Disease relevance of Selenodiglutathione

• The selenium metabolite selenodiglutathione induces cell death by a mechanism distinct from H2O2 toxicity [1].
• PATIENTS AND METHODS: We investigated the activity of two selenium species, methylseleninic acid (MSA) and selenodiglutathione (SDG) in a panel of human lymphoma cell lines and in a primary lymphoma culture system [2].
• One pair of cells, CCL-210 (normal lung fibroblasts) and A549 (lung adenocarcinoma cells), exhibited a large difference in their sensitivity to selenite but no significant difference in their sensitivity to selenodiglutathione [3].
• A single dose of selenodiglutathione (GSSeSG) or sodium selenite (SS) was injected i.v. into pregnant CD-1 mice on day 12 of gestation at dosages varying from 16.4-32.0 mumol/kg body weight [4].

High impact information on Selenodiglutathione

• 3-Mercaptopyruvate sulfurtransferase (3-MST; EC 2.8.1.2) and GAPDH also bound selenium supplied as selenodiglutathione formed from SeO3(2-) and glutathione [5].
• In the presence of a selenium-binding protein, a low level of selenodiglutathione formed from SeO3(2-) and glutathione could effectively replace the high concentrations of selenide routinely used as substrate in the SPS in vitro assays [5].
• Ribonucleotide reductase activity was inhibited in an in vitro assay by selenite and selenodiglutathione but not by selenate [6].
• Selenodiglutathione was the most effective form of selenium examined that inhibited tumor cell growth [7].
• Formation of selenodiglutathione was paralleled by a rapid reduction of cytochrome c, a known oxidant for superoxide anions [8].

Biological context of Selenodiglutathione

• The selenium metabolite selenodiglutathione induces p53 and apoptosis: relevance to the chemopreventive effects of selenium [9]?
• HPLC analysis of bile indicated absence of selenite and presence of selenodiglutathione (GS-Se-SG) and/or its hydrolysis products as the major biliary selenite metabolites [10].

Anatomical context of Selenodiglutathione

• Amino acid incorporation in a cell-free system derived from rat liver has previously been found to be inhibited by GSSeSG (selenodiglutathione) [11].
• Selenite and selenodiglutathione (GS-Se-SG) efficiently inhibited 5-lipoxygenase activity in sonicates of human monoclonal B-lymphocytes [12].
• No interaction of selenite, selanete, or selenodiglutathione with Cd and plasma in the absence of erythrocytes in vitro was noted [13].
• The product of the reaction between sodium selenite and glutathione, designated as selenodiglutathione (GSSeSG), nearly completely inhibits amino acid incorporation from [14C]leucyl-tRNA by free polyribosomes isolated from rat liver [14].

Associations of Selenodiglutathione with other chemical compounds

• Ligated segments, double perfusion experiments, and uptake by BBMV indicated that selenium as selenodiglutathione or selenodicysteine was taken up faster than when present as selenite [15].

Gene context of Selenodiglutathione

• Selenite and selenodiglutathione (GS-Se-SG), inhibit mammalian cell growth and are efficient oxidants of reduced thioredoxin and reduced thioredoxin reductase [16].
• Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase [17].
• These data suggest that selenite and selenodiglutathione inactivate the AP-1 factor and provide a mechanism by which selenium compounds inhibit cell growth [16].
• Selenodiglutathione (GSSeSG), a potent inhibitor of elongation factor 2 (EF2) has been used to study amino acid incorporation in a rat liver cell-free system [18].

Analytical, diagnostic and therapeutic context of Selenodiglutathione

• The liquid chromatography - mass spectrometry (LC-MS) data showed that, in the ionic condition of incubation medium, GSH promptly reduced SeO3(2-) (< or = 2 min) in its elemental form Se0, which cannot ascribe to selenodiglutathione a direct role in the effect of GSH [19].

References