Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro

1987 ◽  
Vol 45 (1) ◽  
pp. 77-91 ◽  
Author(s):  
Frank J. Giblin ◽  
Janet P. McCready ◽  
Lisa Schrimscher ◽  
Venkat N. Reddy
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Cation Transport ◽  
Glutathione Reductase Activity

scholarly journals Antioxidant activity of the probiotic consortium in vitro

2014 ◽  
Vol 2 ◽  
Author(s):  
Saule Saduakhasova ◽  
Almagul Kushugulova ◽  
Samat Kozhakhmetov ◽  
Gulnara Shakhabayeva ◽  
Indira Tynybayeva ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Superoxide Dismutase ◽  
Glutathione Reductase ◽  
Reductase Activity ◽  
Superoxide Dismutase Activity ◽  
Total Antioxidant Activity ◽  
Bacterial Cultures ◽  
Total Antioxidant ◽  
Glutathione Reductase Activity

Introduction: Available evidence suggests that probiotics have different biological functions that depend on several mechanisms, such as antioxidant and DNA-protective activities. The probiotic consortium includes bacterial cultures such as Streptococcus thermophilus, Lactococcus lactis, Lactobacillus plantarum, and other bacterial cultures isolated from traditional Kazakh dairy products (ayran, kumys, shubat, and healthy clinical material). The aim of this study was to investigate the total antioxidant activity of the consortium of probiotic bacteria and to determine the activity of superoxide dismutase, glutathione reductase, and DNA-protective action.Material and methods: In vitro comet assay was used to determine the antigenotoxicity of the probiotic consortium. Total antioxidant activity was determined using a method of analysis with Trolox as the equivalent. The analysis method of superoxide dismutase activity assesses the inhibition rate of the nitroblue tetrazolium reduction to formazan by superoxide dismutase. Determination of glutathione reductase activity is based on the measurement of the NADPH oxidation speed.Results: A significantly high level of the total antioxidant activity of the probiotic consortium intact cells (15.3 mM/ml) was observed whereas the activity index of  lysate  was 11.1 mM/ml.The superoxide dismutase activity of probiotic consortium lysate was evaluated, with values that peaked at 0.24 U/mg protein. The superoxide dismutase activity of the consortium was lower in comparison to L.fernentum E-3 and L.fernentum E-18 cultures with values of 0.85 U/mg and 0.76 U/mg protein, respectively. SOD activity of probiotic consortium whole cells was not observed, which is typical for lactic acid bacteria.Glutathione reductase plays an important role in the optimal protection from oxidative stress. Glutathione reductase activity of the studied probiotic consortium was low; moreover, the activity of the lysate was two times higher than the activity of the cells reaching 0.01 units/ml. Investigations by Dr. Li have shown that the intracellular glutathione may give a significant protection of Lactococcus from the damaging action of H2O2, even at very low concentrations.The data from our study suggests that the co-incubation of the epithelial cells with probiotic bacteria reduces the percentage of damaged cells (damage index–0.60).Conclusion: The studied probiotic consortium has antigenotoxic and antioxidant activities. Preparations and products of this probiotic consortium may serve as a protective component in the intestinal microbial ecosystem. 

scholarly journals Familial deficiency of glutathione reductase in human blood cells

Blood ◽  
1976 ◽  
Vol 48 (1) ◽  
pp. 53-62 ◽  
Author(s):  
H Loos ◽  
D Roos ◽  
R Weening ◽  
J Houwerzijl
Keyword(s):  
Glutathione Reductase ◽  
Blood Cells ◽  
Normal Values ◽  
Reductase Activity ◽  
White Blood Cells ◽  
Human Blood Cells ◽  
Glutathione Reductase Activity ◽  
Fava Beans

A virtually complete absence of glutathione reductase activity was found in the erythrocytes of all three children (one male, two females) from a consanguineous marriage. Intermediate values were found in the erythrocytes of both parents. The enzyme activity could not be restored either by addition of FAD in vitro or by administration of riboflavin in vivo. The amount of reduced glutathione in the erythrocytes was normal in each case. Severely diminished glutathione stability during incubation with acetylphenylhydrazine was observed in the erythrocytes of the siblings, as well as intermediate stability in the parents' red cells. Clinically, this deficiency was manifested by hemolytic crises after eating fava beans in the eldest daughter (patient), and possibly by cataracts in her own and in her brother's eyes. Very low activities of glutathione reductase were also found in the leukocytes of this family: 13%-15% of normal values for the children and 64%-66% for the parents. Moreover, the same deficiency was found in the purified white blood cells of the propositus: 8% of normal values in the polymorphonuclear (PMN) cells, 4% in the lymphocytes, and 15% in the monocytes, together with 11% in the platelets. Finally, we found an abnormal oxygen consumption of the propositus' PMNs after phagocytosis of zymosan particles, suggesting that the glutathione reductase reaction was involved in the bactericidal capacity of these cells.

Changes in rat lens proteins and glutathione reductase activity with advancing age

2004 ◽  
Vol 74 (5) ◽  
pp. 329-333 ◽  
Author(s):  
Katakura ◽  
Kishida ◽  
Hirano
Keyword(s):  
Gene Expression ◽  
Glutathione Reductase ◽  
Total Protein ◽  
Flavin Adenine Dinucleotide ◽  
Reductase Activity ◽  
Water Soluble ◽  
Reductase Gene ◽  
Glutathione Reductase Activity ◽  
Old Rats

We examined the changes in the amounts of water-soluble and water-insoluble proteins of rat lenses, and in glutathione reductase activity and glutathione reductase gene expression, with advancing age. The lens total protein increased in 1-month-old rats, 3-month-old rats, and 6-month-old rats, but thereafter decreased in 12-month-old-rats. The water-soluble proteins decreased with advancing age, while the water-insoluble proteins increased. The glutathione reductase activity decreased with advancing age, but the decreased glutathione reductase activity almost recovered by addition of flavin adenine dinucleotide (FAD) in vitro. However, advancing age had no effect on the level of mRNA for glutathione reductase.

Evaluation of the In Vitro Interference of Bilirubin and Lipids in the Measurement of the Plasma Glutathione Reductase Activity

2014 ◽  
Vol 60 (08/2014) ◽  
Author(s):  
Carine Hermes ◽  
Taís Almeida ◽  
Bruna Hausen ◽  
Lara Cargnin ◽  
Etiane Tatsch ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Glutathione Reductase Activity ◽  
Plasma Glutathione

Effect of Polyamines on Glutathione Reductase Activity in Spinach

2008 ◽  
Vol 63 (3-4) ◽  
pp. 260-266
Author(s):  
Mustafa Erat ◽  
Lokman Ozturk ◽  
Leonardo M. Casano ◽  
Yavuz Demir
Keyword(s):  
Glutathione Reductase ◽  
Spinacia Oleracea ◽  
Reductase Activity ◽  
Reaction Medium ◽  
Direct Interaction ◽  
Sand Culture ◽  
Glutathione Reductase Activity ◽  
Spinach Leaves

The effects of polyamines (putrescine, spermidine and spermine) on glutathione reductase (glutathione: NADP+ oxidoreductase, EC 1.8.1.7; GR) activity of spinach leaves (Spinacia oleracea L. cv. Gladiator) were investigated under in vivo and in vitro conditions. Spinach was grown in sand culture under controlled conditions for 30 d. In in vivo assays 30-day-old plants were sprayed with polyamines once, and leaves were harvested 1, 5, 10 and 15 d after treatment. The three polyamines decreased the GR activity to different degrees, depending on time after application, type of compound and their concentration. In order to study whether or not polyamines can exert a direct effect on GR, the enzyme was partially purified from spinach leaves and incubated with polyamines in the reaction medium. Under these in vitro conditions, GR was inhibited by polyamines in a polyamine type- and concentrationdependent manner. Interestingly, spermine exerted the most intense inhibitory effect in both in vivo and in vitro experiments. It is proposed that the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme

scholarly journals Familial deficiency of glutathione reductase in human blood cells

Blood ◽  
1976 ◽  
Vol 48 (1) ◽  
pp. 53-62 ◽  
Author(s):  
H Loos ◽  
D Roos ◽  
R Weening ◽  
J Houwerzijl
Keyword(s):  
Glutathione Reductase ◽  
Blood Cells ◽  
Normal Values ◽  
Reductase Activity ◽  
White Blood Cells ◽  
Human Blood Cells ◽  
Glutathione Reductase Activity ◽  
Fava Beans

Abstract A virtually complete absence of glutathione reductase activity was found in the erythrocytes of all three children (one male, two females) from a consanguineous marriage. Intermediate values were found in the erythrocytes of both parents. The enzyme activity could not be restored either by addition of FAD in vitro or by administration of riboflavin in vivo. The amount of reduced glutathione in the erythrocytes was normal in each case. Severely diminished glutathione stability during incubation with acetylphenylhydrazine was observed in the erythrocytes of the siblings, as well as intermediate stability in the parents' red cells. Clinically, this deficiency was manifested by hemolytic crises after eating fava beans in the eldest daughter (patient), and possibly by cataracts in her own and in her brother's eyes. Very low activities of glutathione reductase were also found in the leukocytes of this family: 13%-15% of normal values for the children and 64%-66% for the parents. Moreover, the same deficiency was found in the purified white blood cells of the propositus: 8% of normal values in the polymorphonuclear (PMN) cells, 4% in the lymphocytes, and 15% in the monocytes, together with 11% in the platelets. Finally, we found an abnormal oxygen consumption of the propositus' PMNs after phagocytosis of zymosan particles, suggesting that the glutathione reductase reaction was involved in the bactericidal capacity of these cells.

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