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

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

doi:10.1016/j.febslet.2007.11.076

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 journal › Article › peer-review

20 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 language	English
Pages (from-to)	5935-5939
Number of pages	5
Journal	FEBS Letters
Volume	581
Issue number	30
DOIs	https://doi.org/10.1016/j.febslet.2007.11.076
Publication status	Published - Dec 22 2007
Externally published	Yes

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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10.1016/j.febslet.2007.11.076

Cite this

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

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.",

keywords = "Aeromonas sobria, Bacteria, Coagulation, DIC, Protease, Prothrombin",

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T1 - Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria

AU - Nitta, Hidetoshi

AU - Kobayashi, Hidetomo

AU - Irie, Atsushi

AU - Baba, Hideo

AU - Okamoto, Keinosuke

AU - Imamura, Takahisa

PY - 2007/12/22

Y1 - 2007/12/22

N2 - 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.

AB - 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.

KW - Aeromonas sobria

KW - Bacteria

KW - Coagulation

KW - DIC

KW - Protease

KW - Prothrombin

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JO - FEBS Letters

JF - FEBS Letters

IS - 30

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

Abstract

Keywords

ASJC Scopus subject areas

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