Expression of Human Phospholipid Hydroperoxide Glutathione Peroxidase

  • Kunio Yagi
  • Sadaaki Komura
  • Nobuko Ohishi
Part of the Methods in Molecular Biology™ book series (MIMB, volume 196)


Among lipid peroxides and related free radicals in the process of lipid peroxidation, the first stable products, lipid hydroperoxides, are unique from the viewpoint of pathogenicity. Because of their stability, these hydroperoxides can migrate throughout the body via the bloodstream. This disseminates the deleterious effects of these species, resulting in the provocation of secondary disorders of a disease. Accordingly, the elimination of lipid hydroperoxides would contribute to the prevention of lipid peroxide-mediated diseases. For this purpose, enzymatic decomposition of the hydroperoxides would be the most preferable approach. As enzymes capable of decomposing lipid hydroperoxides, at least four types of glutathione peroxidase (GPx) have been reported (1); that is, classical GPx; gastrointestinal GPx; plasma GPx; and phospholipid hydroperoxide GPx or monomeric GPx (PHGPx).


104C1 Cell Sodium Selenite Lipid Hydroperoxide Phospholipid Hydroperoxide Linoleic Acid Hydroperoxide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. 1.
    Chu, F.-F. (1994) The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively. Cytogenet. Cell Genet. 66, 96–98.PubMedCrossRefGoogle Scholar
  2. 2.
    Godeas, C., Sandri, G., and Panfili, E. (1994) Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria. Biochim. Biophys. Acta. 1191, 147–150.PubMedCrossRefGoogle Scholar
  3. 3.
    Yagi, K., Komura, S., Kojima, H., Sun, Q., Nagata, N., Ohishi, N., and Nishikimi, M. (1996) Expression of human phospholipid hydroperoxide glutathione peroxidase gene for protection of host cells from lipid hydroperoxide-mediated injury. Biochem. Biophys. Res. Commun. 219, 486–491.PubMedCrossRefGoogle Scholar
  4. 4.
    Yagi, K., Shidoji, Y., Komura, S., Kojima, H., and Ohishi, N. (1998) Dissipation of mitochondrial membrane potential by exogenous phospholipid monohydroperoxide and protection against this effect by transfection of cells with phospholipid hydroperoxide glutathione peroxidase gene. Biochem. Biophys. Res. Commun. 245, 528–533.PubMedCrossRefGoogle Scholar
  5. 5.
    Yagi, K., Noda, H., Kurono, M., and Ohishi, N. (1993) Efficient gene transfer with less cytotoxicity by means of cationic multilamellar liposomes. Biochem. Biophys. Res. Commun. 196, 1042–1048.PubMedCrossRefGoogle Scholar
  6. 6.
    Duan, Y.-J., Komura, S., Fiszer-Szafarz, B., Szafarz, D., and Yagi, K. (1988) Purification and characterization of a novel monomeric glutathione peroxidase. J. Biol. Chem. 263, 19003–19008.PubMedGoogle Scholar
  7. 7.
    Nakashima, M., Komura, S., Ohishi, N., and Yagi, K. (1993) Immunochemical differentiation between novel monomeric and classic tetrameric rat liver glutathione peroxidases. Biochem. Mol. Biol. Int. 29, 1139–1144.PubMedGoogle Scholar

Copyright information

© Humana Press Inc. 2002

Authors and Affiliations

  • Kunio Yagi
    • 1
  • Sadaaki Komura
    • 1
  • Nobuko Ohishi
    • 1
  1. 1.Institute of Applied BiochemistryMitakeJapan

Personalised recommendations