title: [Glutathione S-transferases (GSTs)].
abstract: Glutathione S-transferases (GSTs) are a family of multifunctional detoxifying enzymes that catalyse the conjugation of glutathione with large number of compounds bearing an electrophilic center, including carcinogens, and also bind a variety of nonsubstrate ligands. The transferases are widely distributed in the mammalian species and can be grouped into three classes on the basis of subunit composition: alpha (basic), mu (neutral), and pi (acidic). The liver is an organ possessing abundant GST-alpha. GST-mu is also present in the liver and lymphocytes, but this is absent in approximately 50% of the human population. GST-pi (originally found in the placenta) is widely located in the lung, kidney, GI tract, erythrocytes and cancer cells. The present review describes a new nomenclature of human GST isoenzymes and recent investigations of this enzymes, including ours. Implications of each isoenzyme are also discussed.
authors.affiliation: Second Department of Internal Medicine, Toho University School of Medicine.
authors.forename: M
authors.initials: M
authors.lastname: Sugimoto
mesh_terms: D000818:Animals; D005982:Glutathione Transferase / Q000145:classification / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000145:classification / Q000378:metabolism; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008107:Liver Diseases / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D009626:Terminology as Topic
chemical_list: D007527:Isoenzymes; D005982:Glutathione Transferase