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Volume 272, Number 7, Issue of February 14, 1997 pp. 4043-4049
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Interactions of Mast Cell Tryptase with Thrombin Receptors and PAR-2

(Received for publication, October 3, 1996)

Marina Molino Dagger § , Elliot S. Barnathan Dagger , Robert Numerof ** , Jim Clark ** , Mark Dreyer ** , Albana Cumashi Dagger § , James A. Hoxie Dagger , Norman Schechter Dagger Dagger , Marilyn Woolkalis §§ and Lawrence F. Brass Dagger ¶¶

From the Departments of Dagger  Medicine, ¶¶ Pathology, and Dagger Dagger  Dermatology and the ¶¶ Center for Experimental Therapeutics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, the § Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Santa Maria Imbaro, Italy, the §§ Department of Physiology of Thomas Jefferson University, Philadelphia, Pennsylvania 19107, and ** Arris Pharmaceutical Corporation, South San Francisco, California 94080

Tryptase is a serine protease secreted by mast cells that is able to activate other cells. In the present studies we have tested whether these responses could be mediated by thrombin receptors or PAR-2, two G-protein-coupled receptors that are activated by proteolysis. When added to a peptide corresponding to the N terminus of PAR-2, tryptase cleaved the peptide at the activating site, but at higher concentrations it also cleaved downstream, as did trypsin, a known activator of PAR-2. Thrombin, factor Xa, plasmin, urokinase, plasma kallikrein, and tissue kallikrein had no effect. Tryptase also cleaved the analogous thrombin receptor peptide at the activating site but less efficiently. When added to COS-1 cells expressing either receptor, tryptase stimulated phosphoinositide hydrolysis. With PAR-2, this response was half-maximal at 1 nM tryptase and could be inhibited by the tryptase inhibitor, APC366, or by antibodies to tryptase and PAR-2. When added to human endothelial cells, which normally express PAR-2 and thrombin receptors, or keratinocytes, which express only PAR-2, tryptase caused an increase in cytosolic Ca2+. However, when added to platelets or CHRF-288 cells, which express thrombin receptors but not PAR-2, tryptase caused neither aggregation nor increased Ca2+. These results show that 1) tryptase has the potential to activate both PAR-2 and thrombin receptors; 2) for PAR-2, this potential is realized, although cleavage at secondary sites may limit activation, particularly at higher tryptase concentrations; and 3) in contrast, although tryptase clearly activates thrombin receptors in COS-1 cells, it does not appear to cleave endogenous thrombin receptors in platelets or CHRF-288 cells. These distinctions correlate with the observed differences in the rate of cleavage of the PAR-2 and thrombin receptor peptides by tryptase. Tryptase is the first protease other than trypsin that has been shown to activate human PAR-2. Its presence within mast cell granules places it in tissues where PAR-2 is expressed but trypsin is unlikely to reach.


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