| Research Abstract |
Destruction of periodontal tissues, including alveolar bone, is one of the most important pathological conditions of progressive periodontal disease. Although the actual mechanism of periodontal tissue breakdown during disease progression remains to be clarified, proteolytic enzymes derived from both host cells and oral microorganisms are thought to play a key role in pathogenicity of the disease. The present study was undertaken to establish new clinical paramethers for diagnosis of the disease and to develop new therapeutic and prevenmtive drugs. For this purpose, the present work was designed to identify periodontopathogenic proteinases and to clarify how they participate in the progression of the disease. Host-derived proteinases, including cysteine proteinases (cathepsin B,H,and L), serine proteinases (cathepsin G and medullasin) and aspartic proteinase (cathepsin D), were released into gingival crevices of periodontitis patients and their levels in gingival crevicular fluid (GCF) were positively correlated with the severity of the disease. A major cysteine proteinases produced by the major periodontopathogen Porphyromonas gingivalis, termed Arg-gingipain, was also concentrated in GCF of the patients. The enzyme was shown to be involved in the direct destruction of periodontal tissues and the disrukption of normal host defense mechanisms. The enzyme was also implicated in the hemagglutinating activity of the organism.
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