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- Title
Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria
- Authors
Nitta, Hidetoshi; Kobayashi, Hidetomo; Irie, Atsushi; Baba, Hideo; Okamoto, Keinosuke; Imamura, Takahisa
- Abstract
Abstract: 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.
- Subjects
SERINE proteinases; PROTHROMBIN; AEROMONAS; BLOOD coagulation factors
- Publication
FEBS Letters, 2007, Vol 581, Issue 30, p5935
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.11.076