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Open Access Pathophysiological actions of protease activated receptors (PARs)

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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.

Document Type: Research Article


Affiliations: 1: Department of Pharmacology, C. U. Shah College of Pharmacy and Research, Wadhwan City, Dist. Surendranagar, 363030, India,, Email: 2: Department of Pharmacology, L. M. College of Pharmacy, Strasse, Navrangpura, Ahmedabad, India

Publication date: March 1, 2007

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  • Pharmazie is one of the world's leading pharmaceutical journals. As a peer-reviewed scientific journal, DiePharmazie is regularly indexed in Current Contents/Life Sciences, Excerpta Medica, Analytical Abstracts, International Pharmaceutical Abstracts, Beilstein Current Facts in Chemistry, Chemical Engineering and Biotechnology Abstracts (CEABA) and Science Citation Index.
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