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Titolo:
Inhibition of trypsin-like cysteine proteinases (gingipains) from Porphyromonas gingivalis by tetracycline and its analogues
Autore:
Imamura, T; Matsushita, K; Travis, J; Potempa, J;
Indirizzi:
Kumamoto Univ, Grad Sch Med Sci, Dept Neurosci & Immunol, Div Mol Pathol, Kumamoto 8600811, Japan Kumamoto Univ Kumamoto Japan 8600811 Mol Pathol, Kumamoto 8600811, Japan Jagiellonian Univ, Inst Mol Biol, Dept Microbiol & Immunol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 mmunol, PL-31120 Krakow, Poland Univ Georgia, Dept Biochem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 rgia, Dept Biochem, Athens, GA 30602 USA Kagoshima Univ, Sch Dent, Dept Operat Dent & Endodontol, Kagoshima 8908544, Japan Kagoshima Univ Kagoshima Japan 8908544 odontol, Kagoshima 8908544, Japan
Titolo Testata:
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
fascicolo: 10, volume: 45, anno: 2001,
pagine: 2871 - 2876
SICI:
0066-4804(200110)45:10<2871:IOTCP(>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATRIX METALLOPROTEINASES; PERIODONTAL-DISEASES; BLOOD-COAGULATION; MOUSE MODEL; THROMBIN; ACTIVATION; PROTEASES; PERMEABILITY; COLLAGENASES; NEUTROPHIL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Imamura, T Kumamoto Univ, Grad Sch Med Sci, Dept Neurosci & Immunol, Div Mol Pathol, 2-2-1 Honjo, Kumamoto 8600811, Japan Kumamoto Univ 2-2-1 Honjo Kumamoto Japan 8600811 600811, Japan
Citazione:
T. Imamura et al., "Inhibition of trypsin-like cysteine proteinases (gingipains) from Porphyromonas gingivalis by tetracycline and its analogues", ANTIM AG CH, 45(10), 2001, pp. 2871-2876

Abstract

Extracellular cysteine proteinases, referred to as gingipains, are considered important virulence factors for Porphyromonas gingivalis, a bacterium recognized as a major etiologic agent of chronic periodontitis. We investigated the effect of tetracycline and its analogues, doxycycline and minocycline, on the enzymatic activities of gingipains. Tetracyclines at 100 muM totally inhibited the amidolytic activity of arginine-specific gingipains (HRgpA and RgpB). In contrast, inhibition of Kgp was less efficient and required a somewhat higher concentration of the antibiotic to achieve the same effect. Among tetracycline derivatives, the most potent gingipain inhibitor was doxycycline, followed by tetracycline and minocycline. RgpB was inhibitedby doxycycline in an uncompetitive and reversible manner with a 50% inhibitory concentration of 3 muM. Significantly, inhibition was unaffected by calcium, excluding the chelating activity of tetracyclines as the mechanism of gingipain inactivation. In contrast, the inhibitory activities of the tetracyclines were reduced by cysteine, a reducing agent, suggesting an interference of the drug at the oxidative region with the catalytic system of theenzyme. Doxycycline, at 10 muM, significantly inhibited the RgpB-mediated production of vascular permeability-enhancing activity from human plasma, thus proving an effective inhibition of gingipain in vivo. These results indicate a new activity of tetracyclines as cysteine proteinase inhibitors andmay explain the therapeutic efficiency of these antibiotics in the treatment of periodontitis.

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Documento generato il 18/09/20 alle ore 17:01:34