Cellular and Molecular Life Sciences CMLS

, Volume 57, Issue 13–14, pp 1825–1835

The glutathione peroxidases

  • J. R. Arthur

DOI: 10.1007/PL00000664

Cite this article as:
Arthur, J. CMLS, Cell. Mol. Life Sci. (2001) 57: 1825. doi:10.1007/PL00000664


There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to their biological function. The functions of the selenoperoxidases were originally studied in systems where their activity was manipulated by changing dietary selenium levels. More recently, molecular techniques have allowed overexpression of selenoperoxidases in cell lines and animals. Additionally, cellular glutathione peroxidase knockout mice have been used to investigate the functions of this protein. From this work it is clear that the selenoperoxidases are involved in cell antioxidant systems. However, they also have more subtle functions in ensuring the regulation and formation of arachadonic acid metabolites that are derived from hydroperoxide intermediates. The range of biological processes, which are potentially dependent on optimal selenoperoxidase activity in mammals, emphasises the importance of achieving adequate selenium intake in the diet.

Key words. Selenium; glutathione peroxidase; peroxides; overexpression; knockouts. 

Copyright information

© Birkhäuser Verlag Basel, 2000

Authors and Affiliations

  • J. R. Arthur
    • 1
  1. 1.Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, Scotland (United Kingdom), Fax +44 01224 716629, e-mail: jra@rri.sari.ac.uk GB

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