Influence of γ-Glutamyl Transpeptidase Inactivation on the Status of Extracellular Glutathione and Glutathione Conjugates

  • Donald J. Reed
  • William W. Ellis
Part of the Advances in Experimental Medicine and Biology book series (AEMB)


Glutathione-S-transferases, which catalyze the conjugation of GSH* with a large number of electrophilic chemicals, have been studied extensively as indicated by the recent review of Chasseaud, 1979. Neither the intermediary fate of these glutathione-Sconjugates nor the extent of extrahepatic sites for the initial hydrolytic reaction catalyzed by γ-glutamyl transpeptidase (EC 2.3. 2.2) is well understood. Biliary excretion of glutathione-Sconjugates from the liver can be quantitative in some instances (Wahlländer and Sies, 1979). While GSH may be released from the liver to the systemic circulation, both GSH and GSSG appear to be excreted via the bile (Sies et al., 1978). A majority of the systemic glutathione appears to be degraded extracellularly by the kidney (Hahn et al., 1978; Häberle et al., 1979). In contrast, biliary glutathione and glutathioné-S-conjugates may be substrates for γ-glutamyl transpeptidase located in canalicular plasma membranes, plasma membrane of biliary duct epithelial cells (Rutenberg et al., 1969; Tanaka, 1974) and intestinal mucosal cells (Grafström et al., 1980).


Total Glutathione Ethacrynic Acid Glutathione Conjugate Mercapturic Acid Diethyl Maleate 


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Copyright information

© Springer Science+Business Media New York 1982

Authors and Affiliations

  • Donald J. Reed
    • 1
  • William W. Ellis
    • 1
  1. 1.Department of Biochemistry and BiophysicsOregon State UniversityCorvallisUSA

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