Which platelet receptor is critical for platelet aggregation?

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The Glycoprotein IIb/IIIa receptor is fundamentally important for platelet aggregation because it serves as the main receptor that binds fibrinogen, which acts as a bridge between platelets. When platelets are activated, they express Glycoprotein IIb/IIIa on their surface, allowing them to stick together and form a platelet plug. This receptor plays a pivotal role in the final common pathway of platelet activation, where the binding of fibrinogen or von Willebrand factor (vWF) promotes the clustering of platelets, leading to aggregation and thrombus formation.

The other receptors mentioned have distinct functions. The P2Y12 receptor is primarily involved in the amplification of platelet activation by responding to ADP, but it does not directly mediate aggregation. Glycoprotein Ib is crucial for platelet adhesion to the damaged vascular wall, particularly in binding to vWF, but it does not play a role in the aggregation process itself. Integrin α2β1 is associated with platelet adhesion to collagen, aiding in the initial stages of platelet interaction with the subendothelial matrix but is not the key player in the aggregation process. Therefore, the Glycoprotein IIb/IIIa receptor's function in mediating the

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