Thrombin regulation of cell function through protease-activated receptors: implications for therapeutic intervention.
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.
Derian
C K
CK
The R. W. Johnson Pharmaceutical Research Institute, Welsh and McKean Roads, PO Box 776, Spring House, PA 19477-0776, USA.
Damiano
B P
BP
D'Andrea
M R
MR
Andrade-Gordon
P
P
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D009369:Neoplasms / Q000378:metabolism; D044463:Receptor, PAR-1; D018179:Receptors, Thrombin / Q000378:metabolism*; D013917:Thrombin / Q000378:metabolism*; D013927:Thrombosis
D044463:Receptor, PAR-1; D018179:Receptors, Thrombin; C105295:protease-activated receptor 3; D010450:Endopeptidases; D013917:Thrombin; C112908:protease-activated receptor 4