PGE_2 production in macrophages and bone resorption by etiologic agents of human periodontal diseases
| Project/Area Number |
08457496
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
病態科学系歯学(含放射線系歯学)
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| Research Institution | HOKKIDO UNIVERSITY |
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Principal Investigator |
SAKAMOTO Wataru Hokkaido University, School of Dentistry, Associate Professor, 歯学部, 助教授 (30001952)
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| Co-Investigator(Kenkyū-buntansha) |
AMEMIYA Akira Hokkaido University, School of Dentistry Professor, 歯学部, 名誉教授 (80018415)
NISHIKATA Makoto Hokkaido University, School of Dentistry, Instructor, 歯学部, 教務職員 (00150243)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥5,800,000 (Direct Cost: ¥5,800,000)
Fiscal Year 1997: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1996: ¥4,200,000 (Direct Cost: ¥4,200,000)
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| Keywords | Porphyromonas ginigivalis / Periodontal disease / Macrophage / PGE_2 / IL-1beta / TNF- alpha / LPS / 45 kDa protease / 歯周囲病原性因子 / マクロファージ / モノカイン / 44kDaタンパク質 / COX-2 / tyrosine kinase |
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| Research Abstract |
Porphyromonas gingivalis, a gram-negative anaerobe implicated in the etiology and pathogenesis of human periodontal diseases, produces a variety of potent proteolytic enzymes. In order to clarify the pathogenic roles for proteases from Porphyromonas gingivalis, 45 kDa protease was isolated from Porphyromonas gingivalis culture medium by a combination of gelfiltrations (Bio-Gel A) and ion-exchange chromatographies (DEAE-Spephacel). The enzyme was found to have a molecular mass 45 kDa by SDS-PAGE and to require mercaptoethanol for its activation. The 45 kDa protease cleaved T-kininogen into small fragments, but failed to release Kinin. The protein (2.5mug/ml) showed no stimulation activity on the productions of PGE<@D22@>D2, IL-1beta, and TNF-alphafrom the macrophages, whereas LPS (2.5mug/ml) makedly induced the productions of them from the macrophages (134.4(]SY.+-。[)51.0 PGE<@D22@>D2ng/ 10<@D16@>D1 cells ; 917 (]SY.+-。[)103IL-1beta pg/ 10<@D16@>D1 cells ; 560 (]SY.+-。[)74TNF-alpha pg/ 10<@D16@>D1 cells). These results suggest that 45KDa protease neither releases Kinin from the Kininogen nor stimulates PGE<@D22@>D2 and monokimes, implicated in the bone resorption.
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Report
(3 results)
Research Products
(15 results)
