Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80640
Type: Artigo de periódico
Title: Inhibition of the activity of matrix metalloproteinase 2 by triethylene glycol dimethacrylate
Author: de Carvalho, RV
Ogliari, FA
Marques, MR
de Souza, AP
Petzhold, CL
Line, SRP
Piva, E
Etges, A
Abstract: The aim of this study was to evaluate the effect of different concentrations of triethylene glycol dimethacrylate (TEGDMA) on the inhibition of matrix metalloproteinase 2 (MMP-2). Mouse gingival explants were cultured overnight in DMEM and the expression of secreted enzymes was analyzed by gelatin zymography in buffers containing 5 mM CaCl(2) (Tris-CaCl(2)) in 50 mM Tris-HCl buffer with the addition of TEGDMA at different concentrations (0.62%, 1.25%, 2.5%, or 5.0% (v/v)). The gelatinolytic proteinase present in the conditioned media was characterized as matrix metalloproteinase by means of specific chemical inhibition. The matrix metalloproteinases present in the conditioned media were characterized as MMP-2 by immunoprecipitation. The eletrophoretic bands were scanned and the transmittance values were analyzed. Data was plotted and submitted to linear regression to investigate MMP-2 inhibition as a function of TEGDMA concentration. Three major bands were detected in the zymographic assays. These bands were characterized as MMP-2. Zymogene (72 kDa), intermediate (66 kDa) and active forms of MMP-2 (62 kDa) were inhibited by TEGDMA in a dose-dependent way. These findings suggest that TEGDMA could inhibit MMP-2 expression even at small concentrations.
Subject: Gelatinase A
Matrix metalloproteinase 2
Triethyleneglycol dimethacrylate
TEGDMA
Polyacrylamide gel electrophoresis
Country: Alemanha
Editor: Springer Heidelberg
Rights: fechado
Identifier DOI: 10.1007/s00784-010-0443-5
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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