title: Role of glutathione on acrolein-induced cytotoxicity and mutagenicity in Escherichia coli.
abstract: The reduced form of glutathione (GSH) is a well-known antioxidant, while there have been few reports indicating the contribution of glutathione to protection of Escherichia coli cells from the lethal effect of oxidative damage. Here, we report that depletion of glutathione causes hypersensitivity of E. coli to acrolein, the structurally simplest alpha, beta-unsaturated aldehyde derived from lipid peroxide-degradation, and that GSH can chemically react with acrolein in vitro thus reducing its toxicity. We further demonstrated that acrolein inactivates glutathione oxidoreductase followed by depletion of glutathione, probably as a part of the toxic effect of acrolein. These results suggested that GSH contributes to cellular defense against the toxic effects.
authors.affiliation: Department of Molecular and Cellular Biology, Biological Institute, Graduate School of Science, Tohoku University, Sendai 980-8578, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nunoshiba
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
mesh_terms: D000171:Acrolein / Q000737:chemistry / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects* / Q000502:physiology; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism*; D005980:Glutathione Reductase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D009153:Mutagens / Q000494:pharmacology*; D018384:Oxidative Stress
chemical_list: D009153:Mutagens; D000171:Acrolein; D006861:Hydrogen Peroxide; D005980:Glutathione Reductase; D005978:Glutathione