Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria

Hidetoshi Nitta, Hidetomo Kobayashi, Atsushi Irie, Hideo Baba, Keinosuke Okamoto, Takahisa Imamura

Research output: Contribution to journalArticle

18 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)5935-5939
Number of pages5
JournalFEBS Letters
Volume581
Issue number30
DOIs
Publication statusPublished - Dec 22 2007

Keywords

  • Aeromonas sobria
  • Bacteria
  • Coagulation
  • DIC
  • Protease
  • Prothrombin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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