title: Thrombin regulation of cell function through protease-activated receptors: implications for therapeutic intervention.
abstract: 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.
authors.affiliation: The R. W. Johnson Pharmaceutical Research Institute, Welsh and McKean Roads, PO Box 776, Spring House, PA 19477-0776, USA.
authors.forename: C K
authors.initials: CK
authors.lastname: Derian
authors.forename: B P
authors.initials: BP
authors.lastname: Damiano
authors.forename: M R
authors.initials: MR
authors.lastname: D'Andrea
authors.forename: P
authors.initials: P
authors.lastname: Andrade-Gordon
mesh_terms: 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
chemical_list: D044463:Receptor, PAR-1; D018179:Receptors, Thrombin; C105295:protease-activated receptor 3; D010450:Endopeptidases; D013917:Thrombin; C112908:protease-activated receptor 4