Abstract
Studies have shown that thrombin stimulates the activation of extracellular regulated kinase (ERK 1/2) and Rho/Rho Kinase, which are associated with cellular proliferation and migration in vascular diseases such as hypertrophy and atherosclerosis. Thrombin activates these kinases through protease activated receptors (PARs). PARs are a subfamily of G‐protein coupled receptors activated by proteolytic cleavage. PAR‐1, the prototype receptor, is known to mediate vascular smooth muscle cell (VSMC) migration, the hallmark of atherogenesis. However, little is known in regards to PAR‐4 function in VSMCs. To elucidate a role for PAR‐4 in VSMCs, we utilized PAR‐4 activating peptide AYPGKF to probe receptor function. AYPGKF induced approximately a 4‐fold increase in migration of VSMCs. We also observed rapid phosphorylation of a Rho kinase substrate, myosin light chain phosphatase (MYPT), and sustained phosphorylation of ERK.
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