Elsevier

Methods in Enzymology

Volume 105, 1984, Pages 445-451
Methods in Enzymology

[59] Glutathione disulfide (GSSG) efflux from cells and tissues

https://doi.org/10.1016/S0076-6879(84)05062-XGet rights and content

Publisher Summary

Because of the release of glutathione disulfide (GSSG) into the extracellular space, cells, such as erythrocytes, or tissues, such as eye lens or liver, were found to respond to oxidizing conditions. Under steady-state conditions, the rate of metabolism of an externally added model hydroperoxide, t-butyl hydroperoxide, was observed to be linearly related to the rate of efflux of GSSG from the isolated perfused rat liver; in this organ, about 3% of the flux through glutathione (GSH) peroxidase is represented by an extracellular appearance of GSSG. Thus, even though most cell types contain an appreciable activity of GSSG reductase, a rise in the intracellular production of GSSG is accompanied by an export of the disulfide; apparently, there are multiple ways of disposing of GSSG, which may accumulate. Based on the relation between hydroperoxide metabolism and GSSG efflux, it was proposed that the latter might be a useful extracellular parameter to assess hydroperoxide turnover in cells and tissues. Because of the multiple factors that may influence the rate of GSSG efflux, appropriate caution is required in each particular case in which the parameter is used.

References (30)

  • S.K. Srivastava et al.

    J. Biol. Chem.

    (1969)
  • H. Sies et al.

    FEBS Lett.

    (1972)
  • H. Güntherberg et al.

    Anal. Biochem.

    (1966)
  • O.W. Griffith

    Anal. Biochem.

    (1980)
  • C.W. Tabor et al.

    Anal. Biochem.

    (1977)
  • D.J. Reed et al.

    Anal. Biochem.

    (1980)
  • F. Tietze

    Anal. Biochem.

    (1969)
  • T.P.M. Akerboom et al.

    J. Biol. Chem.

    (1982)
  • D. Eberle et al.

    J. Biol. Chem.

    (1981)
  • M.E. Anderson et al.

    J. Biol. Chem.

    (1980)
  • T.W. Rall et al.

    J. Biol. Chem.

    (1952)
  • G.M. Bartoli et al.

    FEBS Lett.

    (1978)
  • D. Häberle et al.

    FEBS Lett.

    (1979)
  • R.A. Lawrence et al.

    J. Nutr.

    (1978)
  • J. Isaacs et al.

    Biochim. Biophys. Acta

    (1977)
  • Cited by (193)

    • The stay-green phenotype of TaNAM-RNAi wheat plants is associated with maintenance of chloroplast structure and high enzymatic antioxidant activity

      2016, Plant Physiology and Biochemistry
      Citation Excerpt :

      The supernatant was diluted with potassium phosphate buffer 100 mM, EDTA 5 mM pH 7.5. Total thiol content was determined at 412 nm after reduction of 5,5′-ditiobis-(2-nitrobenzoic acid) (Sies and Akerboom, 1984). Homogenates were prepared as described in 2.4.

    • Auranofin-induced oxidative stress causes redistribution of the glutathione pool in Taenia crassiceps cysticerci

      2015, Molecular and Biochemical Parasitology
      Citation Excerpt :

      Both of these protective systems are dependent of the glutathione-reductase activity of the multifunctional TGR. A second potential mechanism to contend with oxidative conditions is the translocation of disulfide form of glutathione (GSSG) to cytoplasm compartments as in vacuoles [68] or its excretion of the outside of the cell [14,15]. In the present work, we have demonstrated that significant amounts of GSSG are extruded from the cysticerci in the presence of AF (Figs. Fig. 44c and Fig. 66).

    • HPLC separation of human serum albumin isoforms based on their isoelectric points

      2014, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
    View all citing articles on Scopus
    View full text