ArticleThe Biochemical journal2001
(S)-preferential detoxification of 4-hydroxy-2(E)-nonenal enantiomers by hepatic glutathione S-transferase isoforms in guinea-pigs and rats.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Contrasting the genetic architecture of cardiac glutathione against other organs: unveiling a unique tissue-specific locus.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- Mass Spectrometry in Advancement of Redox Precision Medicine.Advances in experimental medicine and biology · 2019Review
- Proteomics and Beyond: Cell Decision-Making Shaped by Reactive Electrophiles.Trends in biochemical sciences · 2019Review
- Effects of Local Heart Irradiation in a Glutathione S-Transferase Alpha 4-Null Mouse Model.Radiation research · 2015Article
- Glutathionylated 4-hydroxy-2-(E)-alkenal enantiomers in rat organs and their contributions toward the disposal of 4-hydroxy-2-(E)-nonenal in rat liver.Free radical biology & medicine · 2014Article
- Stereoselective effects of 4-hydroxynonenal in cultured mouse hepatocytes.Chemical research in toxicology · 2010Article
- Oxidative stress and covalent modification of protein with bioactive aldehydes.The Journal of biological chemistry · 2008Review
- The stereochemical course of 4-hydroxy-2-nonenal metabolism by glutathione S-transferases.The Journal of biological chemistry · 2008Article
- Effect of Docosahexaenoic Acid Ingestion on Temporal Change in Urinary Excretion of Mercapturic Acid in ODS Rats.Journal of clinical biochemistry and nutrition · 2007Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In guinea-pig liver cytosol, racemic 4-hydroxy-2(E)-nonenal (HNE), a reactive and highly toxic product released from biomembranes by lipid peroxidation, was detoxified (S)-preferentially by GSH conjugation mediated by glutathione S-transferases (GSTs) and (R)-preferentially by NAD(+)-dependent oxidation mediated by aldehyde dehydrogenase (ALDH). The GST-mediated detoxification of the HNE enantiomers proceeded at much higher rates than that mediated by ALDH in guinea-pig liver cytosol. All the major guinea-pig GSTs, A1-1, M1-1, M1-2 and M1-3*, isolated from guinea-pig liver cytosol also catalysed the (S)-preferential conjugation of the HNE enantiomers. The liver and other major tissues of guinea-pigs had no immunologically detectable level of a putative GSTA4-4 orthologue, which exists as a minor GST protein in rat, mouse and human livers and exhibits extremely high catalytic activity towards HNE. All the hepatic rat GSTs, A1-1(2), A1-3, A4-4, M1-1, M1-2 and M2-2, also catalysed the (S)-preferential conjugation of HNE enantiomers.
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