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Titolo:
Studies on the aminopeptidase activities of Porphyromonas gingivalis
Autore:
Grenier, D; Gauthier, P; Plamondon, P; Nakayama, K; Mayrand, D;
Indirizzi:
Univ Laval, Fac Med Dent, Grp Rech Ecol Buccale, Quebec City, PQ G1K 7P4, Canada Univ Laval Quebec City PQ Canada G1K 7P4 Quebec City, PQ G1K 7P4, Canada Univ Laval, Fac Sci & Genie, Quebec City, PQ G1K 7P4, Canada Univ Laval Quebec City PQ Canada G1K 7P4 Quebec City, PQ G1K 7P4, Canada Nagasaki Univ, Sch Dent, Dept Microbiol, Nagasaki 852, Japan Nagasaki Univ Nagasaki Japan 852 nt, Dept Microbiol, Nagasaki 852, Japan
Titolo Testata:
ORAL MICROBIOLOGY AND IMMUNOLOGY
fascicolo: 4, volume: 16, anno: 2001,
pagine: 212 - 217
SICI:
0902-0055(200108)16:4<212:SOTAAO>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT CATHEPSIN-H; ACTINOBACILLUS-ACTINOMYCETEMCOMITANS; ORAL BACTERIA; VIRULENCE; CONSTRUCTION; PROTEASES; GINGIPAIN; MUTANTS;
Keywords:
periodontal disease; Porphyromonas gingivalis; proteinase; aminopeptidase; inhibitors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Grenier, D Univ Laval, Fac Med Dent, Grp Rech Ecol Buccale, Cite Univ, Quebec City, PQ G1K 7P4, Canada Univ Laval Cite Univ Quebec City PQ Canada G1K7P4 7P4, Canada
Citazione:
D. Grenier et al., "Studies on the aminopeptidase activities of Porphyromonas gingivalis", ORAL MICROB, 16(4), 2001, pp. 212-217

Abstract

Porphyromonas gingivalis is an asaccharolytic bacterium that requires nitrogen substrates as carbon and energy sources. The aims of this study were to investigate the aminopeptidase activities of P. gingivalis and to evaluate the effect of aminopeptidase inhibitors on bacterial growth. Only arginine aminopeptidase and dipeptidyl aminopeptidase IV activities were detected. Experimental evidence was obtained suggesting that the Arg-gingipains of P. gingivalis can function as both an endopeptidase and an aminopeptidase. Firstly, the arginine aminopeptidase activity was found to be inhibited by leupeptin, a well-known inhibitor of Arg-gingipain activity. Secondly, a preparation of Arg-gingipain activity could hydrolyze the chromogenic substrate for arginine aminopeptidase. Lastly, a mutant of P. gingivalis constructed via gene disruption by use of suicide plasmids and deficient in both Arg-gingipain A and B was also devoid of arginine aminopeptidase activity. To investigate the key role of aminopeptidase activities in growth of P. gingivalis, aminopeptidase inhibitors were incorporated in the culture medium prior to inoculation. Bestatin and actinonin were the only ones to inhibit growth of P. gingivalis. Their mechanism of growth inhibition appears to be different but does not involve inhibition of the two major aminopeptidase activities (arginine aminopeptidase and dipeptidyl aminopeptidase IV).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 06:54:04