Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/38693
Title: Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?
Authors: Tezvergil-Mutluay, Arzu
Agee, Kelli A.
Mazzoni, Annalisa
Carvalho, Ricardo M.
Carrilho, Marcela
Tersariol, Ivarne L. [UNIFESP]
Nascimento, Fabio D.
Imazato, Satoshi
Tjaderhane, Leo
Breschi, Lorenzo
Tay, Franklin R.
Pashley, David H.
Univ Turku
Georgia Regents Univ
Univ Bologna
Univ British Columbia
UNIBAN Univ Bandeirante Anhanguera
Univ Mogi das Cruzes
Universidade Federal de São Paulo (UNIFESP)
Osaka Univ
Univ Oulu
Keywords: Degradation of collagen
CTX
ICTP
Quaternary ammonium compounds
MMPs
Cathepsins
Issue Date: 1-Feb-2015
Publisher: Elsevier B.V.
Citation: Dental Materials. Oxford: Elsevier B.V., v. 31, n. 2, p. E25-E32, 2015.
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. (C) 2014 Academy of Dental Materials. Published by Elsevier B.V. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/38693
ISSN: 0109-5641
Other Identifiers: http://dx.doi.org/10.1016/j.dental.2014.10.006
Appears in Collections:Em verificação - Geral

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