Dentin proteolytic enzymes

Dentin proteolytic enzymes are a group of host-derived enzymes, primarily matrix metalloproteinases (MMPs) and cysteine cathepsins, that are sequestered within the mineralized dentin matrix during tooth formation (Tjäderhane et al., 2015, https://doi.org/10.1177/0022034515582224). The most prominent members of this group include matrix metalloproteinases such as MMP-2, MMP-8, and MMP-9, as well as various cysteine cathepsins like cathepsin B and K (Tersariol et al., 2010, https://doi.org/10.1177/0022034510363380). These enzymes remain inactive until they are exposed and activated by acidic challenges, such as those from cariogenic bacteria or the acid-etching step in dental bonding procedures (Mazzoni et al., 2015, https://doi.org/10.1016/j.jdent.2014.08.015). Once active, they catalyze the degradation of type I collagen, which constitutes the bulk of the dentin organic matrix. This degradation is a major factor in the progression of dental caries and the long-term failure of resin-dentin bonds, as the enzymes break down the hybrid layer formed during restoration (Carrilho et al., 2007, https://doi.org/10.1177/154405910708600115). Therapeutic interventions often involve the use of protease inhibitors like chlorhexidine or cross-linking agents to preserve the structural integrity of the dentin and improve the longevity of dental restorations (Scaffa et al., 2012, https://doi.org/10.1177/0022034512445202).

Other names

Endogenous dentin proteasesDentin-bound matrix metalloproteinasesDentin-bound cathepsinsHost-derived dentin proteases

Inhibition of proteolytic activity through competitive binding, chelation of essential metal ions such as zinc and calcium, or collagen cross-linking to prevent enzymatic access to cleavage sites.