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In addition, human recombinant proMMP\u20108 was in vitro activated by <jats:italic>Treponema denticola<\/jats:italic> chymotrypsin\u2010like protease (Td\u2010CTLP), sodium hypochlorite (NaOCl, 1\u00a0mM, oxidant) or amino phenyl mercuric acetate (APMA, 1\u00a0mM).<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>In saliva of periodontitis\u2010affected individuals, MMP\u20108 is found in multiple forms, that is, complexes, active and pro\u2010forms of neutrophilic and mesenchymal\u2010type MMP\u20108, and especially 20\u201327\u00a0kDa fragments. The quantity of these fragments was elevated in both localized and generalized forms of periodontitis. Moreover, the tested activators (Td\u2010CTLP, NaOCl and APMA) activated inactive proMMP\u20108, resulting in fragments of 20\u201327\u00a0kDa, in vitro, and salivary concentrations of <jats:italic>T.\u00a0denticola<\/jats:italic> correlated significantly with salivary levels of fragmented MMP\u20108.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>The present results indicate that during the development and progression of periodontitis, MMP\u20108 appears as activated and fragmented, and treponemal proteases most likely play role in this cascade.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jcpe.13024","type":"journal-article","created":{"date-parts":[[2018,10,20]],"date-time":"2018-10-20T13:15:02Z","timestamp":1540041302000},"page":"1421-1428","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Molecular forms and fragments of salivary MMP\u20108 in relation to 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