Oxidant-mediated modulation of the intracellular redox state affects the apoptotic cascade by altering the balance between cellular signals for survival and suicide. Apolipoprotein A-IV (Apo A-IV) is known to possess antioxidant-like activity. In the present study, we tested 1) whether Apo A-IV could influence redox-dependent apoptosis and, if so, 2) whether such an effect could be mediated by ...

Glucose-6-phosphate dehydrogenase (G6PDH)-deficient cells of Saccharomyces cerevisiae showed increased susceptibility and were unable to induce adaptation to oxidative stress. Historically, mainly in human erythrocytes, it has been suggested and accepted that decreased cellular GSH, due to loss of the NADPH-dependent activity of glutathione reductase (GR), is responsible for the increased sensi...

Altered antioxidant status has been reported in schizophrenia. The glutathione (GSH) redox system is important for reducing oxidative stress. GSH, a radical scavenger, is converted to oxidized glutathione (GSSG) through glutathione peroxidase (GPx), and converted back to GSH by glutathione reductase (GR). Measurements of GSH, GSSG and its related enzymatic reactions are thus important for evalu...

Bangia fuscopurpurea is a widespread intertidal seaweed that commercially cultured in China. This frequently exposed to hyposalinity stress, but little known about the adaptation mechanisms. Ascorbate−glutathione (AsA−GSH) cycle plays important roles many organisms under variety of abiotic including hyposaline stress. In this study, we investigated response key metabolites and enzymes involved ...

Recent evidence suggests that the endogenous antioxidant glutathione may play a protective role in cardiovascular disease. To directly investigate the role of glutathione in the regulation of glucose metabolism in hypertension, we studied the acute effects of in vivo infusions of this antioxidant (alone or in combination with insulin) on whole body glucose disposal (WBGD) using euglycemic gluco...

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...

Spatial and temporal expression and regulation of the antioxidant enzymes, glutathione peroxidase (GSH-Px), glutathione disulfide reductase (GSSG-Rd) may be important in determining cell-specific susceptibility to embryotoxicants. Creation of tissue-specific ontogenies for antioxidant enzyme activities during development is an important first step in understanding regulatory relationships. Earl...

Two glutathione peroxidase activities have been described in rat liver. One contains selenium and is virtually absent in selenium deficiency. The other seems to be unaffected by selenium status. The selenium-dependent glutathione peroxidase utilizes H,O, and organic hydroperoxides as substrates, but the selenium-independent glutathione peroxidase is much more efficient with organic hydroperoxid...

Biosurfaces are universally covered with fluid microfilms containing reduced glutathione (GSH) and other antioxidants whose putative roles include the detoxification of ambient ozone (O(3)). It is generally believed that O(3) accepts an electron from the thiolate GS(2-) function [pK(a)(GS(-)) = 8.8] of GSH to produce thiyl GS(*-) radicals en route to the disulfide GSSG. Here, we report novel el...

Aim: The current study aims to examine the balance between glutathione and glutathione sulfide and how this was disturbed in patients with impaired fasting glucose (IFG) level. The study also included 8-hydroxy-2’-deoxyguanosine to provide a more comprehensive picture of the overall redox state. Methodology: A cross-sectional analysis of ninety medication free participants without reported hist...