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Both proteases prominently induced the angiogenesis-promoting geneCyr61 and connective tissue growth factor. Inhibition of PAR-1 cleavage abolished MAP kinase phosphorylation and gene induction by Xa, demonstrating that Xa signals through PAR-1 and not through a novel member of the PAR family. Activation of cell surface prothrombin with the snake venom enzyme Ecarin also produced PAR-1\u2013dependent signaling. However, though the response to Ecarin was completely blocked by the thrombin inhibitor hirudin, the response to Xa was not. This suggests that the Xa response is not mediated by locally generated thrombin. The concentration dependence of Xa for PAR-1 activation is consistent with previously characterized Xa-mediated PAR-2 signaling, suggesting that local concentration of Xa on the cell surface, rather than sequence-specific recognition of the PAR scissile bond, determines receptor cleavage. This study demonstrates that PAR-1 cleavage by Xa can elicit the same cellular response as thrombin, but mechanistic differences in receptor recognition may be crucial for specific roles for Xa in signaling during spatial or temporal separation from thrombin generation.<\/jats:p>","DOI":"10.1182\/blood.v97.10.3109","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T12:46:40Z","timestamp":1027774000000},"page":"3109-3116","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":152,"title":["Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1"],"prefix":"10.1182","volume":"97","author":[{"given":"Matthias","family":"Riewald","sequence":"first","affiliation":[{"name":"From the Department of Immunology and Vascular Biology, The Scripps Research Institute, La Jolla, CA; and the Department of Medicine and Pharmacology, University of Pennsylvania, 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