Relationship among standard semen parameters, glutathione peroxidase/glutathione reductase activity, and mRNA expression and reduced glutathione content in ejaculated spermatozoa from fertile and infertile men

2004 ◽  
Vol 82 ◽  
pp. 1059-1066 ◽  
Author(s):  
Nicolás Garrido ◽  
Marcos Meseguer ◽  
Juan Alvarez ◽  
Carlos Simón ◽  
Antonio Pellicer ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Mrna Expression ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Semen Parameters ◽  
Infertile Men ◽  
Glutathione Reductase Activity

scholarly journals Activity of glutathione-dependent enzymes in spermatozoa in patients with pathospermia

2017 ◽  
Author(s):  
O. K. Onufrovych ◽  
R. V. Fafula ◽  
Io. A. Nakonechnyi ◽  
D. Z. Vorobets ◽  
U. P. Iefremova ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Antioxidant System ◽  
Reductase Activity ◽  
Sperm Cells ◽  
Compensatory Mechanisms ◽  
Glutathione Antioxidant System ◽  
Healthy Men ◽  
Infertile Men ◽  
Glutathione Reductase Activity

The results of glutathione peroxidase and glutathione reductase activity in spermatozoa of patients with different forms pathospermia are presented in the paper. It was shown that glutathione peroxidase and glutathione reductase activity in sperm cells of patients is reduced in comparison with healthy men with preserved fertility. However, the most expressed changes in the activity of glutathione peroxidase and glutathione reductase are in spermatozoa of infertile men with associated forms patospermia and leucospermia. These changes indicate exhaustion of compensatory mechanisms of glutathione antioxidant system in the sperm cells of infertile men with pahospermia.

scholarly journals Influence of mouse age and erythrocyte age on glutathione metabolism

1978 ◽  
Vol 174 (3) ◽  
pp. 819-825 ◽  
Author(s):  
E C Abraham ◽  
J F Taylor ◽  
C A Lang
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Specific Radioactivity ◽  
Phthalate Ester ◽  
Pulse Labelling ◽  
Very Old ◽  
Free Thiol ◽  
Glutathione Reductase Activity

In order to determine whether the biological age of a mouse influences erythrocyte metabolism and erythrocyte aging in vivo, blood samples were collected from male C57/BL6J mice of different biological ages ranging from mature (10 months) to “very old” (37 months). In the very old mouse, compared with the mature mouse, the erythrocyte survival time was decreased, erythrocyte densities were increased, the concentrations of total free thiol and reduced glutathione, and glutathione reductase activity were decreased. Erythrocytes were separated into different density (age) groups by phthalate ester two-phase centrifugation or by albumin density-gradient centrifugation. The density-age relationship of erythrocytes was established by pulse-labelling with 59Fe in vivo and by subsequent determinations of specific radioactivity of erythrocyte fractions of different densities prepared during a chase period of 60 days. The age of erythrocytes in mice of all ages was directly related to density. Also, in older erythrocytes compared with younger erythrocytes, decreased concentrations of total free thiol and reduced glutathione, and decreased glutathione reductase activity were observed. These were the lowest in the old erythrocytes of very old mice. These results in aging erythrocytes from aging mice suggest that the glutathione status the erythrocyte may be an index of aging, not only of the cell but also of the organism.

THE AMPEROMETRIC DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN HUMAN ERYTHROCYTES

1955 ◽  
Vol 33 (3) ◽  
pp. 404-407 ◽  
Author(s):  
H. Bruce Collier ◽  
Sheila C. McRae
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Human Erythrocytes ◽  
Amperometric Titration ◽  
Amperometric Determination ◽  
Marked Inhibition ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.

The Oxidation of Glutathione by Serum

1964 ◽  
Vol 10 (1) ◽  
pp. 53-61
Author(s):  
Hugo R Rony ◽  
Michael West ◽  
Hyman J Zimmerman
Keyword(s):  
Cytochrome C ◽  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Glutathione Reductase Activity

Abstract Studies of serum glutathione reductase activity in this laboratory prompted an attempt to demonstrate glutathione oxidase in the serum. The oxidation of reduced glutathione in the sera of patients with various diseases does not differ from normal sera. Preheating the serum and addition of cytochrome c does not effect the oxidizing capacity of the serum. The ability of serum to oxidize reduced glutathione appears to represent autoxidation, not the effect of an oxidizing enzyme.

Analysis of Glutathione-Dependent Enzyme Activities in two Different Rat Hepatomas and in Normal Liver in Relation to their Role in Resistance to Oxidative Stress

1988 ◽  
Vol 74 (6) ◽  
pp. 617-621 ◽  
Author(s):  
Maria Armida Rossi ◽  
Mario Umberto Dianzani
Keyword(s):  
Oxidative Stress ◽  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Reductase Activity ◽  
Antioxidant Properties ◽  
Liver Microsomes ◽  
Normal Liver ◽  
Lipid Hydroperoxides ◽  
Glutathione S Transferases ◽  
Glutathione Reductase Activity

The importance of some glutathione metabolic pathways was examined in two highly dedifferentiated hepatomas, Yoshida AH-130 and Morris 3924 A hepatomas, and in normal liver in relation to their role against oxidative stress. The cytosol prepared from Yoshida hepatoma cells decreased the peroxidation rate in normal liver microsomes and mitochondria, but this antioxidant property was not displayed by Morris hepatoma. Glutathione peroxidase and glutathione-S-transferases activities were extremely low in both hepatomas; glutathione reductase activity values were about half the normal liver values. The large decrease in glutathione peroxidase and glutathione-S-transferases suggests that in these two tumors only small amounts of GSH can be used in reduction or conjugation reactions, such as the reduction of hydrogen peroxide and lipid hydroperoxides or the conjugation of GSH with the end products of lipoperoxidation, aldehydes or ketones. The hypothesis of a more efficient GSSG reduction in hepatomas, due to the low glutathione peroxidase/glutathione reductase activity ratio, is also discussed. The described changes in glutathione related enzymes do not seem to have any correlation with the protective effect against the lipoperoxidative processes displayed by some tumors since these enzymatic activities were similar in both hepatomas whereas only Yoshida hepatoma showed antioxidant properties.

THE AMPEROMETRIC DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN HUMAN ERYTHROCYTES

1955 ◽  
Vol 33 (1) ◽  
pp. 404-407 ◽  
Author(s):  
H. Bruce Collier ◽  
Sheila C. McRae
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Human Erythrocytes ◽  
Amperometric Titration ◽  
Amperometric Determination ◽  
Marked Inhibition ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.

scholarly journals АНТИОКСИДАНТНИЙ ЗАХИСТ ТА ПЕРОКИСНЕ ОКИСНЕННЯ ЛІПІДІВ ОРГАНІЗМУ ВИСОКОТІЛЬНИХ КОРІВ ПРИ ПРОФІЛАКТИЦІ САЛЬМОНЕЛЬОЗУ ЗА ВПЛИВУ НАНОПРЕПАРАТУ ГЕРМАКАПУ

2016 ◽  
Vol 18 (2(66)) ◽  
pp. 112-116
Author(s):  
P.Y. Lavriv
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Antioxidant Defense ◽  
Reductase Activity ◽  
Lipid Body ◽  
Antioxidant Defense System ◽  
Glutathione System ◽  
Defense System ◽  
Glutathione Reductase Activity ◽  
Radical Processes

The article  deals with the results of experimental research data of relationship between the antioxidant defense system and lipid body peroxidation of high calves cows  under  the influence of nanpreparation Germakap conducted  with simultaneous vaccination with inactivated formol vaccination with repeated  in two weeks later  at the same doses as their  stability and immunity to Salmonella. It was found the likely increase in activity of glutathione peroxidase and glutathione reductase and at the same time, reduction of malon dialdehyde and hydroperoxides lipids and superoxidimutase. These changes in animals  body occur due to complex components adaptive nan preparation Germakap that lead to the normalization of metabolic and free radical processes in animals.  However, the increase in the catalytic activity of glutathione peroxidase and glutathione reductase activity in plasma of high calves cows  from research group can be explained by increasing intensity of synthesis in which these enzymes by introducing nan preparation Germakap closely associated with the regeneration of glutathione in the cell, and also the activity of glutathione peroxidase.  Through interaction with restoration of glutathione and glutathione peroxidase, glutathione reductase it was formed glutathione system that protects cells from stress peroxidation

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