RELATIONSHIP BETWEEN PERIODONTAL DISEASE AND Porphyromonas gingivalis PROTEASE
| Project/Area Number |
04454461
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Morphological basic dentistry
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| Research Institution | FUKUOKA DENTAL COLLEGE |
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Principal Investigator |
HAGIWARA Yoshisato FUKUOKA DENTAL COLLEGE, PROFESSOR, 歯学部, 教授 (00088931)
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| Co-Investigator(Kenkyū-buntansha) |
KAMINISHI Hedenori FUKUOKA DENTAL COLLEGE, ASSOCIATE PROFESSOR, 歯学部, 助教授 (90084300)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥6,100,000 (Direct Cost: ¥6,100,000)
Fiscal Year 1993: ¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1992: ¥3,800,000 (Direct Cost: ¥3,800,000)
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| Keywords | P.gingivalis / PROTEASE / PATHOGENESIS / KALLIKREIN / HAGEMAN FACTOR / BRADYKININ / INFLAMMATION / Kallikrein / Kinin |
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| Research Abstract |
Among a great number of microorganisms inhabiting subgingivally, Porphyromonas gingivalis is consider the most important pathogen in adult periodontal disease. It is well known that this organism pruduces a tripsin-like thiol-acti-vatable protease into the culture fluid, and delailed characteristics of the protease have been reported. Improtant virulence factors of the organism are considered to be its capacity of degradation of immunoglobulins, complement factors, cell matrix grycoproteins, collagen and protease inhibitors. This broad proteolytic activity may play an ingenious role ion invasion of the arganism into the host tissue and destruction of tissue as well as evasion from the host defense mechanisms. During our study on P.gingivalis, we found that its substrate specificity for synthetic substrate was indeed identical to that of plasma kallikrein and to that of activated Hageman factor. Kallikrein is also known to generate bradykinin directly from high molecular kininogen, and it is also kown to activate Hageman factor. In the present work we demonstrated that a protease produced by P.gingivalis caused vascular permeability enhancement when injected into guinea pig skin. The permeability-enhancing reactio caused by the protease was not affected by anti histaminic reagent, but was greatly augmented by simultaneous infection of a kinin potentiator, carboxypeptidase N inhibitor. However, the reaction was inhibited by soybean tripsin inhibitor or alpha_2antiplasmin. A bradykinin-degrading enzyme, carboxypeptidase B, weakend this vascular reaction. Results obtained from present study indicate that the permeabilty-en-hancing reaction induced by the protease is caused by the activation of the kallikrein-kinin cascade in the tissue. These results suggest that P.gingivalis protease plays an important role in the infection of this organism by activating inflammatory factors and tissue degeneration.
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Report
(3 results)
Research Products
(10 results)
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[Publications] Kaminishi, H., Cho, T., Sakima, T.Hagihara, Y., Iwata, A., Kasawaki, K., Itoh, T.and Fujii, T.: "Activation of plasma clotting factors by Candida albicans proteinase." J.J.Oral Biol.35. 221-226 (1993)
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Publications] Kaminishi, H., Cho, T., Itoh, T., Iwata, A., Kawasaki, K., Hagihara, Y.and Maeda, H.: "Vascular permeability enhancing activity of Porphyromonas gingivalis protease in guinea pigs." FEMS Microbiol. Letts.114. 109-114 (1993)
Description
「研究成果報告書概要(欧文)」より
Related Report
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