Methyl linoleate ozonide: a substrate for rat glutathione S-transferases.
Glutathione S-transferases (GST) were shown to be capable of reducing the toxicity of the ozonide of methyl linoleate (MLO) by catalyzing its reaction with reduced glutathione (GSH). MLO was a substrate for both cytosolic and microsomal GST. Isoenzyme 2-2 demonstrated the highest specific activity. Oxidised glutathione and aldehydes were identified as products of the reaction, with unstable glutathione-conjugates being formed as intermediates only. It was concluded that the GST-activity toward MLO may be similar to the GST-peroxidase activity with lipid hydroperoxides as substrates.
Vos
R M
RM
Department of Toxicology, Agricultural University, Wageningen, The Netherlands.
Rietjens
I M
IM
Alink
G M
GM
van Bladeren
P J
PJ
D000818:Animals; D005978:Glutathione / Q000494:pharmacology; D005982:Glutathione Transferase / Q000378:metabolism*; D008658:Inactivation, Metabolic; D008041:Linoleic Acids; D008099:Liver / Q000166:cytology / Q000201:enzymology; D008168:Lung / Q000166:cytology / Q000201:enzymology; D008264:Macrophages / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology; D010126:Ozone / Q000493:pharmacokinetics*; D051381:Rats; D013379:Substrate Specificity
D008041:Linoleic Acids; D010126:Ozone; D005982:Glutathione Transferase; D005978:Glutathione; C052559:methyl linoleate ozonide