4.7 Article

Inhibition of Enzymatic Degradation of Adhesive-Dentin Interfaces

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

  1. FWO [1.5.198.07, G.0206.07]
  2. KU Leuven [OT/06/55, GOA2007-2011]

向作者/读者索取更多资源

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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