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Platelet surface receptors are a diverse group of membrane proteins that orchestrate the response of platelets to vascular injury. This group includes adhesion receptors like the Glycoprotein Ib-IX-V complex and Glycoprotein VI, which recognize von Willebrand factor and collagen in the exposed subendothelial matrix, respectively [Rivera et al., 2009]. Following initial adhesion, activation receptors such as the G protein-coupled receptors P2Y12 and Protease-activated receptors (PAR1 and PAR4) respond to soluble agonists like ADP and thrombin to amplify the platelet response [Gachet, 2006]. The final common pathway of platelet activation involves the conformational change of Integrin alpha-IIb beta-3 (GPIIb/IIIa), which enables platelet aggregation via fibrinogen bridging [Shattil et al., 1998]. Because of their central role in arterial thrombosis, these receptors are primary targets for antiplatelet therapy in cardiovascular diseases such as myocardial infarction and stroke [Angiolillo et al., 2017]. Pharmacological modulation of these receptors, while effective in reducing ischemic events, carries an inherent risk of bleeding complications due to the impairment of physiological hemostasis [Serebruany et al., 2004].
Inhibition of platelet activation and aggregation through the antagonism of specific surface receptors, including P2Y12 (ADP receptor), PAR1 (thrombin receptor), and Integrin alpha-IIb beta-3 (fibrinogen receptor) [Angiolillo et al., 2017].
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