The role of host-derived dentinal matrix metalloproteinases in reducing dentin bonding of resin adhesives.
- Author:
Shan-chuan ZHANG
1
;
Matthias KERN
Author Information
- Publication Type:Journal Article
- MeSH: Chlorhexidine; pharmacology; Collagen; metabolism; ultrastructure; Dental Bonding; Dentin; enzymology; ultrastructure; Dentin-Bonding Agents; chemistry; Enzyme Inhibitors; pharmacology; Humans; Hydrolysis; Matrix Metalloproteinase Inhibitors; Matrix Metalloproteinases; metabolism; Resin Cements; chemistry
- From: International Journal of Oral Science 2009;1(4):163-176
- CountryChina
- Language:English
- Abstract: Dentin matrix metalloproteinases (MMPs) are a family of host-derived proteolytic enzymes trapped within mineralized dentin matrix, which have the ability to hydrolyze the organic matrix of demineralized dentin. After bonding with resins to dentin there are usually some exposed collagen fibrils at the bottom of the hybrid layer owing to imperfect resin impregnation of the demineralized dentin matrix. Exposed collagen fibrils might be affected by MMPs inducing hydrolytic degradation, which might result in reduced bond strength. Most MMPs are synthesized and released from odontoblasts in the form of proenzymes, requiring activation to degrade extracellular matrix components. Unfortunately, they can be activated by modem self-etch and etch-and-rinse adhesives. The aim of this review is to summarize the current knowledge of the role of dentinal host-derived MMPs in dentin matrix degradation. We also discuss various available MMP inhibitors, especially chlorhexidine, and suggest that they could provide a potential pathway for inhibiting collagen degradation in bonding interfaces thereby increasing dentin bonding durability.
