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Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria
Author(s) -
Nitta Hidetoshi,
Kobayashi Hidetomo,
Irie Atsushi,
Baba Hideo,
Okamoto Keinosuke,
Imamura Takahisa
Publication year - 2007
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/j.febslet.2007.11.076
Subject(s) - serine protease , thrombin , coagulation , chemistry , protease , serine , disseminated intravascular coagulation , biochemistry , enzyme , aeromonas , microbiology and biotechnology , biology , bacteria , immunology , platelet , medicine , genetics
The effect of a serine protease (ASP) secreted from Aeromonas sobria on plasma coagulation was investigated. Proteolytically active ASP promoted human plasma coagulation in a dose‐dependent manner. Consistent with the preference for a factor Xa‐specific oligo‐peptide substrate, ASP produced enzymatic activity from human prothrombin but not from factors IX and X. ASP cleaved prothrombin to produce enzymatically active 37 kDa‐fragment displaying the same molecular mass as α‐thrombin. ASP is the first bacterial serine protease that produces α‐thrombin, through which ASP may contribute to the induction of thrombotic tendency in disseminated intravascular coagulation complicated with sepsis caused by A. sobria infections.