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Titolo:
Activation of protein C by arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis
Autore:
Hosotaki, K; Imamura, T; Potempa, J; Kitamura, N; Travis, J;
Indirizzi:
KumamotoumamotoGrad Sch Med Sci, Dept Neurosci & Immunol, Div Mol Pathol, K Kumamoto Univ Kumamoto Japan 8600811 urosci & Immunol, Div Mol Pathol, K Kumamoto Univ, Sch Med, Dept Surg 1, Kumamoto 8600811, Japan Kumamoto Univ Kumamoto Japan 8600811 ept Surg 1, Kumamoto 8600811, Japan Jagiellonian,Univ, Inst Mol Biol, Dept Microbiol & Immunol, PL-31120 Krakow Jagiellonian Univ Krakow Poland PL-31120 biol & Immunol, PL-31120 Krakow Univ Georgia, Dept Biochem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 rgia, Dept Biochem, Athens, GA 30602 USA
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 1, volume: 380, anno: 1999,
pagine: 75 - 80
SICI:
1431-6730(199901)380:1<75:AOPCBA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
DISSEMINATED INTRAVASCULAR COAGULATION; HUMAN FACTOR-VIII; BLOOD-COAGULATION; FACTOR-V; TISSUE FACTOR; THROMBOMODULIN; INACTIVATION; THROMBIN; PATHWAY; PERIODONTITIS;
Keywords:
bacteria; disseminated intravascular coagulation periodontitis; phospholipid; sepsis; zymogen activation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Imamura, T KumamotoumamotoGrad Sch Med Sci, Dept Neurosci & Immunol, Div Mol Pathol, K Kumamoto Univ Kumamoto Japan 8600811 munol, Div Mol Pathol, K
Citazione:
K. Hosotaki et al., "Activation of protein C by arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis", BIOL CHEM, 380(1), 1999, pp. 75-80

Abstract

In order to determine the effect of bacterial proteinases on activation ofthe protein C system, a negative regulator of blood coagulation, two arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis, a causative bacterium of adult periodontitis, were examined. Each enzyme activated human protein C in a dose- and incubation time-dependent manner. Interestingly, the form of enzyme being composed of a non-covalent complex containing both catalytic and adhesion domains (RgpA) produced activatedprotein C 14-fold more efficiently than RgpB which contained the catalyticdomain alone. The k(cat)/K-m value of RgpA was 18-fold higher than that ofRgpB and comparable to that of the thrombin-thrombomodulin complex, the physiological activator of protein C. RgpA catalyzed protein C activation wasaugmented 1.4-fold by phospholipids, ubiquitous cell membrane components. Furthermore, RgpA, but not RgpB, could activate protein C in plasma and this resulted in a decrease of the protein C concentration in plasma, which isoften observed in patients with sepsis during the development of disseminated intravascular coagulation (DIC). These data indicate that RgpA is a more potent activator of protein C than RgpB and suggest that only the former enzyme can cause protein C activation in vivo. The present study further suggests that bacterial proteinases may possibly contribute to the consumption of plasma protein C which predisposes to DIC and/or promotes a thrombotictendency towards DIC in sepsis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 16:15:25