{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T22:44:17Z","timestamp":1790117057725,"version":"4.0.1"},"reference-count":57,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,11,23]],"date-time":"2005-11-23T00:00:00Z","timestamp":1132704000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Oral Diseases"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:p><jats:bold>Objective:\u2002<\/jats:bold> Several collagenolytic matrix metalloproteinases (MMPs) have recently been identified in gingival fibroblasts, while secreted cysteine proteinases could also participate in connective tissue destruction in periodontitis. To clarify their involvement, we examined enzyme release during collagen breakdown by cultured cytokine\u2010stimulated fibroblasts.<\/jats:p><jats:p><jats:bold>Materials and methods:\u2002<\/jats:bold> Gingival fibroblasts were derived from four chronic periodontitis patients and cultured on collagen gels in serum\u2010free medium for 1\u20134\u2003days. Collagenolysis was measured by hydroxyproline release into the medium. Proteinases were assessed by electrophoresis and immunoblotting.<\/jats:p><jats:p><jats:bold>Results:\u2002<\/jats:bold> Adding interleukin\u20101<jats:italic>\u03b2<\/jats:italic> resulted in progressive gel breakdown. This was associated particularly with a shift in MMP\u20101 band position from proenzyme to active enzyme and the appearance of active as well as proenzyme forms of cathepsin B. There was also partial processing of pro\u2010MMP\u201013 and increased immunoreactivity for active cathepsin L. In addition, both pro\u2010forms and active forms of MMP\u20108, membrane\u2010type\u20101\u2010MMP and MMP\u20102 were present in control and treated cultures.<\/jats:p><jats:p><jats:bold>Conclusions:\u2002<\/jats:bold> Fibroblast MMP\u20101 was most likely responsible for collagen dissolution in the culture model, while cathepsin B may have been part of an activation pathway. All studied proteinases contribute to extracellular matrix destruction in inflamed gingival tissue, where they probably activate each other in proteolytic cascades.<\/jats:p>","DOI":"10.1111\/j.1601-0825.2005.01153.x","type":"journal-article","created":{"date-parts":[[2005,11,23]],"date-time":"2005-11-23T15:40:41Z","timestamp":1132760441000},"page":"34-40","source":"Crossref","is-referenced-by-count":64,"title":["Collagen degradation by interleukin\u20101<i>\u03b2<\/i>\u2010stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine 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