Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?

Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?

Autor Tezvergil-Mutluay, Arzu Google Scholar
Agee, Kelli A. Google Scholar
Mazzoni, Annalisa Google Scholar
Carvalho, Ricardo M. Google Scholar
Carrilho, Marcela Google Scholar
Tersariol, Ivarne L. Autor UNIFESP Google Scholar
Nascimento, Fabio D. Google Scholar
Imazato, Satoshi Google Scholar
Tjaderhane, Leo Google Scholar
Breschi, Lorenzo Google Scholar
Tay, Franklin R. Google Scholar
Pashley, David H. Google Scholar
Instituição 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
Resumo 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.
Palavra-chave Degradation of collagen
CTX
ICTP
Quaternary ammonium compounds
MMPs
Cathepsins
Idioma Inglês
Financiador NIDCR
Academy of Finland
Finnish Dental Society Apollonia
Número do financiamento NIDCR: R01 DE015306
Data de publicação 2015-02-01
Publicado em Dental Materials. Oxford: Elsevier B.V., v. 31, n. 2, p. E25-E32, 2015.
ISSN 0109-5641 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão E25-E32
Fonte http://dx.doi.org/10.1016/j.dental.2014.10.006
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000349759400003
Endereço permanente http://repositorio.unifesp.br/handle/11600/38693

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