Modulation of glutathione and its dependent enzymes in gill cells of Anguilla anguilla exposed to silica coated iron oxide nanoparticles with or without mercury co-exposure under in vitro condition

Abstract

The current study aimed to investigate the modulation of glutathione (GSH) and its dependent enzymes (glutathione reductase, GR; glutathione peroxidase, GPx; glutathione sulfotransferase, GST) from 0 to 72 h in the gill cells of Anguilla anguilla under in vitro condition exposed to silica coated iron oxide nanoparticles functionalized with dithiocarbamate (Fe3O4@SiO2/SiDTC, hereafter called 'IONPs'; 100 nm; 2.5 mg L-1) with or without mercury (Hg) coexposure. Significantly decreased TGSH content under IONP alone exposure from 0 to 72 h indicated increased utilization of the TGSH in response to IONP stress. Significant increases in the activity of GR, GPx and GST were depicted when exposed to IONP alone. Lipid peroxidation (LPG), a membrane damage trait also significantly increased under IONP alone exposure indicating the efficient role of antioxidant induction abolishing the IONP-mediated enhanced reactive oxygen species. Under Hg exposure, gill cells displayed significantly increased activity of the studied enzymes (GR, GPx and GST) and LPO which was accompanied by significantly decreased TGSH content. Concomitant (IONPs + Hg) exposure displayed a synergistic response to that of individual responses of either IOPN or Hg which was evident by significant increases in GR, GPx, GST and LPO. Overall, our findings revealed a fine tuning among the GSH and its dependent enzyme modulation under IONP, Hg and its concomitant (IONPs + Hg) exposure in A. anguilla gill cells under in vitro condition. (C) 2014 Elsevier Inc. All rights reserved.