Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide

Brigelius, Regina; Muckel, Christian; Akerboom, Theodorus P.M.; Sies, Helmut

doi:10.1016/0006-2952(83)90014-x

Cited by 348 publications

(154 citation statements)

References 19 publications

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“…GSH content of cells was determined using a previously described assay. 13 For the analysis of GSSG, samples were treated with N-ethylmaleimide and bathophenanthroline disulfonic acid, derivatized and analyzed by high-performance liquid columns (HPLC) as described previously. 14 MDA was analyzed by HPLC.…”

Section: Blood Samples and Analytical Proceduresmentioning

confidence: 99%

Impact of the components of metabolic syndrome on oxidative stress and enzymatic antioxidant activity in essential hypertension

et al. 2006

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The objective of the present study was to analyze the impact of metabolic syndrome (MS) and its individual components on oxidative stress (OX) and on the activity of antioxidant enzymes of patients with essential hypertension. One hundred and eighty-seven hypertensives, 127 (61.9%) of them having criteria for MS according to the International Diabetes Federation criteria and 30 healthy normotensive subjects were included. OX status was assessed by measuring glutathione oxidized/glutathione reduced and reactive oxygen species-induced byproducts of lipid peroxidation, malondialdehide, and DNA damage, 8-oxo-dG genomic and mitochondrial. Antioxidant enzymatic activity of Cu/Zn extracellular-superoxide dismutase (SOD) and catalase (CAT) was measured in plasma and glutathione peroxidase 1 in hemolysad erythrocytes. In mononuclear cells, total-SOD activity, CAT and glutathione peroxidase 1, were assessed as well. The OX state in both blood and peripheral mononuclear cells observed in hypertensives were not enhanced by the addition of components of the so-called MS. Likewise, the reduction in the activity of antioxidant enzymes, both extracellular and cytoplasmic, was not affected by the presence of additional components of the MS. Neither the number of components nor the individual addition of each of them, low high-density lipoprotein, triglycerides, abdominal obesity or fasting glucose, further impact in the OX abnormalities observed in those with only hypertension in absence of other components. In conclusion, the present data indicates that contribution of MS components to the OX burden generated by high blood pressure is minimal.

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Section: Blood Samples and Analytical Proceduresmentioning

confidence: 99%

Impact of the components of metabolic syndrome on oxidative stress and enzymatic antioxidant activity in essential hypertension

et al. 2006

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“…Owing to the limitation of sample size, direct determination of GSH by, eg, GSH S-transferase, 25 was not feasible. Therefore, we used the HUVECs were treated with the respective agents for the times indicated, washed, and incubated for 2 hours with 1 ng/mL TNF-␣ or IL-1.…”

Section: Glutathionementioning

confidence: 99%

Inhibition of Tumor Necrosis Factor-α– and Interleukin-1–Induced Endothelial E-Selectin Expression by Thiol-Modifying Agents

Friedrichs

Müller

Brigelius‐Flohé

1998

ATVB

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Abstract-The expression of endothelial-leukocyte adhesion molecules has been postulated to be regulated by redoxsensitive events. Tumor necrosis factor-␣ (TNF-␣)-and interleukin-1 (IL-1)-induced E-selectin expression was analyzed after pretreating human umbilical vein endothelial cells with different thiol-modifying agents, ie, diamide, phenylarsine oxide, N-ethylmaleimide, and diethyl maleate. E-selectin protein expression was quantified by indirect immunofluorescence. All compounds suppressed the cytokine-induced E-selectin expression in a concentrationdependent manner, whereas the antioxidant N-acetylcysteine showed no effect. The inhibitory effect of diamide (100 mol/L, 1 hour) was reversible within 6 hours when the cells were allowed to recover before application of cytokines. Reversibility was strongly delayed when cells were deprived of glutathione by buthionine sulfoximine pretreatment. Glutathione depletion alone did not influence cytokine-induced E-selectin expression. Analysis of cellular glutathione status showed a 3-fold increase in oxidized glutathione after diamide treatment. Monochlorobimane labeling also revealed a decrease in total cellular thiols. During recovery, the glutathione status was restored within 1 hour, whereas total thiol content and E-selectin expression needed at least 6 hours to return to baseline. Complete inhibition of E-selectin expression by the vicinal thiol blocker phenylarsine oxide (0.5 mol/L) was reversed by dithiols like dithiothreitol or dimercaptopropanol, but not by the monothiol 2-mercaptoethanol. These data suggest that proteins with essential thiols, most probably vicinal thiols. are involved in the IL-1-and TNF-␣-mediated induction of E-selectin. These thiols must be in the reduced state; oxidation or other modification thereof attenuates or abolishes the cells' response to the cytokines.

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“…The GSH content of the suspension was determined according to Ball [24]. Dithiothreitol can react with Ellman's reagent, therefore GSH content was measured by the GSH transferase assay when dithiothreitol was present in the incubations [25]. Intracellular cAMP concentration was measured by radioimmunoassay [26].…”

Section: Measurement Of Metabolitesmentioning

confidence: 99%

Glutathione depletion induces glycogenolysis dependent ascorbate synthesis in isolated murine hepatocytes

et al. 1996

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The relationship between glutathione deficiency, glycogen metabolism and ascorbate synthesis was investigated in isolated murine hepatocytes. Glutathione deficiency caused by various agents increased ascorbate synthesis with a stimulation of glycogen breakdown. Increased ascorbate synthesis from UDP-glucose or gulonolactone could not be further affected by glutathione depletion. Fructose prevented the stimulated glycogenolysis and ascorbate synthesis caused by glutathione consumption. Reduction of oxidised glutathione by dithiothreitol decreased the elevated glycogenolysis and ascorbate synthesis in diamide or menadione treated hepatocytes. Our results suggest that a change in GSI-I/GSSG ratio seems to be a sufficient precondition of altering glycogenolysis and a consequent ascorbate synthesis.

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Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide

Cited by 348 publications

References 19 publications

Impact of the components of metabolic syndrome on oxidative stress and enzymatic antioxidant activity in essential hypertension

Impact of the components of metabolic syndrome on oxidative stress and enzymatic antioxidant activity in essential hypertension

Inhibition of Tumor Necrosis Factor-α– and Interleukin-1–Induced Endothelial E-Selectin Expression by Thiol-Modifying Agents

Glutathione depletion induces glycogenolysis dependent ascorbate synthesis in isolated murine hepatocytes

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