Abstract
Thrombin, a serine protease, is a potent platelet agonist that signals primarily through the protease-activated receptors (PARs). The PAR family contains four G-protein coupled receptors (GPCRs), named PARs1–4, that are activated by enzymatic cleavage of the N-terminus to expose a tethered ligand that intramolecularly activates the receptor. The expression profile of PARs on platelets is species-specific; PAR1 and PAR4 are expressed on human platelets and are the focus of this chapter. PAR1 and PAR4 interact with thrombin through distinct mechanisms. Once activated, PARs mediate signaling through overlapping pathways with distinct kinetics. PAR1 signaling is rapid and short-lived, while PAR4 initiates slower but sustained signaling. PARs have become important targets for antiplatelet therapies and the development of PAR antagonists has facilitated a greater understanding of their molecular structure and physiological roles in vivo.
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