Dentin collagen and collagenolytic enzymes (Matrix Metalloproteinases and Cysteine Cathepsins)

Dentin collagen, primarily Type I collagen, constitutes approximately 90% of the organic matrix of dentin and provides the structural framework for tooth mineralization (Mazzoni et al., 2015). Sequestrated within this mineralized matrix are endogenous collagenolytic enzymes, including matrix metalloproteinases (MMPs-2, -8, -9, and -20) and cysteine cathepsins (Cathepsins B and K) (Tjäderhane et al., 1998; Tersariol et al., 2010). These enzymes are typically inactive but can be activated by the acidic environment produced by cariogenic bacteria or by the acid-etching procedures used in adhesive dentistry (Pashley et al., 2004). Once activated, these proteases degrade the collagen fibrils, which is a primary cause of the degradation of the resin-dentin hybrid layer and the progression of dental caries (Carrilho et al., 2007). Therapeutic interventions aim to preserve the integrity of the dentin matrix by using protease inhibitors like chlorhexidine or collagen cross-linkers like carbodiimides (Mazzoni et al., 2014). These strategies are crucial for improving the clinical longevity of dental restorations and managing deep carious lesions.

Other names

Dentin organic matrixDentin MMPsDentin cathepsinsType I collagen in dentinDentin matrix proteases

Inhibition of endogenous matrix metalloproteinases (MMPs) and cysteine cathepsins through competitive or non-competitive binding, and stabilization of the dentin collagen matrix via chemical cross-linking to prevent proteolytic degradation.