2-Hydroxyethyl methacrylate as an inhibitor of matrix metalloproteinase-2

被引:29
作者
Carvalho, Rodrigo V. [1 ]
Ogliari, Fabricio A. [1 ]
de Souza, Ana P. [2 ]
Silva, Adriana F. [1 ]
Petzhold, Cesar L. [3 ]
Line, Sergio R. P. [2 ]
Piva, Evandro [1 ]
Etges, Adriana [4 ]
机构
[1] Univ Fed Pelotas, Sch Dent, Dept Operat Dent, BR-96015560 Pelotas, RS, Brazil
[2] Univ Estadual Campinas, Piracicaba Dent Sch, Dept Morphol, Sao Paulo, Brazil
[3] Univ Fed Rio Grande do Sul, Inst Chem, Dept Organ Chem, BR-90046900 Porto Alegre, RS, Brazil
[4] Univ Fed Pelotas, Sch Dent, Dept Oral Pathol, BR-96015560 Pelotas, RS, Brazil
关键词
2-hydroxyethyl methacrylate; gelatinase A; matrix metalloproteinase-2; matrix metalloproteinases; polyacrylamide gel electrophoresis; SELF-ETCHING ADHESIVES; LONG-TERM DURABILITY; IN-VIVO; GELATINASES MMP-2; DENTIN; CHLORHEXIDINE; DEGRADATION; ACTIVATION;
D O I
10.1111/j.1600-0722.2008.00591.x
中图分类号
R78 [口腔科学];
学科分类号
100302 [口腔临床医学];
摘要
This study evaluated the effect of different concentrations of 2-hydroxyethyl methacrylate (HEMA) on the inhibition of matrix metalloproteinase-2 (MMP-2) in vitro. Mouse gingival explants were cultured overnight in Dulbecco's modified Eagle's minimal essential medium, following which the expression of secreted enzymes was analyzed by gelatin zymography and the effects of different amounts of HEMA on enzyme activity were investigated. The gelatinolytic proteinases present in the conditioned media were characterized as being matrix metalloproteinases (MMPs) by means of specific chemical inhibition. The MMPs present in the conditioned media were identified, using immunoprecipitation, as MMP-2. Three major bands were detected in the zymographic assays and were characterized, according to their respective molecular weights, into the following forms of MMP-2: zymogene (72 kDa), intermediate (66 kDa), and active (62 kDa). All forms of MMP-2 were inhibited by HEMA in a dose-dependent manner, implying that MMP-2 may be inhibited by HEMA in vivo.
引用
收藏
页码:64 / 67
页数:4
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