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Glutathione synthesis is increased by induction of γ-glutamyl-cysteinyl synthetase,148 and so are the phase-II-detoxifying enzymes, GST149 and UDP-glucuronosyltransferase.147 GST induction enhances the co-ordinated inactivation, via GSH conjugation, of DNA hydroperoxides and lipid hydroperoxides formed as secondary metabolites during oxidative stress.150 GST also catalyzes GSH conjugation of highly-reactive, toxic αβ-unsaturated lipid aldehydes generated by β-scission of lipid hydroperoxides of ω-6 polyunsaturated fatty acids, 4-hydroxy trans-2-nonenal (HNE) being the most abundant.151 These lipid-peroxidation products combine spontaneously with cysteine, histidine and lysine residues of proteins, potentially modifying protein function and resulting in cellular toxicity, and have been suggested to mediate and amplify the cellular effects of their free-radical precursors.152 UDP-glucuronosyltransferase induction would improve the metabolisation, via glucuronidation, of pro-oxidant toxicants, such as benzo(a)pyrene,153 pentachlorophenol,154 acetaminophen,155 aliphatic alcohols156 and manadione.157 Phase-II products are then extruded from the cell via the hepatocellular efflux pumps, MRP1, MRP2, MRP3, MRP4 (ABCC4) and the breast cancer resistance protein (BCRP, ABCG2), all of which are also upregulated.158-160 Glutathione conjugates are substrates of MRP2 and MRP1.161,162 Since these transporters also transfer GSSG, MRP1/2-mediated GSSG extrusion helps to maintain low intracellular GSSG levels, when GSSG reduction back to GSH via GSSG reductase becomes rate-limiting

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Material characterization of MCNs/Ln/GD/FR NPs As illustrated in Fig