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Biochemistry (Mosc). 2002 Jan;67(1):56-64.

Thrombin regulation of cell function through protease-activated receptors: implications for therapeutic intervention.

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  • 1The R. W. Johnson Pharmaceutical Research Institute, Welsh and McKean Roads, PO Box 776, Spring House, PA 19477-0776, USA.


The serine protease thrombin is well recognized as being pivotal to the maintenance of hemostasis under both normal and pathological conditions. Its cellular actions are mediated through a unique family of protease-activated receptors (PARs). These receptors represent a novel family of G protein-coupled receptors that undergo proteolytic cleavage of their amino terminus and subsequent autoactivation by a tethered peptide ligand. This paper reviews the consequences of PAR activation in thrombosis, vascular injury, inflammation, tissue injury, and within the tumor microenvironment.

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