Glutathione S-Transferases

  • Abhijit Raha
  • Kenneth D. Tew
Part of the Cancer Treatment and Research book series (CTAR, volume 87)

Abstract

Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1]. GSH is synthesized via the γ-glutamyl cycle (Figure 4–1). The rate-limiting step is catalyzed by γ-glutamylcysteine synthetase (γ-GCS) to form γ-glutamylcysteine. The following step is catalyzed by glutathione synthetase, which forms GSH. The glyoxalase system, which consists of glyoxalase I and II, converts methylglyoxal to D-lactate and replenishes GSH. Glutathione that is oxidized by oxidants (GSSG), such as hydrogen peroxide, and in response to oxidant stress is converted back to the reduced form of glutathione (GSH) by glutathione reductase. Glutathione is broken down into cysteinyl glycine by γ-glutamyltranspeptidase; GSH, as a nucleophile, is utilized as a cofactor in a variety of detoxification reactions. Among the enzymes that employ GSH in this manner are the glutathione S-transferases.

Keywords

Lipase Thiol Histidine Pyrene Carboplatin 

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Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Abhijit Raha
  • Kenneth D. Tew

There are no affiliations available

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