title: Pleiotropic effects of a vibrio extracellular protease on the activation of contact system.
abstract: Many proteases secreted by pathogenic bacteria can affect seriously on hemostatic system. We have reported that an extracellular zinc metalloprotease (named vEP-45) from Vibrio vulnificus ATCC29307 activates prothrombin to active thrombin, leading the formation of fibrin clot. In this study, the effects of vEP-45 on the intrinsic pathway of coagulation and the kallikrein/kinin system were examined. The protease could activate proteolytically clotting factor zymogens, including FXII, FXI, FX, and prothrombin, to their functional enzymes in vitro and plasma milieu. In addition, it could cleave plasma prekallikrein (PPK) to form an active kallikrein as well as actively digest high-molecular weight kininogen (HK), probably producing bradykinin. In fact, vEP-45 could induce a vascular permeability in a dose-dependent manner in vivo. Taken together, the results demonstrate that vEP-45 can activate plasma contact system by cleaving key zymogen molecules, participating in the intrinsic pathway of coagulation and the kallikrein/kinin system.
authors.affiliation: Department of Biomedical Science, BK21-plus Research Team for Bioactive Control Technology, National Research Center for Dementia, College of Natural Sciences, Chosun University, Gwangju 501-759, Republic of Korea.
authors.forename: Jung Eun
authors.initials: JE
authors.lastname: Park
authors.affiliation: Department of Biomedical Science, BK21-plus Research Team for Bioactive Control Technology, National Research Center for Dementia, College of Natural Sciences, Chosun University, Gwangju 501-759, Republic of Korea.
authors.forename: Jong Woo
authors.initials: JW
authors.lastname: Park
authors.affiliation: Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
authors.forename: Weontae
authors.initials: W
authors.lastname: Lee
authors.affiliation: Department of Biomedical Science, BK21-plus Research Team for Bioactive Control Technology, National Research Center for Dementia, College of Natural Sciences, Chosun University, Gwangju 501-759, Republic of Korea. Electronic address: jsplee@chosun.ac.kr.
authors.forename: Jung Sup
authors.initials: JS
authors.lastname: Lee
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001777:Blood Coagulation / Q000502:physiology*; D001920:Bradykinin / Q000378:metabolism; D002199:Capillary Permeability; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D006168:Guinea Pigs; D006801:Humans; D016234:Kallikrein-Kinin System / Q000502:physiology*; D019679:Kininogen, High-Molecular-Weight / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism*; D010949:Plasma; D041261:Vibrio vulnificus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D004792:Enzyme Precursors; D019679:Kininogen, High-Molecular-Weight; D008666:Metalloendopeptidases; D001920:Bradykinin
keywords: Coagulation; Contact system; Kallikrein/kinin; Vascular permeability; Vibrio vulnificus; vEP-45 protease