Changes in glutathione status and 3,5,3'-triiodothyronine action in livers of rats given cysteine-deficient diets

1989 ◽  
Vol 61 (2) ◽  
pp. 301-307 ◽  
Author(s):  
H. Garcin ◽  
C. Suberville ◽  
P. Higueret ◽  
D. Higueret
Keyword(s):  
Malate Dehydrogenase ◽  
Nuclear Protein ◽  
Protein Complexes ◽  
Reduced Glutathione ◽  
Scatchard Analysis ◽  
Oxidized Glutathione ◽  
Deficient Diet ◽  
Young Rats ◽  
Glutathione Status ◽  
Glucose 6 Phosphate Dehydrogenase

1. For a period of 32 d young rats were given a diet containing (g/kg) 220 casein, 120 casein +1.93 L-cysteine (Cys), or 120 casein.2. The formation of 3,5,3'-triiodothyronine (T3)-nuclear protein complexes was reduced in rats fed on the Cys-deficient diet.3. Scatchard analysis showed that decreased formation of T3 -nuclear protein complexes was due to a decreased affinity of T3 receptors; this decrease was induced, at least in part, by a reduced glutathione content.4. In rats fed on the Cys-deficient diet there was an expected decrease in growth but an unexpected increase in the activities of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40). It is suggested that this increase is related to an increased oxidized glutathione: reduced glutathione ratio.

Vitamin A deficiency and tri-iodothyronine action at the cellular level in the rat

1989 ◽  
Vol 121 (1) ◽  
pp. 75-79 ◽  
Author(s):  
P. Higueret ◽  
I. Pailler ◽  
H. Garcin
Keyword(s):  
Vitamin A ◽  
Nuclear Protein ◽  
Protein Complexes ◽  
Vitamin A Deficiency ◽  
Cellular Level ◽  
Scatchard Analysis ◽  
Lipogenic Enzymes ◽  
Deficient Diet ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT Young rats were given a diet with or without vitamin A for a period of 7 weeks. In rats on the vitamin A-deficient diet, the formation of tri-iodothyronine (T3) complexes with nuclear proteins was reduced, and Scatchard analysis showed a decreased capacity of nuclear T3 receptors. In these rats, a decrease in growth and a decrease in the activity of lipogenic enzymes (glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase and l-malate dehydrogenase) occurred, which could be related to the decreased formation of T3–nuclear protein complexes. Journal of Endocrinology (1989) 121, 75–79

Glutathione metabolism in heart and liver of the aging rat

1994 ◽  
Vol 72 (1-2) ◽  
pp. 58-61 ◽  
Author(s):  
M. Stio ◽  
T. Iantomasi ◽  
F. Favilli ◽  
P. Marraccini ◽  
B. Lunghi ◽  
...  
Keyword(s):  
Rat Heart ◽  
Reduced Glutathione ◽  
Age Groups ◽  
Glutathione Metabolism ◽  
Oxidized Glutathione ◽  
Glutathione S Transferase ◽  
Age Related ◽  
Glutamylcysteine Synthetase ◽  
Old Rats ◽  
Glucose 6 Phosphate Dehydrogenase

A comprehensive study on glutathione metabolism in rat heart and liver as a function of age was performed. In the heart, reduced glutathione, total glutathione, and the glutathione redox index showed a decrease during aging, while oxidized glutathione levels increased in 5-month-old rats with respect to the young animals and remained quite constant in 14- and 27-month-old rats. In the liver, the highest levels of reduced glutathione were found in the 2-month-old rats, while oxidized glutathione reached a peak at 5 months. Glutathione-associated enzymes showed age-related changes. Glutathione peroxidase, unaffected by aging in the heart, decreased in the liver of the 27-month-old rats. In the heart and the liver, the highest values of glutathione S-transferase were found at 5 months and 27 months, respectively. Glucose-6-phosphate dehydrogenase followed a similar trend in both heart and liver. Glutathione reductase also showed the same behaviour in heart and in liver, increasing in old rats with respect to the other age groups. A decrease in γ-glutamylcysteine synthetase was found in the heart and liver of 27-month-old rats in comparison with the 2-month-old ones. In conclusion, a decreased antioxidant capability has been demonstrated in both heart and liver of old rats.Key words: glutathione metabolism, age, rat heart, rat liver.

Blood glutathione status during exercise: effect of carbohydrate supplementation

1993 ◽  
Vol 74 (2) ◽  
pp. 788-792 ◽  
Author(s):  
L. L. Ji ◽  
A. Katz ◽  
R. Fu ◽  
M. Griffiths ◽  
M. Spencer
Keyword(s):  
Prolonged Exercise ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Work Load ◽  
Inhibitory Effects ◽  
Carbohydrate Supplementation ◽  
Glutathione Status ◽  
Exercise Effect ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Gssg Reductase

Blood glutathione status and activities of antioxidant enzymes have been investigated during prolonged exercise with or without carbohydrate (CHO) supplementation. Eight subjects cycled at approximately 70% of maximal oxygen uptake to fatigue [134 +/- 19 (SE) min] on the first occasion (control, CON) and at the same work load and duration on the second occasion but with CHO ingestion during exercise. Blood reduced glutathione (GSH) concentration increased from 0.55 +/- 0.05 mM at rest to 0.77 +/- 0.09 mM after 120 min of exercise during CON (P < 0.01) but remained constant during CHO exercise. Blood glutathione disulfide (GSSG) levels were unchanged during CON and CHO exercise. Blood GSH + GSSG content and GSH/GSSG ratio were also significantly (P < 0.05) elevated during CON but not during CHO exercise. The increases in GSH and GSH + GSSG in CON were associated with decreases in plasma glucose and insulin levels. Activities of blood GSH peroxidase, GSSG reductase, and glucose-6-phosphate dehydrogenase were significantly increased during the CHO exercise, whereas only GSSG reductase activity was elevated during the CON ride. It is concluded that blood GSH increases during prolonged exercise and that CHO supplementation may prevent blood GSH increase possibly because of its inhibitory effects on hepatic hormonal releases, which stimulate GSH output.

scholarly journals The effect of experimental neoplastic disease on malondialdehyde level and glutathione status in erythrocytes of rats.

1997 ◽  
Vol 44 (4) ◽  
pp. 767-769 ◽  
Author(s):  
J Batko
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Elevated Level ◽  
Reduced Glutathione ◽  
Early Stage ◽  
Tumor Development ◽  
Neoplastic Disease ◽  
Advanced Stage ◽  
Oxidized Glutathione ◽  
Glutathione Status

The level of lipid peroxidation products and the content of glutathione in erythrocytes of rats with Morris 5123 hepatoma at different stages of tumor development were examined. The content of endogenous malondialdehyde (MDA) was increased throughout all periods of tumor development as compared to the results for healthy rats. From the extent of MDA generation under oxidative stress we concluded that erythrocytes of Morris 5123 hepatoma bearing rats were more susceptible to autoxidation than those from control rats. The content of reduced glutathione (GSH) and oxidized glutathione (GSSG) was increased at the early stage of tumor growth. At the advanced stage of the disease both the content of GSH and the GSH/GSSG ratio were decreased while the content of GSSG remained at the elevated level.

scholarly journals Investigation of the Defect in a Variant of Hereditary Methemoglobinemia

Blood ◽  
1962 ◽  
Vol 19 (1) ◽  
pp. 60-74 ◽  
Author(s):  
PHILIP L. TOWNES ◽  
MARTIN MORRISON
Keyword(s):  
Lactic Acid ◽  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Reduced Glutathione ◽  
Coupled System ◽  
Oxidized Glutathione ◽  
Total Glutathione ◽  
Primary Defect ◽  
New Variant ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract 1. Further evidence has been presented to confirm the fact that the methemoglobin found in a new variant of hereditary methemoglobinemia was normal methemoglobin. 2. The reduced glutathione content of the red cells of this variant was less than 50 per cent of normal. 3. The total glutathione and oxidized glutathione were proportionally deficient. 4. The low glutathione content did not result from abnormal degradation nor lack of adequate reducing mechanisms. The primary defect was considered to be one of inadequate glutathione synthesis. 5. Various enzymes were assayed, including the following: glucose 6-phosphate dehydrogenase, lactic acid dehydrogenase, triosephosphate dehydrogenase, glutathione reductase, glucose 6-phosphate dehydrogenase-glutathione reductase (coupled system) and catalase. 6. This variant of methemoglobinemia was considered to result from inadequate synthesis of glutathione. The deficiency of this essential co-factor apparently results in an impairment of triosephosphate dehydrogenase activity and consequently insufficient reduction of DPN, an essential component of the DPNH-dependent methemoglobin reductase.

Exhaustive physical exercise causes oxidation of glutathione status in blood: prevention by antioxidant administration

1992 ◽  
Vol 263 (5) ◽  
pp. R992-R995 ◽  
Author(s):  
J. Sastre ◽  
M. Asensi ◽  
E. Gasco ◽  
F. V. Pallardo ◽  
J. A. Ferrero ◽  
...  
Keyword(s):  
Physical Exercise ◽  
Normal Values ◽  
Reduced Glutathione ◽  
Redox Status ◽  
Oxidized Glutathione ◽  
Oral Vitamin ◽  
Glutathione Status ◽  
Glutathione Oxidation ◽  
Lactate And Pyruvate ◽  
Glutathione Redox

We have studied the effect of exhaustive concentric physical exercise on glutathione redox status and the possible relationship between blood glutathione oxidation and blood lactate and pyruvate levels. Levels of oxidized glutathione (GSSG) in blood increase after exhaustive concentric physical exercise in trained humans. GSSG levels were 72% higher immediately after exercise than at rest. They returned to normal values 1 h after exercise. Blood reduced glutathione (GSH) levels did not change significantly after the exercise. We have found a linear relationship between GSSG-to-GSH and lactate-to-pyruvate ratios in human blood before, during, and after exhaustive exercise. In rats, physical exercise also caused an increase in blood GSSG levels that were 200% higher after physical exercise than at rest. GSH levels did not change significantly. Thus, both in rats and humans, exhaustive physical exercise causes a change in glutathione redox status in blood. We have also found that antioxidant administration, i.e., oral vitamin C, N-acetyl-L-cysteine, or glutathione, is effective in preventing oxidation of the blood glutathione pool after physical exercise in rats.

scholarly journals Reduction of Oxidized Glutathione in Normal and Glucose-6-Phosphate Dehydrogenase Deficient Erythrocytes and Their Hemolysates

Blood ◽  
1970 ◽  
Vol 35 (2) ◽  
pp. 166-172 ◽  
Author(s):  
EGMOND E. RIEBER ◽  
ERNST R. JAFFÉ
Keyword(s):  
Dehydrogenase Activity ◽  
Hemolytic Anemia ◽  
Dehydrogenase Deficiency ◽  
Reduced Glutathione ◽  
Human Erythrocytes ◽  
Red Cells ◽  
Oxidized Glutathione ◽  
Metabolic Processes ◽  
Intact Cells ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract When assayed by the ability to reduce oxidized glutathione to reduced glutathione, glucose-6-phosphate dehydrogenase deficiency of either the Negro or Caucasian mutant variety could be demonstrated in hemolysates only with hemoglobin concentrations below 2.0 Gm. per 100 ml. In intact erythrocytes, the inability to regenerate reduced glutathione was apparent regardless of the concentration of red cells. The process of hemolysis, therefore, appeared to permit the demonstration of higher levels of activity in G-6-PD deficient human erythrocytes than was possible in intact cells. A markedly deficient capacity to regenerate endogenous reduced glutathione or to reduce exogenous oxidized glutathione, however, could be demonstrated with the hemolysate of erythrocytes from a patient with hereditary nonspherocytic hemolytic anemia associated with a deficiency of glucose-6-phosphate dehydrogenase activity. These studies have emphasized the hazards involved in extrapolating the results of studies performed with hemolysates to metabolic processes within intact erythrocytes.

scholarly journals Basic components of glutathion system in rat erythrocytes under conditions of toxic damage on the background of an alimental protein lack

2020 ◽  
Vol 12 (1) ◽  
pp. 31-38
Author(s):  
Halyna Kopylchuk ◽  
Ivanna Nykolaichuk
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Peroxidase Activity ◽  
Glutathione Transferase ◽  
Reduced Glutathione ◽  
Oxidized Glutathione ◽  
Glutathione Peroxidase Activity ◽  
Rat Erythrocytes ◽  
Toxic Damage ◽  
Glucose 6 Phosphate Dehydrogenase

The article is devoted to the study of the main components of the glutathione system under conditions of toxic damage against the background of nutritional protein deficiency: the content of reduced and oxidized glutathione with the determination of the GSH/GSSG ratio, the activity of glutathione-dependent enzymes – glutathione peroxidase, glutathione transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase. The concentration of reduced glutathione in the erythrocyte hemolysate was studied using Elman's reagent after deproteinization of the samples. Glutathione transferase activity was determined by the rate of formation of glutathione S conjugates by reacting reduced glutathione with a substrate of 1-chloro-2.4-dinitrobenzene. Glutathione peroxidase activity was evaluated by the formation of oxidized glutathione. The activity of glutathione reductase in erythrocytes was determined by the method, is based on measuring the oxidation rate of NADPH+H+, which is recorded by decreasing absorption at a wavelength of 340 nm. A decrease in the ratio of GSH/GSSG in rat erythrocytes under conditions of toxic damage against a nutritional deficiency of protein is indicated by a functional shift in the thiol-disulfide balance towards increased use of the reduced form of glutathione for antioxidant protection. It was established that toxic damage is a key factor in reducing the level of glutathione transferase against the background of an increase in glutathione peroxidase activity in rat erythrocytes, the activation of which probably prevents the progression of LPO processes. At the same time, under conditions of toxic damage, against the background of alimentary protein deficiency, a decrease in glutathione reductase and glucose-6-phosphate dehydrogenase activity is observed, which leads to blocking of the first stage of glucose-6-phosphate metabolism in the pentose phosphate cycle, resulting in a decrease in the amount of NADPH and, accordingly reduced glutathione.

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