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Zinc reduces collagen degradation in demineralized human dentin explants
Authors:Osorio R  Yamauti M  Osorio E  Ruiz-Requena M E  Pashley D H  Tay F R  Toledano M
Affiliation:a Department of Dental Materials, School of Dentistry, Campus de Cartuja s/n, University of Granada, E-18071 Granada, Spain
b Department of Biochemistry and Molecular Biology, School of Medicine, Av. de Madrid s/n, University of Granada, E-18071 Granada, Spain
c Department of Oral Biology, School of Dentistry, Medical College of Georgia, 1120 15th Street, Augusta, GA, USA
d Department of Endodontics, School of Dentistry, Medical College of Georgia, 1120 15th Street, Augusta, GA, USA
Abstract:

Objectives

Dentin matrix metalloproteinases are implicated in the pathogenesis of caries and contribute to collagen degradation in resin-dentin interfaces. The objective was to determine if collagen degradation may be modulated by an excess of zinc or zinc chelators.

Methods

Mineralized and phosphoric acid demineralized human dentin specimens were tested. Chlorhexidine digluconate, doxycycline or ZnCl2 were added to the media. In half of the groups, active exogenous metalloproteinase-2 was incorporated into the solution. C-terminal telopeptide determinations (radioimmunoassay) were performed after 24 h, 1 and 3 weeks.

Results

Collagen degradation was prominent in demineralized dentin. Doxycycline fully blocked dentin proteolysis. Chlorhexidine digluconate reduced the degradation at the 24-h period. Zinc in excess strongly inhibits hydrolysis of collagen and its effect was maintained for 3 weeks.

Conclusions

Zinc in excess reduces MMP-mediated collagen degradation. The hypothesis that binding of zinc to collagen results in protection of sensitive cleavage sites of metalloproteinases requires further validation.
Keywords:Matrix metalloproteinase   Dentin   Zinc, Collagen   Degradation   Demineralization
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