Serine proteases such as thrombin, mast cell tryptase, trypsin, or cathepsin G, for example, are highly active mediators with diverse biological activities. So far, proteases have been considered to act primarily as degradative enzymes in the extracellular space. However, their biological
actions in tissues and cells suggest important roles as a part of the body's hormonal communication system during inflammation and immune response. These effects can be attributed to the activation of a new subfamily of G protein-coupled receptors, termed protease-activated receptors
(PARs). Four members of the PAR family have been cloned so far. Thus, certain proteases act as signaling molecules that specifically regulate cells by activating PARs. After stimulation, PARs couple to various G proteins and activate signal transduction pathways resulting in the rapid transcription
of genes that are involved in inflammation. For example, PARs are widely expressed by cells involved in immune responses and inflammation, regulate endothelial-leukocyte interactions, and modulate the secretion of inflammatory mediators or neuropeptides. Together, the PAR family necessitates
a paradigm shift in thinking about hormone action, to include proteases as key modulators of biological function. Novel compounds that can modulate PAR function may be potent candidates for the treatment of inflammatory or immune diseases.
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Document Type: Research Article
Department of Pharmacology, C. U. Shah College of Pharmacy and Research, Wadhwan City, Dist. Surendranagar, 363030, India, [email protected], Email: [email protected]
Department of Pharmacology, L. M. College of Pharmacy, Strasse, Navrangpura, Ahmedabad, India
Publication date: 01 March 2007
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