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Updated: Jun 25, 2026

Measuring Global Cellular Matrix Metalloproteinase and Metabolic Activity in 3D Hydrogels
Published on: January 22, 2019
2-hydroxyethyl methacrylate as an inhibitor of matrix metalloproteinase-2
Rodrigo V Carvalho1, Fabrício A Ogliari, Ana P de Souza
1Department of Operative Dentistry, School of Dentistry, Federal University of Pelotas, Rio Grande do Sul, Brazil. rodrigo.varella@gmail.com
Abstract:
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.

