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Effect of reactive oxygen and carbonyl species on crucial cellular antioxidant enzymes
Authors:Lesgards Jean-François  Gauthier Cyrielle  Iovanna Juan  Vidal Nicolas  Dolla Alain  Stocker Pierre
Affiliation:aBiosciences (Institut des sciences moléculaire de Marseille), université Paul Cézanne - UMR 6263, 13397 Marseille, France;bInteraction et Modulateurs de Réponses – CNRS-UPR3243, IFR 88, 13009 Marseille, France;cStress cellulaire - INSERM 624, parc scientifique et technologique de luminy, 13288 Marseille, France
Abstract:Numerous reactive oxygen species (ROS) and reactive carbonyl species (RCS) issuing from lipid and sugar oxidation are known to damage a large number of proteins leading to enzyme inhibition and alteration of cellular functions. Whereas studies in literature only focus on the reactivity of one or two of these compounds, we aimed at comparing in the same conditions of incubations (4 and 24 h at 37 °C) the effects of both various RCS (4-hydroxynonenal, 4-hydroxyhexenal, acrolein, methylglyoxal, glyoxal, malondialdehyde) and ROS (H2O2, AAPH) on the activity of key enzymes involved in cellular oxidative stress: superoxide dismutase (Cu,Zn-SOD), glutathione peroxidase (GPx), glutathione S-transferase (GST) and glucose-6-phosphate dehydrogenase (G6PDH). This was realized both in vitro on purified proteins and MIAPaCa-2 cells. Incubation of these enzymes with RCS resulted in a significant time- and concentration-dependent inhibition for both pure enzymes and in cell lysates. Among all RCS and ROS, hydroxynonenal (HNE) was observed as the most toxic for all studied enzymes except for SOD and is followed by hydrogen peroxide. At 100 μM, HNE resulted in a 50% reduction of GPx, 56% of GST, 65% of G6PDH, and only 10% of Cu,Zn-SOD. Meanwhile it seems that concentrations used in our study are closer to biological conditions for ROS than for RCS. H2O2 and AAPH-induced peroxyl radicals may be probably more toxic towards the studied enzymes in vivo.
Keywords:ROS   RCS   Antioxidant enzyme   Inhibition
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