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Activation mechanism of human Hageman factor‐plasma kallikreinkinin system by Vibrio vulnificus metalloprotease
Author(s) -
Miyoshi Shin-ichi,
Shinoda Sumio
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81301-2
Subject(s) - prekallikrein , kallikrein , kininogen , bradykinin , chemistry , high molecular weight kininogen , factor xii , metalloproteinase , biochemistry , alpha 2 macroglobulin , human plasma , macroglobulin , enzyme , microbiology and biotechnology , biology , medicine , receptor , coagulation , chromatography
Vibro vulnificus , an opportunistic human pathogen, secretes a metalloprotease (VVP). The VVP inoculated into a guinea pig is known to generate bradykinin through activation of the Hageman factor‐plasma kallikrein‐kinin system. VVP was shown to poisess the ability to activate the human system through the same mechanism as that clarified in the guinea pig system, namely, VVP converted both human zymogens (Hageman factor and plasma prekallikrein) to active enzymes (activated Hageman factor and plasma kallikrein), and the then generated kallikrein liberated bradykinin from high molecular‐weight kininogen. However, in the presence of plasma α 2 ‐macroglobulin (α 2 M), the VVP action was drastically decreased. This finding suggests that the human system might be activated only at the interstitial‐tissue space which contains negligible amounts of α 2 M or in the bloodstream of the individuals whom plasma α 2 M level is extremely reduced.