Abstract
Platelet integrin αIIbβ3 a prototypic non-I domain integrin, plays an essential role in platelet aggregation. The structure and function of αIIbβ3 is dramatically changed during platelet plug formation and pathological thrombus formation. The function of this integrin is regulated by the balance of actions of positive and negative regulatory factors. Several novel regulators have emerged from recent studies. As a positive regulator, the P2Y12 plays a critical role in thrombus stability; and continuous interaction between ADP and P2Y12 is essential for sustained αIIbβ3 activation. Semaphorin 3A and SHPS-1 have been identified as negative regulators. These molecules are secreted from or expressed on endothelial cells and inhibit the function of platelets as well as αIIbβ3. Investigation on these positive and negative regulatory factors should provide a new insight into the treatment of pathological thrombosis.
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