Physiological role of mGSTA4-4, a glutathione S-transferase metabolizing 4-hydroxynonenal: generation and analysis of mGsta4 null mouse.

@article{Engle2004PhysiologicalRO,
  title={Physiological role of mGSTA4-4, a glutathione S-transferase metabolizing 4-hydroxynonenal: generation and analysis of mGsta4 null mouse.},
  author={Mark R Engle and Sharda P. Singh and P. Czernik and D. Gaddy and D. Montague and J. Ceci and Yusong Yang and S. Awasthi and Y. Awasthi and P. Zimniak},
  journal={Toxicology and applied pharmacology},
  year={2004},
  volume={194 3},
  pages={
          296-308
        }
}
The lipid peroxidation product 4-hydroxynon-2-enal (4-HNE) is a strong electrophile that forms covalent adducts with proteins and, to a lesser extent, nucleic acids and phospholipids. The generation of 4-HNE appears to be an inevitable consequence of aerobic metabolism. The metabolism of 4-HNE is mainly, although not entirely, conjugative, and proceeds via Michael addition of glutathione to the double bond of 4-HNE. This reaction is catalyzed by specialized glutathione S-transferases (GSTs… Expand
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Molecular mechanisms of ALDH3A1-mediated cellular protection against 4-hydroxy-2-nonenal.
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Two distinct 4-hydroxynonenal metabolizing glutathione S-transferase isozymes are differentially expressed in human tissues.
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