Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria.
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 alpha-thrombin. ASP is the first bacterial serine protease that produces alpha-thrombin, through which ASP may contribute to the induction of thrombotic tendency in disseminated intravascular coagulation complicated with sepsis caused by A. sobria infections.
Nitta
Hidetoshi
H
Department of Molecular Pathology, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto 860-8556, Japan.
Kobayashi
Hidetomo
H
Irie
Atsushi
A
Baba
Hideo
H
Okamoto
Keinosuke
K
Imamura
Takahisa
T
D000333:Aeromonas / Q000187:drug effects / Q000201:enzymology*; D000595:Amino Acid Sequence; D001777:Blood Coagulation / Q000187:drug effects; D001779:Blood Coagulation Factors / Q000737:chemistry / Q000378:metabolism; D004792:Enzyme Precursors / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011516:Prothrombin / Q000737:chemistry / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000494:pharmacology*; D013379:Substrate Specificity / Q000187:drug effects
D001779:Blood Coagulation Factors; D004792:Enzyme Precursors; D010455:Peptides; D011516:Prothrombin; D012697:Serine Endopeptidases