Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?

• Published in: Dental materials Vol. 31; no. 2; pp. e25 - e32
• Main Authors: Tezvergil-Mutluay, Arzu, Agee, Kelli A, Mazzoni, Annalisa, Carvalho, Ricardo M, Carrilho, Marcela, Tersariol, Ivarne L, Nascimento, Fabio D, Imazato, Satoshi, Tjäderhane, Leo, Breschi, Lorenzo, Tay, Franklin R, Pashley, David H
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.02.2015
• Subjects: Advanced Basic Science; Ammonium Compounds - pharmacology; Beams (structural); Cathepsin K - metabolism; Cathepsin K - pharmacology; Cathepsins; Control equipment; CTX; Degradation; Degradation of collagen; Dentin; Dentin - metabolism; Dentistry; Dipping; Enzyme-Linked Immunosorbent Assay; Fragments; Humans; ICTP; Inhibitors; Matrix Metalloproteinases - metabolism; Matrix Metalloproteinases - pharmacology; Methacrylates - pharmacology; MMPs; Protease; Quaternary ammonium compounds; Cathepsins; Quaternary ammonium compounds; ICTP; CTX; Degradation of collagen; MMPs
• ISSN: 0109-5641; 1879-0097
• DOI: 10.1016/j.dental.2014.10.006

Abstract Objective Dentin matrices release ICTP and CTX fragments during collagen degradation. ICTP fragments are known to be produced by MMPs. CTX fragments are thought to come from cathepsin K activity. The purpose of this study was to determine if quaternary methacrylates (QAMs) can inhibit matrix MMPs and cathepsins. Methods Dentin beams were demineralizated, and dried to constant weight. Beams were incubated with rh-cathepsin B, K, L or S for 24 h at pH 7.4 to identify which cathepsins release CTX at neutral pH. Beams were dipped in ATA, an antimicrobial QAM to determine if it can inhibit dentin matrix proteases. Other beams were dipped in another QAM (MDPB) to determine if it produced similar inhibition of dentin proteases. Results Only beams incubated with cathepsin K lost more dry mass than the controls and released CTX. Dentin beams dipped in ATA and incubated for 1 week at pH 7.4, showed a concentration-dependent reduction in weight-loss. There was no change in ICTP release from control values, meaning that ATA did not inhibit MMPs. Media concentrations of CTX fell significantly at 15 wt% ATA indicating that ATA inhibits capthesins. Beams dipped in increasing concentrations of MDPB lost progressively less mass, showing that MDPB is a protease-inhibitor. ICTP released from controls or beams exposed to low concentrations were the same, while 5 or 10% MDPB significantly lowered ICTP production. CTX levels were strongly inhibited by 2.5–10% MDPB, indicating that MDPB is a potent inhibitor of both MMPs and cathepsin K. Significance CTX seems to be released from dentin matrix only by cathepsin K. MMPs and cathepsin K and B may all contribute to matrix degradation.