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2‐Hydroxyethyl methacrylate as an inhibitor of matrix metalloproteinase‐2
Author(s) -
Carvalho Rodrigo V.,
Ogliari Fabrício A.,
De Souza Ana P.,
Silva Adriana F.,
Petzhold Cesar L.,
Line Sergio R. P.,
Piva Evandro,
Etges Adriana
Publication year - 2009
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.2008.00591.x
Subject(s) - matrix metalloproteinase , zymography , in vivo , methacrylate , in vitro , matrix (chemical analysis) , chemistry , enzyme , microbiology and biotechnology , biochemistry , gelatinase , gelatin , biology , chromatography , organic chemistry , copolymer , polymer
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 .