Effect of dentin etching and chlorhexidine application on metalloproteinase-mediated collagen degradation

Dentin matrix metalloproteinases (MMPs) are involved in the degradation of collagen in resin-dentin interfaces. This study evaluated whether collagen degradation can be prevented by chlorhexidine digluconate (CHX) after different dentin demineralization procedures. The demineralization of human dentin was performed with phosphoric acid (PA), EDTA or acidic monomers (Clearfil SE Bond and Xeno V). Specimens were stored (for 24h, or for 1 or 3wk) in the presence or absence of CHX. In half of the groups, active MMP-2 was incorporated into the storage solution. At the end of each storage period, the C-terminal telopeptide (ICTP) concentration (which indicates the amount of collagen degradation) was measured in the storage solution. Collagen degradation was higher in PA- and EDTA-demineralized dentin. Chlorhexidine digluconate reduced collagen degradation in these groups only for 24h. When dentin was demineralized with Clearfil SE Bond or Xeno V, collagen degradation was reduced by up to 30%, but the addition of exogenous MMP-2 significantly increased collagen degradation. In self-etchant-treated dentin, the inhibitory effect of CHX on MMPs lasted for up to 3wk. Treating dentin with EDTA, PA or self-etching agents produces enough demineralization to permit cleavage of the exposed collagen. Monomer infiltration may exert protection on demineralized collagen, probably through immobilization of MMPs. The partial inhibitory action of CHX on MMP activity produced by self-etching adhesives was prolonged compared with the short-acting PA- or EDTA-treated dentin.