelet integrin alpha IIb beta 3: inside-out, outside-in, and sideways". Thrombosis and Haemostasis. 82 (2): 318–25. doi:10.1055/s-0037-1615849. PMID10605720. S2CID83902334.