Effect of Chlorhexidine and Cystatin Incorporated Adhesives on MMPs and Cysteine Cathepsin-An In-vitro Zymographic Analysis

Abstract

Introduction: Host-derived proteases such as Matrix Metallo Proteinases (MMPs) and Cysteine Cathepsin have been reported to degrade the collagen matrix of incompletely-resin infiltrated dentin. In an effort to improve the bond durability, specific and non-specific proteolytic inhibitors have been identified. Aim: The aim of this study was to comparatively evaluate the presence of MMPs and Cysteine Cathepsin in dentin after the incorporation of non-specific inhibitor 0.2% chlorhexidine and specific inhibitor cystatin to total etch and self-etch adhesives using zymographic analysis. Materials and Methods: Quantitative analysis of 135 coronal dentin specimens of human mandibular molars, which were randomly divided into three groups, based on the adhesive systems with and without the inhibitors was done. These were further subjected to zymographic analysis at various time periods at CLRI Institute, Chennai, following this the results were subjected to descriptive analysis. Results: The results obtained were calculated and expressed in terms of frequency. Results revealed that with combined use of both 0.2% chlorhexidine and cystatin, the gelatinolytic activity was completely absent at all time intervals. Conclusion: The incorporation of both 0.2% chlorhexidine and cystatin in adhesives inhibited MMPs and Cysteine Cathepsin activity completely, thereby prolonging the durability of resin dentin bond over a period of time.

Keywords

• collagen degradation
• proteases
• proteolytic inhibitors
• self-etch adhesives
• total etch adhesives