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Söderling, E.; Syed, S.; Mäkinen, P.-L.; Mäkinen, K. K. (2011)
Publisher: Microbial Ecology in Health and Disease
Journal: Microbial Ecology in Health and Disease
Languages: English
Types: Article

Classified by OpenAIRE into

mesheuropmc: stomatognathic diseases, stomatognathic system
The proteolytic activities of whole cells and extracts of sonicated cells from Treponema denticola ATCC 35405, T. vincentii ATCC 35580, T. socranskii ATCC 35536 and seven clinical isolates of T. denticola were compared using early stationary phase cultures. Synthetic bacterial collagenase substrates (FALGPA: furylacryloyl-L-leucyl-glycyl-L-prolyl-D-arginine and PZ-PLGPA: phenylazobenzyloxycarbonyl-L-prolyl-L-leucyl-glycyl-L-prolyl-D-arginine) were hydrolysed by all Treponema extracts. Soluble type I collagen and reconstituted [3H]collagen were slowly hydrolysed by extracts from T. denticola and T. vincentii but not that from T. socranskii. The extracts of T. denticola ATCC 35405 and most clinical isolates of T. dentkola readily hydrolysed gelatin and collagen-derived polypeptides. Slow or no hydrolysis of these substrates was observed for T. vincentii and T. socranskii. Soluble type I collagen, gelatin and the collagen-derived peptides were hydrolysed by whole cells of T. denticola ATCC 35405 but not by those of T. vincentii and T. socranskii. The proteolytic activities of the Treponema-extxacts towards the synthetic collagenase substrates appeared not to be affected by the growth rate or the growth phase of the cells, but the aminopeptidase and iminopeptidase activities (substrates: N-aminoacyl-2-naphthylamines of arginine and proline) varied during growth. A labile, apparently membrane-associated, low-molecular weight FALGPA-hydrolysing protease was partially purified from T. denticola ATCC 35405. The enzyme degraded soluble type I collagen, synthetic collagen substrates, gelatin and collagen-derived polypeptides. The enzyme retained its activity in extracellular conditions and it was activated by a heat-denaturable factor (Mw >30 000) present in the rat inflammatory exudate. The pH optimum of the enzyme was at approximately pH 7.5. Thus, T. dentkola appeared to possess proteases which hydrolysed substrates representing both early and late stages of collagen breakdown and which may be active in conditions existing in the crevicular fluid.Keywords - Treponemes, Proteolytic enzymes, Subgingival plaque, Periodontal disease, Collagen.

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