scholarly journals Redox regulation of antioxidant enzymes: post-translational modulation of catalase and glutathione peroxidase activity by resveratrol in diabetic rat liver

2014 ◽  
Vol 393 (1-2) ◽  
pp. 111-122 ◽  
Author(s):  
Gökhan Sadi ◽  
Davut Bozan ◽  
Huseyin Bekir Yildiz
Keyword(s):  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Redox Regulation ◽  
Diabetic Rat ◽  
Glutathione Peroxidase Activity

scholarly journals The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Cell Types ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Liver Parenchymal ◽  
Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

scholarly journals Experience of measuring glutathione peroxidase activity in surgically induced endometrial-like lesions in rats

2021 ◽  
Vol 70 (2) ◽  
pp. 55-61
Author(s):  
Aleksey V. Razygraev ◽  
Elena V. Baziyan ◽  
Lyudmila S. Polyanskikh ◽  
Mariya A. Petrosyan
Keyword(s):  
Hydrogen Peroxide ◽  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Rat Model ◽  
Peroxidase Activity ◽  
Specific Activity ◽  
Reduced Glutathione ◽  
Glutathione Peroxidase Activity ◽  
Nitrobenzoic Acid ◽  
Surgically Induced

BACKGROUND: Endometriosis is known to be linked with altered activities of antioxidant enzymes and with their gene polymorphisms. Progestins are known to induce glutathione peroxidase activity in the endometrium and promote reduction of endometrial lesions. It could be useful to estimate the correlation between the activity of glutathione peroxidase within endometrial lesions and their degree of reduction. AIM: The present study was aimed at estimating glutathione peroxidase activity in surgically induced endometrial-like lesions of different degree of reduction in rat model of endometriosis. MATERIALS AND METHODS: The method for determining glutathione peroxidase activity using hydrogen peroxide as a substrate and 5,5-dithiobis(2-nitrobenzoic acid) for estimation of residual reduced glutathione was applied for quantitative analysis of the enzyme activity in endometriotic foci, surgically induced in female Wistar rats. An assay of glutathione peroxidase activity in tissue homogenates was performed at 37C in a reaction medium containing Tris-HCl buffer supplemented with tetrasodium ethylenediaminetetraacetate and sodium azide (pH 8.5) in the presence of 0.55 mM reduced glutathione and 0.192 mM hydrogen peroxide. Before adding trichloroacetic acid, 40-second incubation was used. The correlation between the specific activity of the enzyme and protein amount in endometriotic foci was estimated. RESULTS: In a rat model of endometriosis, there was a high, well-determined glutathione peroxidase activity in endometriotic foci. For the same endometriotic tissue sample, the enzymatic activity was proportional to the amount of protein in the reaction mixture. The range of specific glutathione peroxidase activity was 2.436.45 micromoles of consumed glutathione per minute per milligram of protein (n = 7). In most reduced endometriotic foci (with the minimum amount of endometriotic tissue), the highest specific activity of glutathione peroxidase was found (the Spearmans rho of 0.93 with p = 0.0067). CONCLUSIONS: The method for determining glutathione peroxidase activity using hydrogen peroxide and 5,5-dithiobis(2-nitrobenzoic acid) is convenient for working with the endometriotic tissue in a rat model of endometriosis. We can accept, with p 0.01, that weight of endometriotic foci is negatively linked with specific glutathione peroxidase activity within their tissue. The results are analogous to the previously obtained data on catalase activity and suggest the involvement of both antioxidant enzymes in reduction of endometrial lesions.

Vitamin B6 Deficiency and Dietary Fats: Effects on Lipid Composition and Glutathione Peroxidase Activity in Rat Liver

2006 ◽  
Vol 50 (3) ◽  
pp. 305-312 ◽  
Author(s):  
Alessandra Bordoni ◽  
Luciana Cabrini ◽  
Mario Marchetti ◽  
Francesca Danesi ◽  
Davide Bochicchio ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Lipid Composition ◽  
Dietary Fats ◽  
Vitamin B ◽  
Glutathione Peroxidase Activity

scholarly journals Influence of zinc administration on its tissue concetration and activity of serum antioxidant enzymes in rats at physical activity

2015 ◽  
Vol 96 (5) ◽  
pp. 862-868
Author(s):  
A A Skal’nyy ◽  
A A Tin’kov ◽  
Yu S Medvedeva ◽  
I B Alchinova ◽  
E Yu Bonitenko ◽  
...  
Keyword(s):  
Physical Activity ◽  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
The Body ◽  
Laboratory Animals ◽  
Glutathione Peroxidase Activity ◽  
High Physical Activity ◽  
Dose Dependent Increase ◽  
Dose Dependent

Aim. To investigate the effect of zinc supplementation at physical exercise on the distribution of the metal in the tissues and the activity of serum antioxidant enzymes. Methods. Physical activity was simulated using the treadmill. Laboratory animals were distributed to 6 even (n=12) groups. The first and fourth groups of animals received no zinc-containing additives and were imposed to low and high physical activity, respectively. Animals of the 2 and 3 as well as 5 and 6 groups received 5 and 15 mg/kg/day of zinc asparaginate intragastrically and were imposed to low and high physical activity, respectively. The zinc concentrantion in the organs and tissues was determined by inductively coupled plasma mass spectrometry. The activity of antioxidant enzymes was determined by spectrophotometry. Results. Administration of zinc asparaginate to the laboratory animals with low physical activity resulted in a dose-dependent increase of the metal concentration in liver and kidney parenchyma and blood serum, as well as in increase of serum glutathione peroxidase activity. Intensive physical activity for 14 days was accompanied by a significant increase in serum and kidney tissue zinc level. At the 7-day exposure to zinc at physical activity, a dose-dependent increase in zinc concentration in the organs and increase of serum glutathione peroxidase activity was registered. Zinc administration together with physical activity for 14 days did not result in a significant change in the balance of metal in the body of animals. In contrast to the 7-day exposure, a combination of factors studied for 14 days was accompanied by increased activity of superoxide dismutase, but not glutathione peroxidase. Conclusion. Physical activity of different duration has a significant effect on the zinc kinetics at oral administration, and the activity of serum antioxidant enzymes in laboratory animals.

scholarly journals The nature of the sex-linked differences in glutathione peroxidase activity and aerobic oxidation of glutathione in male and female rat liver

1969 ◽  
Vol 115 (3) ◽  
pp. 449-456 ◽  
Author(s):  
R E Pinto ◽  
W Bartley
Keyword(s):  
Lipid Peroxidation ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Aerobic Oxidation ◽  
Female Rats ◽  
Ovariectomized Rats ◽  
Female Rat ◽  
Glutathione Peroxidase Activity ◽  
Peroxide Formation

1. Glutathione peroxidase activity in the livers of sham-operated female rats was about 60% higher than in similarly treated male rats. The value in the ovariectomized female was about the same as that in the castrated or sham-operated male. 2. Glutathione peroxidase activity changed during the oestrous cycle. The highest value was in oestrus, and was about 50% higher than the lowest activity, which was found in dioestrus. The activity in proestrus and in metoestrus was respectively about 20 and 30% higher than in dioestrus. 3. In the pregnant female 1 or 2 days before term, glutathione peroxidase activity was about 20% higher than that in the female in oestrus. 4. Subcutaneous implants of both oestra-diol and progesterone in the gonadectomized rats increased the glutathione peroxidase activity approximately to the values found in the female at oestrus. 5. The rate of aerobic oxidation of GSH in the female rat liver was about 80% higher than in the male and about 110% higher than in the gonadectomized rats. Treatment of gonadectomized rats with subcutaneous implants of oestradiol and of progesterone increased the rate of oxidation of GSH by about 100%. 6. In the presence of azide the rate of GSH oxidation in the male and in the female was respectively about 3·5- and 2·1-fold that in the absence of azide. In castrated or ovariectomized rats the increase due to the presence of azide was about 2·4-fold. In the gonadectomized rats treated with oestradiol or progesterone the rate of GSH oxidation in the presence of azide was about 2·2-fold that in its absence. 7. The rate of lipid peroxidation in female was 15–30-fold that in male or in gonadectomized rats. Treatment of the gonadectomized rats with oestradiol or with progesterone increased the rate of lipid peroxidation up to values that were even higher than in the female. In the presence of GSH the formation of malonaldehyde from peroxides was virtually eliminated. 8. The results suggest that the sex-linked differences in glutathione peroxidase activity, in the rate of GSH oxidation and in the rate of lipid peroxidation are due to the female sex hormones. 9. It is suggested that both the catalase activity and the rate of hydrogen peroxide formation are higher in the male than in the female. 10. Sex-linked changes in glutathione peroxidase, in the rate of GSH oxidation and in the rate of lipid peroxide formation are discussed in relation to the metabolism of oestrogens in the liver and also to the possible nature of those sex-linked changes.

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