title: The mutual sparing effects of selenium and vitamin E in animal nutrition may be further explained by the discovery that mammalian thioredoxin reductase is a selenoenzyme.
abstract: The recent discovery that mammalian thioredoxin reductase is a selenoprotein furnishes an additional explanation of the mutual sparing roles of selenium and vitamin E in cellular antioxidant systems. Thioredoxin reductases isolated from human lung adenocarcinoma cells, human Jurkat T-cells and HeLa cells contain selenocysteine which is located in a C-terminal tripeptide, -Cys-SeCys-Gly.
authors.affiliation: Okayama University, Faculty of Agriculture, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Tamura
authors.forename: V
authors.initials: V
authors.lastname: Gladyshev
authors.forename: S Y
authors.initials: SY
authors.lastname: Liu
authors.forename: T C
authors.initials: TC
authors.lastname: Stadtman
mesh_terms: D000595:Amino Acid Sequence; D000824:Animal Nutritional Physiological Phenomena; D000818:Animals; D000975:Antioxidants / Q000494:pharmacology; D006801:Humans; D008322:Mammals / Q000378:metabolism*; D008969:Molecular Sequence Data; D012643:Selenium / Q000737:chemistry / Q000494:pharmacology*; D017279:Selenocysteine / Q000737:chemistry*; D013880:Thioredoxin-Disulfide Reductase / Q000737:chemistry*; D014407:Tumor Cells, Cultured; D014810:Vitamin E / Q000494:pharmacology*
chemical_list: D000975:Antioxidants; D017279:Selenocysteine; D014810:Vitamin E; D013880:Thioredoxin-Disulfide Reductase; D012643:Selenium