Turnover of ECM components is regulated by Matrix Metalloproteinase (MMP) and Tissue Inhibitors of Matrix metalloproteinase (TIMP) activity. During dental injury, acidic / proteolytic agents may lead to disturbances of MMPs and affect regulation of tissue homeostasis. This may directly or indirectly, through the activity of MMPs affect the regulation of odontoblast secretory activity. Objective: This study investigated the immunohistochemical expression of MMPs and TIMPs in tissues of healthy and carious human molar teeth. Methods: Teeth were fixed and processed immediately following extraction. 5 micron wax embedded sections of demineralised teeth were stained with rabbit polyclonal antibodies to MMP-1, –2, –3, –9 and TIMP-1, prior to detection using the StrAviGen method with DAB as the chromophore. Specificity controls included staining following omission of the primary antibody and staining using non-immune rabbit IgG. Results: The presence of MMP-1, -2, -3 and –9 plus TIMP-1 were detected within the odontoblasts, cells of the subodontoblast layer and pulpal fibroblasts, however they were not detected within the predentine or dentine matrix. Staining in tissues from carious teeth showed a similar pattern of expression for all enzymes, however, staining for TIMP-1 was less intense in these carious tissues. Conclusions: These results indicate that a variety of MMP and TIMP species are expressed in the dentine-pulp complex of human molar teeth, and their regulation may be important during tissue repair processes following injury such as caries.

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