Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione levels. Using a glutaredoxin sensor (sCGrx1pER), which rapidly and specifically equilibrates with the reduced glutathione (GSH)–glutathione disul...

Glutathione disappears as a soluble, nonprotein component after it has been added to serum, either in the reduced (GSH) or oxidized (GSSG) form. When GSH is added to serum it is rapidly oxidized to GSSG by some dialyzable component of serum. Glutathione is lost because of interaction of serum proteins with the GSSG formed in this manner or added directly. A similarly rapid loss of glutathione o...

The horseradish peroxidase (HRP)-catalyzed oxidation of p-phenetidine and acetaminophen was investigated. Studies using the spin probe 2-ethyl-1-hydroxy-2,5,5-trimethyl-3-oxazolidine (OXANOH) suggested these oxidations involve the generation of substrate-derived free radicals. This was confirmed by using glutathione (GSH) in these incubations in the presence of the spin trap 5,5-dimethyl-1-pyrr...

To obtain a comprehensive profile of the erythrocyte antioxidant defense potential during aging, we investigated copper-zinc superoxide dismutase (CuZn-SOD), seleno-dependent glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-RD), and glutathione-S-transferase (GSH-S-T) activities in human erythrocytes from 167 apparently healthy subjects, ages one month to 63 years (102 females, 65 m...

Elimination of hydrogen sulfide from glutathione (GSH) converts a well known cellular nucleophile to an electrophilic species, gamma-glutamyldehydroalanylglycine (EdAG). We have found that a sulfonium metabolite formed from GSH and busulfan undergoes a facile beta-elimination reaction to give EdAG, which is an alpha,beta-unsaturated dehydroalanyl analog of GSH. EdAG was identified as a metaboli...

Ifosfamide, a clinically potent chemotherapeutic agent, causes the depletion of intracellular glutathione (GSH) levels in various cell types. GSH is the major intracellular reductant against oxidative stress. 4-Hydroxyifosfamide (4-OH-IF), the activated form of ifosfamide, depletes GSH levels in T cells and natural killer (NK) cells; this is accompanied by a decrease in T-cell and NK-cell funct...

Glutathione, Upsilon-Glu-Cys-Gly, is one of the most abundant small molecules in biosphere. Its main form is the reduced monomer (GSH), serving to detoxicate xenobiotics and heavy metals, reduce protein thiols, maintain cellular membranes and deactivate free radicals. Its oxidized dimer (GSSG) controls metal content of metallothionein. The results presented provided a quantitative and structura...

Lehninger and Schneider (1) studied the swelling of isolat,ed liver mitochondria induced by reduced glutathione (GSH). One outstanding difference from thyroxine-induced swelling was that GSH-induced swelling was not reversible. These studies have been extended by Lehninger and Gotterer (2, 3) with the discovery that GSH-induced swelling is reversed by adenosine triphosphate + Mg ++ + bovine ser...

Lehninger and Schneider (1) studied the swelling of isolat,ed liver mitochondria induced by reduced glutathione (GSH). One outstanding difference from thyroxine-induced swelling was that GSH-induced swelling was not reversible. These studies have been extended by Lehninger and Gotterer (2, 3) with the discovery that GSH-induced swelling is reversed by adenosine triphosphate + Mg ++ + bovine ser...

Research on the electro-oxidation of glutathione (GSH) may give insight into its real oxidation mechanism on biomembranes. In the present work, the unusual oxidation process of GSH on an Au electrode was probed by cyclic voltammetry (CV) technique. Voltammetric studies showed that –SH in GSH was the unique target of electro-oxidation by excluding the other potential oxidation sites (amido group...