THE ROLE OF MATRIX METALLOPROTEINASES (MMPS) ENZYMES IN BONDING EFFECTIVENESS OF ADHESIVES

Demineralized dentin contains bound matrix metalloproteinases -2, -3, -8, -9, and -20 (mmps). these enzymes were activated by acids and can slowly degrade the collagen fibrils of hybrid layer. the contemporary dentin adhesives are very stable at the enamel surface, whereas lose their bond strength to dentin over time. this loss relates to the hydrolysis of collagen matrix of the hybrid layers. the preservation of the collagen matrix integrity is a key issue in the attempts to improve the dentin bonding durability. for this reason, mmps that breakdown collagen fibrils must be inactivated or inhibited. the aim of this review was to evaluate functions of the matrix metalloproteinases enzymes, common mmps inhibitors and current studies that evaluate of the inhibitory effect of these agents using this method.