Pleiotropic effects of a vibrio extracellular protease on the activation of contact system

Jung Eun Park, Jong Woo Park, Weon Tae Lee, Jung Sup Lee

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)1099-1103
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume450
Issue number2
DOIs
Publication statusPublished - 2014 Jul 25

Fingerprint

Kallikreins
Vibrio
Kallikrein-Kinin System
Kinins
Enzyme Precursors
Peptide Hydrolases
Chemical activation
Prothrombin
Coagulation
Plasmas
High Molecular Weight Kininogens
Prekallikrein
Vibrio vulnificus
Blood Coagulation Factors
Capillary Permeability
Metalloproteases
Bradykinin
Hemostatics
Fibrin
Thrombin

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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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.",
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Pleiotropic effects of a vibrio extracellular protease on the activation of contact system. / Park, Jung Eun; Park, Jong Woo; Lee, Weon Tae; Lee, Jung Sup.

In: Biochemical and Biophysical Research Communications, Vol. 450, No. 2, 25.07.2014, p. 1099-1103.

Research output: Contribution to journalArticle

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