In situ detection of matrix metalloproteinase-9 (MMP-9) in gingival epithelium in human periodontal disease
Version of Record online: 18 FEB 2004
Journal of Periodontal Research
Volume 39, Issue 2, pages 87–92, April 2004
How to Cite
Smith, P. C., Muñoz, V. C., Collados, L. and Oyarzún, A. D. (2004), In situ detection of matrix metalloproteinase-9 (MMP-9) in gingival epithelium in human periodontal disease. Journal of Periodontal Research, 39: 87–92. doi: 10.1111/j.1600-0765.2004.00705.x
- Issue online: 18 FEB 2004
- Version of Record online: 18 FEB 2004
- Accepted for publication July 30, 2003
- gelatin zymography;
- gingival epithelium;
- matrix metalloproteinases;
- periodontal disease
Background and objective: As the periodontal lesion develops, the junctional epithelium migrates apically in conjunction with the dissolution of the most coronal Sharpey's fibers. Because matrix metalloproteinase-9 (MMP-9) has been identified in migrating epithelial cells and invading tumors, we propose that this enzyme is produced by gingival keratinocytes in advanced periodontal lesions.
Methods: To test this idea, biopsies of inflamed gingival tissues were obtained from patients with advanced periodontitis. Healthy gingival tissue samples were utilized as controls. The presence and activity of MMP-9 was evaluated by combining indirect immunofluorescence of gingival tissue samples and gelatin zymography of gingival epithelium separated from connective tissue.
Results and conclusions: The staining pattern showed the presence of MMP-9 in junctional and pocket gingival epithelial cells, polymorphonuclear neutrophils (PMNs) and as a scattered deposit along connective tissues of periodontitis-affected gingival tissues. Gelatin zymography permitted the identification of pro-MMP-9 in surcular/pocket epithelium derived from inflamed gingival tissues. Lower levels of MMP-9 were detected in epithelium not exposed to inflammation. These observations suggest a role for MMP-9 in gingival epithelial response to periodontal infection.