NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

Scott, MD; Zuo, L; Lubin, BH; Chiu, DT

doi:10.1182/blood.v77.9.2059.bloodjournal7792059

Cited by 35 publications

(39 citation statements)

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“…As with other compounds (Scott Pt al, 1989a. 1990b, 1991a, the intraerythrocytic entrapment was linear and dose-dependent on the extracellular globin chain concentration (data not shown).…”

Section: Kesultsmentioning

confidence: 88%

α‐ and β‐haemoglobin chain induced changes in normal erythrocyte deformability: comparison to β thalassaemia intermedia and Hb H disease

Scott

Rouyer-Fessard

et al. 1992

Br J Haematol

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The alpha- and beta-thalassaemias are characterized by decreased erythrocyte deformability. To determine what effects excess alpha- and beta-haemoglobin (globin) chains have on cellular and membrane deformability, purified haem-containing alpha- and beta-chains were entrapped within normal erythrocytes. Entrapment of purified alpha-chains in normal erythrocytes resulted in a significant decrease in cellular and membrane deformability similar to that observed in beta-thalassaemia intermedia. The decreased deformability was correlated with alpha-chain membrane deposition, an alteration in membrane proteins and a decrease in membrane reactive thiol groups. These changes in membrane and cellular deformability were time dependent and closely correlated with membrane alpha-chain deposition. The membrane changes and the loss of membrane deformability appeared to account for the loss of cellular deformability in the alpha-chain loaded cells. While both beta-chain loaded and Hb H erythrocytes demonstrated a significant loss of cellular deformability, this loss was less pronounced than in the alpha-chain loaded and beta-thalassaemic cells and may arise from either the increased intracellular viscosity of the beta-chain loaded cells or to the smaller amount of membrane bound globin. In summary, these studies demonstrate that alteration of cellular and membrane deformability occurs very rapidly and as a direct consequence of the autoxidation and membrane binding of the unpaired globin chains.

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“…As with other compounds (Scott Pt al, 1989a. 1990b, 1991a, the intraerythrocytic entrapment was linear and dose-dependent on the extracellular globin chain concentration (data not shown).…”

Section: Kesultsmentioning

confidence: 88%

α‐ and β‐haemoglobin chain induced changes in normal erythrocyte deformability: comparison to β thalassaemia intermedia and Hb H disease

Scott

Rouyer-Fessard

et al. 1992

Br J Haematol

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“…In clinical G-6-PD deficiency, the consequential low concentrations of GSH in erythrocytes are complicated by downstream loss of normal GPX activity (reviewed in Ref. 53), which leads to increased oxidant sensitivity of the cell. It may be recalled that, in a similar manner, sleep deprivation was not associated with increased GPX activity in response to glutathione depletion.…”

Section: Discussionmentioning

confidence: 99%

Antioxidant defense responses to sleep loss and sleep recovery

Everson

Laatsch

Hogg

2005

American Journal of Physiology-Regulatory, Integrative and Comp

151

120

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Sleep deprivation in humans is widely believed to impair health, and sleep is thought to have powerful restorative properties. The specific physical and biochemical factors and processes mediating these outcomes, however, are poorly elucidated. Sleep deprivation in the animal model produces a condition that eventually becomes highly lethal, lacks specific localization, and is reversible with sleep, implying mediation by a biochemical abnormality. Metabolic and immunological consequences of sleep deprivation point to a high potential for antioxidant imbalance. The objective, therefore, was to study glutathione content in the liver, heart, and lung, because glutathione is considered a major free radical scavenger that reflects the degree to which a tissue has been oxidatively challenged. We also investigated major enzymatic antioxidants, including catalase and glutathione peroxidase, as well as indexes of glutathione recycling. Catalase activity and glutathione content, which normally are tightly regulated, were both decreased in liver by 23-36% by 5 and 10 days of sleep deprivation. Such levels are associated with impaired health in other animal models of oxidative stress-associated disease. The decreases were accompanied by markers of generalized cell injury and absence of responses by the other enzymatic antioxidants under study. Enzymatic activities in the heart indicated an increased rate of oxidative pentose phosphate pathway activity during sleep deprivation. Recovery sleep normalized antioxidant content in liver and enhanced enzymatic antioxidant activities in both the liver and the heart. The present results link uncompensated oxidative stress to health effects induced by sleep deprivation and provide evidence that restoration of antioxidant balance is a property of recovery sleep.

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“…Many studies have been reported on the relationship between glutathione and stress response in animal cells [7,8,[26][27][28][29]. In mammalian cells, glutathione peroxidase (GPx) has a primary function to scavenge H202.…”

Section: Discussionmentioning

confidence: 99%

Oxidative stress response in yeast: effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae

1995

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Role of intraceHular glutathione in the response of Saccharomyces cerevisiae to H202 was investigated. Depletion of cellular glutathione or inhibition of ~,-glutamyleysteine synthetase (GSH-I) enhanced the sensitivity to H202 and suppressed the adaptation to H202. A mutant deficient in GSH-I also showed the hypersensitivity and could not adapt to H202. Incubation of the cell with amino acids constituting glutathione (L-GIu, L-Cys, Gly) increased the intracellular glutathione content, and subsequently the cell acquired resistance against H202. These results strongly suggest that intracellular glutathione plays an important role in the adaptive response in S. cerevisiae to oxidative damage.

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NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

Cited by 35 publications

References 0 publications

α‐ and β‐haemoglobin chain induced changes in normal erythrocyte deformability: comparison to β thalassaemia intermedia and Hb H disease

α‐ and β‐haemoglobin chain induced changes in normal erythrocyte deformability: comparison to β thalassaemia intermedia and Hb H disease

Antioxidant defense responses to sleep loss and sleep recovery

Oxidative stress response in yeast: effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae

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