期刊
JOURNAL OF DENTAL RESEARCH
卷 88, 期 12, 页码 1101-1106出版社
SAGE PUBLICATIONS INC
DOI: 10.1177/0022034509346952
关键词
matrix metalloproteinases; SDS-PAGE; dental adhesive
资金
- FWO [1.5.198.07, G.0206.07]
- KU Leuven [OT/06/55, GOA2007-2011]
Adhesive procedures activate dentin-associated matrix metalloproteinases (MMPs), and so iatrogenically initiate bond degradation. We hypothesized that adding MMP inhibitors to adhesive primers may prevent this endogenous enzymatic degradation, thereby improving bond durability. A nonspecific MMP inhibitor (chlorhexidine) and a MMP-2/9-specific inhibitor (SB-3CT) were admixed to the primers of an etch & rinse and a self-etch adhesive, both considered as gold-standard adhesives within their respective categories. For dentin powder exposed to the adhesives under clinical application conditions, gelatin zymography revealed the release of MMP-2 (not of MMP-9) by the etch & rinse adhesive, while no release of enzymes could be detected for the mild self-etch adhesive, most likely because of its limited dentin demineralization effect. The built-in MMP inhibitors appeared effective in reducing bond degradation only for the etch & rinse adhesive, and not for the self-etch adhesive. Water sorption of adhesive interfaces most likely remains the principal mechanism of bond degradation, while endogenous enzymes appear to contribute to bond degradation of only etch & rinse adhesives.
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