Integrins and platelet adhesion receptors (IPAR)

Integrins and platelet adhesion receptors are a diverse group of cell surface glycoproteins essential for the primary hemostatic response. The most prominent member is the integrin alpha-IIb/beta-3 (GPIIb/IIIa), which undergoes a conformational change upon platelet activation to bind fibrinogen and mediate platelet aggregation. Other critical receptors include the Glycoprotein Ib-IX-V complex, which binds von Willebrand factor to initiate platelet tethering under high shear stress, and Glycoprotein VI (GPVI), which serves as the primary signaling receptor for collagen. These receptors are central to the pathogenesis of arterial thrombosis, leading to conditions such as myocardial infarction and ischemic stroke. Consequently, they are major therapeutic targets for antiplatelet drugs, including GPIIb/IIIa inhibitors like abciximab and tirofiban, which are used to prevent ischemic complications during percutaneous coronary interventions. While highly effective at preventing clot formation, pharmacological modulation of these receptors carries a significant risk of bleeding due to their fundamental role in normal hemostasis.

Other names

Platelet adhesion receptorsPlatelet integrinsPlatelet glycoprotein receptorsThrombocyte adhesion molecules

Drugs targeting these receptors typically act as antagonists or inhibitors to prevent the binding of ligands such as fibrinogen, von Willebrand factor (vWF), or collagen, thereby inhibiting platelet adhesion, activation, and aggregation to prevent thrombus formation.