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- W2785193670 abstract "Thrombin, the most potent platelet agonist in vivo, activates human platelets through PAR1 (protease-activated receptor 1) and PAR4 (protease-activated receptor 4) by proteolysis of the N terminus, which exposes the tethered ligands.1 Although these receptors are activated by the same mechanism, the overall sequence identity is only ≈33%, and each has a distinct mode of interaction with thrombin, which impacts the subsequent rates of proteolysis.2–4 PAR1 is an efficient substrate and responds to subnanomolar thrombin. In contrast, PAR4 requires ≈10-fold more thrombin for proteolysis. This difference led to the hypothesis that PAR4 was a redundant backup thrombin receptor, which limited the interest in developing PAR4 antagonists.See accompanying article on page 448 On further examination, the dual receptor system offers the intriguing possibility of pharmacologically fine-tuning thrombin signaling in platelets by taking advantage of the individual contributions of PAR1 and PAR4.5 Both receptors initiate signaling through Gq and G12/13 pathways but with distinct kinetics. PAR1 activation results in a rapid transient signal. In contrast, PAR4 mediates prolonged signaling that is required for stable thrombus formation (Figure [A]). Blocking the sustained signaling from PAR4 may limit thrombosis, while leaving the transient PAR1 signaling mechanism available to initiate hemostasis and limit bleeding (Figure [B]). With this goal in mind, PAR4 has been targeted with inhibitory antibodies, intracellular peptides, and small molecules.6–8 Several compounds that achieve PAR4 antagonism, such as YD-3 and ML354, are currently used as tools to study PAR4 …" @default.
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- W2785193670 date "2018-02-01" @default.
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- W2785193670 title "PAR4 (Protease-Activated Receptor 4)" @default.
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- W2785193670 doi "https://doi.org/10.1161/atvbaha.117.310550" @default.
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