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Cathepsin C, Matrix Metalloproteinases, and their Tissue Inhibitors in Gingiva and Gingival Crevicular Fluid from Periodontitis-affected Patients

¹ Unité INSERM U 424, 11 rue Humann, 67085 Strasbourg CEDEX, France; and
² Parogène, Strasbourg, France;

*corresponding author, h.tenenbaum{at}odonto3.u-strasbg.fr

Successive active phases observed in periodontal diseases may be explained either by a sudden activation of the pro-forms of tissue-stored degradative enzymes such as metalloproteinases (MMPs) or by an imbalance between metalloproteinases and their tissue inhibitors (TIMPs). To discriminate between these two hypotheses, we quantified the levels, the percentage of active form, and the activities of four metalloproteinases (MMPs -1, -2, -3, and -9), as well as the levels of two tissue inhibitors of metalloproteinases (TIMP-1 and -2) and the activity of cathepsin C in tissue extract supernatants and their corresponding gingival crevicular fluid samples collected from periodontitis-affected and healthy patients. Our results supported evidence that tissue destruction results from an imbalance of metalloproteinases over their tissue inhibitors rather than from a sudden activation of the pro-forms of these enzymes. A significant reduction in the activity of cathepsin C also contributed to the degradative process.

KEY WORDS: cathepsin C • matrix metalloproteinases • tissue inhibitors of metalloproteinases • periodontitis

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