PGE_2 production in macrophages and bone resorption by etiologic agents of human periodontal diseases

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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.