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At least 19 recordsLinked to original sources

PubMed1992

Effects of phenol compounds, glutathione analogues and a diuretic drug on glutathione S-transferase, glutathione reductase and glutathione peroxidase from canine erythrocytes.

1. Phenol compounds (ellagic acid, quercetin and purpurogallin), glutathione analogues (S-hexylglutathione and S-octylglutathione) and a diuretic drug (ethacrynic acid) were compared for their inhibitory effects on glutathione S-transferase (GST), glutathione reductase (GR) and glutathione peroxidase (GSH-Px) in the canine erythrocytes. 2. All these compounds inhibited GST activity; quercetin was found to be the most potent inhibitor. 3. Ellagic acid, purpurogallin, quercetin and ethacrynic acid inhibited GR activity; S-hexylglutathione and S-octylglutathione had no effect on GR and GSH-Px activities. 4. Quercetin and purpurogallin inhibited GST non-competitively toward glutathione, whereas ellagic acid showed a competitive inhibition. Ellagic acid and purpurogallin inhibited GR non-competitively toward oxidized glutathione.

Animals↗

PubMed2002

Glutathione determination and a study of the activity of glutathione-peroxidase, glutathione-transferase, and glutathione-reductase in renal transplants.

The aim of this work is to study the temporary variation of oxidative stress in renal transplants, both in plasma and in erythrocytes (CR). In order to do so, we determined total glutathione (GST) levels, both oxidized (GSSG) and reduced (GSH), and the activity of enzymes, glutathione peroxidase (G-px), glutathione reductase (G-red) and glutathione transferase (GSt), in renal transplant patients. Determinations were made 48 h before the transplant 1 week and 2 weeks after the renal transplant. The results obtained confirm a high "oxidative stress" rate, resulting from the equilibrium between the production of free radicals and the activity of antioxidants, the former being higher proportionally. Immediately after the transplant there is an increase of oxidative stress, which results in an increase of G-red, a marked decrease of G-px in plasma and in erythrocytes (CR) and an abrupt drop both in GST levels in plasma and in GSG (as well as in the [GSH]/[GSSG] relationship). As times goes on, after the transplant, there is a significant improvement in the activity of antioxidant enzymes, but there is no normalization, which is easily seen in the fact that total glutathione levels and the activity of the various enzymes approach the average values of the control group.

Erythrocytes↗

PubMed1969

The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates.

1. Changes in liver glutathione reductase and glutathione peroxidase activities in relation to age and sex of rats were measured. Oxidation of GSH was correlated with glutathione peroxidase activity. 2. Glutathione reductase activity in foetal rat liver was about 65% of the adult value. It increased to a value slightly higher than the adult one at about 2-3 days, decreased until about 16 days and then rose after weaning to a maximum at about 31 days, finally reaching adult values at about 45 days old. 3. Weaning rats on to an artificial rat-milk diet prevented the rise in glutathione reductase activity associated with weaning on to the usual diet high in carbohydrate. 4. In male rats glutathione peroxidase activity in the liver increased steadily up to adult values. There were no differences between male and female rats until sexual maturity, when, in females, the activity increased abruptly to an adult value that was about 80% higher than that in males. 5. The rate of GSH oxidation in rat liver homogenates increased steadily from 3 days until maturity, when the rate of oxidation was about 50% higher in female than in male liver. 6. In the liver a positive correlation between glutathione peroxidase activity and GSH oxidation was found. 7. It is suggested that the coupled oxidation-reduction through glutathione reductase and glutathione peroxidase is important for determining the redox state of glutathione and of NADP, and also for controlling the degradation of hydroperoxides. 8. Changes in glutathione reductase and glutathione peroxidase activities are discussed in relation to the redox state of glutathione and NADP and to their effects on the concentration of free CoA in rat liver and its possible action on ketogenesis and lipogenesis.

Age Factors↗

PubMed1997

apd1+, a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: a role for glutathione and a glutathione-conjugate pump.

Mutants in the adenine biosynthetic pathway of yeasts (ade1 and ade2 of Saccharomyces cerevisiae, ade6 and ade7 of Schizosaccharomyces pombe) accumulate an intense red pigment in their vacuoles when grown under adenine-limiting conditions. The precise events that determine the formation of the pigment are however, still unknown. We have begun a genetic investigation into the nature and cause of pigmentation of ade6 mutants of S. pombe and have discovered that one of these pigmentation defective mutants, apd1 (adenine pigmentation defective), is a strict glutathione auxotroph. The gene apd1+ was found to encode the first enzyme in glutathione biosynthesis, gamma-glutamylcysteine synthetase, gcs1+. This gene when expressed in the mutant could confer both glutathione prototrophy and the characteristic red pigmentation, and disruption of the gene led to a loss in both phenotypes. Supplementation of glutathione in the medium, however, could only restore growth but not the pigmentation because the cells were unable to achieve sufficient intracellular levels of glutathione. Disruption of the second enzyme in glutathione biosynthesis, glutathione synthetase gsh2+, also led to glutathione auxotrophy, but only a partial defect in pigment formation. A reevaluation of the major amino acids previously reported to be present in the pigment indicated that the pigment is probably a glutathione conjugate. The ability of vanadate to inhibit pigment formation indicated that the conjugate was transported into the vacuole through a glutathione-conjugate pump. This was further confirmed using strains of S. cerevisiae bearing disruptions in the recently identified glutathione-conjugate pump, YCF1, where a significant reduction in pigment formation was observed. The pump of S. pombe is distinct from the previously identified vacuolar pump, hmt1p, for transporting cadystin peptides into vacuoles of S. pombe.

ATP-Binding Cassette Transporters↗

PubMedDate not supplied

[Effect of chloditan on the changes of activity of glutathione transferase, glutathione reductase and glutathione content in the adrenal glands and liver in rats].

The chloditan (o.p-DDD, mitotane), which causes the destruction of the human and dog adrenal cortex, on the most essential system of xenobiotic metabolism: glutathione-S-transferase--glutathione has been studied. The effect of o,p-DDD on GSH level and activity of glutathione-S-transferase and glutathione reductase which maintain the level of reduced glutathione was analyzed in the adrenal and liver tissue of rats. This species is resistant to adrenocorticolytic action of o,p-DDD. It was shown that feeding of rats weighting 200-240 g with oil solution of o,p-DDD (75 mg daily) for 3 days causes the decrease in activity of glutathione-S-transferase and content of oxidazed glutathione in the adrenals with simultaneous increase of the content of reduced glutathione. The glutathione-S-transferase and glutathione reductase activity in the liver rises under the effect of o,p-DDD, the decrease of the GSH level being observed. The revealed changes may explain the species sensitivity of animals to o,p-DDD.

Adrenal Glands↗

PubMedDate not supplied

Enzymatic conjugation of hexachloro-1,3-butadiene with glutathione. Formation of 1-(glutathion-S-yl)-1,2,3,4,4-pentachlorobuta-1,3-diene and 1,4-bis(glutathion-S-yl)-1,2,3,4-tetrachlorobuta-1,3-diene.

The glutathione-dependent metabolism of the nephrotoxin and nephrocarcinogen hexachloro-1,3-butadiene (HCBD) was investigated in subcellular fractions from rat liver and kidney. HCBD was metabolized by hepatic glutathione S-transferases to (E)- and (Z)-1-(glutathion-S-yl)-pentachlorobuta-1,3-diene (GPCB) in a ratio of 20:1, which were identified by secondary ion MS and by GC-MS after acid hydrolysis. The formation of GPCB was dependent on time and on protein and glutathione concentrations. Microsomal glutathione S-transferases from rat liver catalyzed GPCB formation more efficiently than did cytosolic glutathione S-transferases; very low rates of GPCB formation were observed in kidney subcellular fractions. GPCB is also a substrate for glutathione S-transferases and is metabolized to a diglutathione conjugate, which was identified by secondary ion MS and 13C NMR spectrometry as 1,4-bis(glutathion-S-yl)-1,2,3,4-tetrachlorobuta-1,3-diene (BTCB). BTCB formation from GPCB was dependent on time and on protein, glutathione, and GPCB concentrations. Hepatic cytosol catalyzed BTCB formation more efficiently than did hepatic microsomes; significant amounts of BTCB were also formed in kidney cytosol. Hepatic formation of glutathione S-conjugates, translocation of the S-conjugates to the kidney, and renal processing to form reactive intermediates may be the cause of HCBD-induced nephrotoxicity and, perhaps, nephrocarcinogenicity.

Animals↗

PubMed1985

The effect of chronic ethanol ingestion on hepatic lipid peroxide, glutathione, glutathione peroxidase and glutathione transferase in rats.

Water containing 20% ethanol was given for a period of 3, 6 and 9 weeks to rats, and changes in hepatic lipid peroxide, glutathione, glutathione peroxidase and glutathione transferases were investigated. Lipid peroxide levels and glutathione peroxidase activities remained unchanged after 3 weeks and started to increase thereafter. Glutathione levels and glutathione transferase activities were significantly increased following ethanol consumption. These results show that chronic ethanol consumption stimulates hepatic lipid peroxidation in rats. This stimulation is not dependent on glutathione depletion and the increased glutathione peroxidase and glutathione transferase activities may reflect an adaptive change against ethanol-induced lipid peroxide toxicity.

Alcoholism↗

PubMed1979

Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver.

Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver have been investigated. After perfusing the lung to remove contaminating blood, this organ was found to have an apparent concentration of glutathione (2mM) which is approx. 20% of that found in the liver. Both organs contain very low levels of glutathione disulfide. Neither phenobarbital nor methylcholanthrene had a significant effect on the levels of reduced glutathione in lung and liver. In addition, the activities of some glutathione-metabolizing enzymes--glutathione reductase and glutathione S-transferase activity assayed with four different substrates--were observed to be 5-to 60-fold lower in lung tissue than in the liver.

Animals↗

PubMed1985

Subcellular localization and modification with ageing of glutathione, glutathione peroxidase and glutathione reductase activities in human fibroblasts.

Differential centrifugation and isopycnic equilibration in density gradients were used to localize glutathione (GSH), glutathione peroxidase and glutathione reductase in the subcellular organelles of WI-38 fibroblasts. GSH was present in all the subcellular fractions, whereas the glutathione peroxidase and reductase activities were restrained to the cytoplasm and the mitochondrial fractions. After equilibration in density gradients, the results showed the presence of GSH, glutathione peroxidase and glutathione reductase in both the cytoplasm and mitochondria. GSH was also located in plasma membranes and probably in peroxisomes, endoplasmic reticulum and lysosomal membranes. Evolution of GSH in ageing fibroblasts showed a sudden increase of its concentration just before cell death. The glutathione peroxidase activity already decreases in the early passages, while the decrease of the glutathione reductase activity was constant and reached a drastic low level at the end of the culture. In conclusion, GSH is probably involved in the cell degeneration associated with ageing but because of its multiple functions and its ubiquitous localization, it is difficult to assert to which extent this metabolite is implicated in the ageing process.

Cell Line↗

PubMed1986

Glutathione peroxidase, glutathione reductase and glutathione-S-transferase activities in the rhesus monkey lens as a function of age.

The activities of glutathione peroxidase, glutathione reductase and glutathione-S-transferase were determined in lenses from rhesus monkeys (Macaca mulatta) as a function of age. The ages ranged from 137 day old embryos to a 34 year old. Glutathione peroxidase activity (units/g lens) occurred at a very low level in lenses of fetuses and neonates, but increased dramatically with age, peaking in the adult of about 12 to 20 years of age and declining thereafter. Glutathione reductase activity (units/g lens) decreased throughout juvenile life, leveling off when adulthood was reached (at least 6 years of age). Glutathione-S-transferase activity showed considerable age-related variation. Calculations show that glutathione reductase is rate-limiting in the glutathione redox pathway.

Age Factors↗

PubMed1986

The distribution and comparison of glutathione, glutathione reductase and glutathione S-transferase in various camel tissues.

Extracts prepared from liver, kidney, lung and brain of camel contain glutathione, glutathione S-transferase and glutathione reductase. Liver had the highest level of glutathione (218.7 mumol/g wet weight) whereas brain had the lowest level (66.4 mumol/g wet weight). The highest activity for glutathione reductase was found in the kidney (2.6 mumol/min/mg protein) while the lowest activity was found in the lung (0.9 mumol/min/mg protein). Glutathione S-transferase activity was the highest in liver (4.2 mumol/min/mg protein) and the lowest in brain (1 mumol/min/mg protein). Purified glutathione S-transferases from lung, kidney, brain and liver were similar in their molecular size, subunit composition as well as immuno-reactivity and showed some differences in their response to heat and inhibitors.

Animals↗

PubMed1994

Glutathione peroxidase and glutathione reductase activities towards glutathione-derived antioxidants.

A new class of glutathione derivatives with antioxidant properties has been prepared by transformation of the NH2 group into a pyrrole ring with various substitutions at the 2 and 5 positions. Due to steric hindrance and/or hydrophobicity of the 2-5-disubstituted pyrrole ring, the reduced glutathione derivatives are poor substrates of the glutathione peroxidase and do not effectively compete with GSH. The oxidized glutathione derivatives are, in turn, relatively good substrates (Km = 1.5 mM) of the glutathione reductase as compared to natural oxidized glutathione (Km = 0.51 mM) but are not effective competitors of the enzyme. It can be considered that the new glutathione derivatives do not strongly interfere with the natural enzymatic defence against fatty acid hydroperoxides formed during an oxidative stress.

Animals↗

PubMed1992

Changes in blood glutathione concentrations, and in erythrocyte glutathione reductase and glutathione S-transferase activity after running training and after participation in contests.

Previously sedentary men (n = 23) and women (n = 18) were trained to run a half marathon contest after 40 weeks. Total blood glutathione had increased by 20 weeks of training and had returned to normal after 40 weeks. Erythrocyte glutathione reductase activity had increased by 20 weeks and remained elevated after 40 weeks. This effect was accompanied by decreases in glutathione reductase coefficients, which indicated that increases in the presence of riboflavin may have been responsible for the changes in reductase activity. Erythrocyte glutathione S-transferase activity had increased slightly after 20 weeks of training and a much more marked increase was found after 40 weeks. This may have been indicative of the occurrence of lipid peroxidation in this phase of training. The participants ran a 15-km race after the first 20 weeks of training and a half marathon after 40 weeks. Blood glutathione tended to decrease after the 15-km race and increased after the half marathon. In both cases it had returned to normal values 5 days after the race. Erythrocyte glutathione reductase was elevated 1 day after the races, and had returned to normal after 5 days. This could also have been explained from concurrent changes in the riboflavin content of the erythrocytes. Erythrocyte glutathione S-transferase activity decreased after both races, but was restored 5 days after the half marathon while such was not the case after the 15-km race.

Adult↗

PubMed1996

N-nitrosamines and their effects on the level of glutathione, glutathione reductase and glutathione S-transferase activities in the liver of male mice.

The present study investigates the influence of different chemical structure of N-nitroso compounds on the hepatic level of reduced glutathione (GSH), glutathione reductase (GSH-R) and glutathione S-transferase (GST) activities in the liver of male Balb/C mice after treatment with 20 mg/kg body weight of each compound for 1 h as a single dose. The level of reduced glutathione decreased significantly between 37 and 70% after the treatment of male mice with ethylbutylnitrosamine (-37%), diphenylnitrosamine (-50%), propylbutylnitrosamine (-52%), diethylnitrosamine (-54%), ethylmethylnitrosamine (-55%), and dibutylnitrosamine (-70%), whereas, methylpropylnitrosamine increased the level of GSH by 71%. All the N-nitrosamine compounds tested increased the activity of glutathione reductase except ethylmethylnitrosamine had no effect. The activity of glutathione S-transferase activity was inhibited after treatment of the male mice with diphenylnitrosamine (-60%), dibutylnitrosamine (-60%), and methylpropylnitrosamine (-81%), while, ethylmethylnitrosamine and ethylbutylnitrosamine had no effect on such activity. On the other hand, diethylnitrosamine increased the activity of glutathione S-transferase by 50%. It can be postulated from this study that the chemical structure of N-nitrosamines plays a significant role in the alteration of GSH level and GSH metabolizing enzymes, since the substitution of different groups on the nitroso group was found to be capable of causing an alteration in such activities.

Animals↗

PubMed1991

Age-related changes of glutathione content, glutathione reductase and glutathione peroxidase activity of human erythrocytes.

1. In order to investigate the effect of aging on the erythrocyte glutathione system, total glutathione (GSH), glutathione reductase (GSH-red) and glutathione peroxidase (GSH-px) levels were measured in erythrocytes from 33 young (mean age = 30.5 +/- 9.7 years) and 28 aged (mean age = 68.9 +/- 11.4 years) healthy individuals. 2. GSH was 3.5 +/- 1.8 microM/g Hb for the young group, a value significantly greater (P less than 0.01) than 2.3 +/- 0.9 microM/g Hb found for the aged group. Similarly, GSH-red activity, 5.5 +/- 1.8 IU/g Hb, was higher (P less than 0.05) for the young group than 3.4 +/- 0.9 IU/g Hb found for the aged group. The GSH-px activity levels for the young group, 21.1 +/- 5.9 IU/g Hb, were significantly greater (P less than 0.01) than 12.0 +/- 3.3 IU/g Hb for the aged group. The lower activity detected in the aged group for all of these parameters of the glutathione redox system was not related to low levels of hematocrit or hemoglobin. 3. There was no statistical difference in the activation coefficient (AC) of reductase (+FAD/-FAD) between groups, which seems to indicate that the lower activity of glutathione reductase observed in the aged group was not due to riboflavin deficiency. 4. Additional information is required to determine the mechanisms controlling the glutathione redox system and its role in the aging process.

Aged↗

PubMed1988

The effect of cholesterol feeding on lipid peroxide, glutathione, glutathione peroxidase and glutathione transferase in the liver of rats.

Liver cholesterol, phospholipid, triglyceride, lipid peroxide and glutathione levels as well as glutathione peroxidase and glutathione transferase activities were determined in rats fed a high-cholesterol (2%, w/w), high-cholic acid (0.5%, w/w) diet for 3 months. Cholesterol feeding caused an increase in hepatic cholesterol and triglyceride levels, but no change was observed in hepatic phospholipid levels. In addition, a significant increase in hepatic lipid peroxide levels and a significant decrease in glutathione peroxidase and glutathione transferase activities have been observed. However, hepatic glutathione content after cholesterol feeding remained unchanged. These results show that cholesterol feeding leads to the stimulation of hepatic lipid peroxidation as well as impairment of glutathione-related enzyme activities in rats.

Animals↗

PubMed1996

Effect of glutathione, glutathione sulphonate and S-hexylglutathione on the conformational stability of class pi glutathione S-transferase.

The glutathione S-transferases (GST) are a supergene family of phase II detoxification enzymes which catalyse the S-conjugation between glutathione and an electrophilic substrate. The active site can be divided into two adjacent functional regions, a highly specific G-site for binding the physiological substrate glutathione and a nonspecific H-site for binding nonpolar electrophilic substrates. Equilibrium and kinetic unfolding experiments employing tryptophan fluorescence and enzyme activity measurements were preformed to study the effect of ligand binding to the G-site on the unfolding and stability of the porcine class pi glutathione S-transferase against urea. The presence of glutathione caused a shift in the equilibrium-unfolding curves towards lower urea concentrations and enhanced the first-order rate constant for unfolding suggesting a destabilisation of the pGSTP1-1 structure against urea. The presence of either glutathione sulphonate or S-hexylglutathione, however, produced the opposite effect in that their binding to the G-site appeared to exet a stablising effect against urea. The binding of these glutathione analogues also reduced significantly the degree of cooperativity of unfolding indicating a possible change in the protein's unfolding pathway.

Animals↗

PubMed2003

Study of the activity of glutathione-peroxidase, glutathione-transferase, and glutathione-reductase in renal transplants.

The aim of this work was to study the temporare variation of oxidative stress in the plasma and erythrocytes (CR) of renal transplant patients We determined total glutathione (GST), as well as oxidized (GSSG) and reduced (GSH) fractions and the activity of glutathione peroxidase (G-px), glutathione reductase (G-red) and glutathione transferase (GSt). Determinations were performed 48 hours before transplant as well as 1 and 2 weeks after the renal transplant. The results showed a high "oxidative stress" rate, resulting from the equilibrium between the production of free radicals and the activity of antioxidants, the former being higher proportionally. Immediately after the transplant, there was an increase in oxidative stress, which resulted in an increased G-red, a marked decrease in plasma and in erythrocyte G-px (CR9 and an abrupt drop both in GST levels in plasma and in GSG (as well as in the [GSH]/[GSSG] relationship). Thereafter there was a significant improvement in the activity of antioxidant enzymes, but without normalization; the total glutathione levels and the activity of various enzymes approached the average values of the control group.

Erythrocytes↗