Modulation of glutathione and related enzymes in reversal of resistance to anticancer drugs

Hematol Oncol Clin North Am. 1995 Apr;9(2):383-96.

Abstract

Eukaryotic cells have evolved several mechanisms to protect cellular constituents, especially DNA, from highly reactive molecules entering from without. The greater affinity of electrophiles for thiol groups than for hydroxyl or amine groups provides a teleologic rationale that the availability of high concentrations of thiol could be protective of these other important entities. The major intracellular nonprotein thiol is the tripeptide glutathione.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Antineoplastic Agents / pharmacokinetics*
  • Buthionine Sulfoximine
  • CHO Cells
  • Cricetinae
  • Drug Resistance* / physiology
  • Ethacrynic Acid / pharmacology
  • Ethacrynic Acid / therapeutic use
  • Female
  • Gene Expression Regulation, Neoplastic
  • Glutathione / antagonists & inhibitors
  • Glutathione / metabolism*
  • Glutathione Peroxidase / metabolism*
  • Glutathione Synthase / metabolism*
  • Glutathione Transferase / antagonists & inhibitors
  • Glutathione Transferase / metabolism*
  • Humans
  • Inactivation, Metabolic
  • Male
  • Methionine Sulfoximine / analogs & derivatives
  • Methionine Sulfoximine / pharmacology
  • Methionine Sulfoximine / therapeutic use
  • Neoplasm Proteins / metabolism*
  • Oxidation-Reduction
  • Thiotepa / pharmacology
  • Thiotepa / therapeutic use
  • Tumor Cells, Cultured
  • gamma-Glutamyltransferase / metabolism*

Substances

  • Antineoplastic Agents
  • Neoplasm Proteins
  • Methionine Sulfoximine
  • Buthionine Sulfoximine
  • Thiotepa
  • Glutathione Peroxidase
  • gamma-Glutamyltransferase
  • Glutathione Transferase
  • Glutathione Synthase
  • Glutathione
  • Ethacrynic Acid