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Involvement of MT1‐MMP and TIMP‐2 in human periodontal disease
Authors:A Oyarzún  R Arancibia  R Hidalgo  C Peñafiel  M Cáceres  M‐J González  J Martínez  PC Smith
Institution:1. Faculty of Odontology, Universidad Finis Terrae;2. Laboratory of Periodontal Physiology, Dentistry Academic Unit, Faculty of Medicine, Pontificia Universidad Católica de Chile;3. Faculty of Odontology, Universidad de Chile;4. Cell Biology Program, Institute of Biomedical Sciences, Faculty of Medicine, Universidad de Chile;5. Laboratory of Cell Biology, Institute of Nutrition and Food Technology, Universidad de Chile, Santiago, Chile
Abstract:Oral Diseases (2010) 16 , 388–395 Objectives: Periodontal disease is characterized by an increased collagen metabolism. Although membrane type‐1 matrix metalloproteinase (MT1‐MMP) plays a critical role in collagen degradation, its involvement in human periodontitis remains to be determined. Methods: MT1‐MMP and TIMP‐2 expression and distribution were evaluated in gingival tissue samples derived from 10 healthy and 12 periodontitis‐affected human subjects. MT1‐MMP and TIMP‐2 expression were assessed through Western‐blot of tissue homogenates. The main cell types involved in MT1‐MMP and TIMP‐2 production were evaluated by means of immunohistochemistry. Results: Both MT1‐MMP and TIMP‐2 were significantly increased in periodontitis‐affected gingival tissues when compared to healthy gingiva. Moreover, the balance between MT1‐MMP and its inhibitor TIMP‐2 was altered in periodontitis‐affected tissues, suggesting an imbalance in this proteolytic axis. Immunohistochemistry demonstrated the expression of MT1‐MMP in fibroblasts and macrophages in gingival tissues. MT1‐MMP was detected in cells in close association with the gingival collagen matrix. TIMP‐2 expression was identified in fibroblasts, macrophages and epithelial cells. Conclusions: Our observations show an increased expression of MT1‐MMP and TIMP‐2 in periodontitis‐affected gingival tissues. The altered balance between these two molecular mediators of collagen remodeling suggests their involvement in human periodontal disease.
Keywords:MMP  MMP‐14  MT1‐MMP  TIMP‐2  periodontal disease
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