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Titolo:
ACTIVATION OF BLOOD-COAGULATION FACTOR-X BY ARGININE-SPECIFIC CYSTEINE PROTEINASES (GINGIPAIN-RS) FROM PORPHYROMONAS-GINGIVALIS
Autore:
IMAMURA T; POTEMPA J; TANASE S; TRAVIS J;
Indirizzi:
UNIV GEORGIA,DEPT BIOCHEM ATHENS GA 30602 UNIV GEORGIA,DEPT BIOCHEM ATHENS GA 30602 KUMAMOTO UNIV,GRAD SCH MED SCI,DEPT NEUROSCI & IMMUNOL,DIV MOL PATHOLKUMAMOTO 860 JAPAN JAGIELLONIAN UNIV,INST MOL BIOL,DEPT IMMUNOL & MICROBIOL PL-31120 KRAKOW POLAND
Titolo Testata:
The Journal of biological chemistry
fascicolo: 25, volume: 272, anno: 1997,
pagine: 16062 - 16067
SICI:
0021-9258(1997)272:25<16062:AOBFBA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CREVICULAR FLUID; TISSUE-FACTOR; BACTEROIDES-GINGIVALIS; PERIODONTAL-DISEASE; VIPER VENOM; EXOENZYME-S; THROMBIN; PATHOGENESIS; ENZYME; INTERLEUKIN-1-BETA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
T. Imamura et al., "ACTIVATION OF BLOOD-COAGULATION FACTOR-X BY ARGININE-SPECIFIC CYSTEINE PROTEINASES (GINGIPAIN-RS) FROM PORPHYROMONAS-GINGIVALIS", The Journal of biological chemistry, 272(25), 1997, pp. 16062-16067

Abstract

The effect of two arginine-specific cysteine proteinases (gingipain Rs) from Porphyromonas gingivalis, a causative bacterium of adult periodontitis, on human blood coagulation was investigated, Activated partial thromboplastin time and prothrombin time were shortened by these proteinases, with a 95-kDa gingipain R containing adhesin domains being B-fold more efficient in comparison to a 50-kDa gingipain R containingthe catalytic domain alone, The 50-kDa enzyme reduced each coagulation time in several plasmas deficient in various coagulation factors, while it was ineffective in factor X-deficient plasma unless reconstituted with this protein. Each proteinase activated factor X in a dose- and time-dependent manner, with Michaelis constants (K-m) being found tobe lower than the normal plasma factor X concentration, strongly suggesting that factor X activation by gingipain Rs, especially the 95-kDaform which is strongly activated by phospholipids, could occur in plasma. This is the first report of factor X activation by bacterial proteinases and indicates that the gingipain Rs could be responsible for the production of thrombin and, indirectly, with the generation of prostaglandins, interleukin-1, etc., which have been found to be associated with the development of periodontitis induced by P. gingivalis infections. Furthermore, the data support the hypothesis that induction of blood coagulation by bacterial proteinases may be a causative agent inthe pathogenesis of disseminated intravascular coagulation 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 17:21:39