scholarly journals The effects of selenium and copper deficiencies on glutathione S-transferase and glutathione peroxidase in rat liver

1987 ◽  
Vol 248 (2) ◽  
pp. 539-544 ◽  
Author(s):  
J R Arthur ◽  
P C Morrice ◽  
F Nicol ◽  
S E Beddows ◽  
R Boyd ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Similar Extent ◽  
Compensatory Response ◽  
Cu Deficiency ◽  
Hepatic Glutathione ◽  
Gshpx Activity ◽  
Se Deficiency ◽  
Gst Activity

Selenium (Se) deficiency in rats produced significant increases in the activity of hepatic glutathione S-transferase (GST) with 1-chloro-2,4-dinitrobenzene as substrate and in various GST isoenzymes when determined by radioimmunoassay. These changes is GST activity and concentration were associated with Se deficiency that was severe enough to provoke decreases of over 98% in hepatic Se-containing glutathione peroxidase activity (Se-GSHpx). However, decreases in hepatic Se-GSHpx of 60% induced by copper (Cu) deficiency had no effect on GST activity or concentration. Increased GST activity in Se deficiency has previously been postulated to be a compensatory response to loss of Se-GSHpx, since some GSTs have a non-Se-glutathione peroxidase (non-Se-GSHpx) activity. However, the GST isoenzymes determined in this study, GST Yb1Yb1, GST YcYc and GST YaYa, are known to have up to 30-fold differences in non-Se-GSHpx activity, but they were all significantly increased to a similar extent in the Se-deficient rats.

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.

The effect of dietary protein and sulfur amino acids on hepatic glutathione concentration and glutathione-dependent enzyme activities in the rat

1988 ◽  
Vol 66 (8) ◽  
pp. 1048-1052 ◽  
Author(s):  
P. F. Bauman ◽  
T. K. Smith ◽  
T. M. Bray
Keyword(s):  
Amino Acids ◽  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Dietary Protein ◽  
Transferase Activity ◽  
Sulfur Amino Acids ◽  
Glutathione S Transferase ◽  
Glutathione Concentration ◽  
Hepatic Glutathione ◽  
Protein Diets

Hepatic glutathione concentration and glutathione-dependent enzymes, glutathione S-transferase, glutathione peroxidase, and glutathione reductase, are important for protection against toxic compounds. Rats were fed diets containing 4, 7.5, 15, or 45% protein for 2 weeks. Glutathione and cysteine concentrations in rats fed the 4 and 7.5% protein diets were significantly lower (p < 0.05) than in rats fed the 15 and 45% protein diets. Glutathione S-transferase activity increased with increasing dietary protein. Glutathione peroxidase activity was significantly lower (p < 0.05) in rats fed 4 and 7.5% protein compared with rats fed 15 and 45% protein, whereas the activity of glutathione reductase was higher in rats fed 4 and 7.5% protein then in rats fed 15 or 45% protein. Dietary sulfur amino acids alone could account for the increase in glutathione concentration resulting from the increase in dietary protein from 7.5 to 15%. The limited availability of glutathione in animals fed the low protein diets could reduce the potential for detoxification of xenobiotics.

scholarly journals Toxicity of naphthalene in the Neotropical Fish Astyanax Lacustris (Characiformes: Characidae) and Geophagus Brasiliensis (Perciformes: Cichlidae)

2017 ◽  
Vol 17 (1) ◽  
pp. 7-22 ◽  
Author(s):  
Geonildo Rodrigo Disner ◽  
Sabrina Louise Moraes Calado ◽  
Helena Cristina Silva Assis ◽  
Marta Margarete Cestari
Keyword(s):  
Dna Damage ◽  
Comet Assay ◽  
Micronucleus Test ◽  
Glutathione S Transferase ◽  
Neotropical Fish ◽  
Compensatory Response ◽  
Low Concentrations ◽  
Geophagus Brasiliensis ◽  
Polycyclic Aromatic ◽  
Gst Activity

Polycyclic aromatic hydrocarbons are one of the most important organic pollutants in environmental studies. The aim of this study was to assess the naphthalene acute toxicity in two fish species, Astyanax lacustris (LLcust, 1875) and Geophagus brasiliensis (Quoy & Gaimard, 1824). The fish were exposed to naphthalene (0.005, 0.03, 0.3, and 3 mgL-1) in water and after that the piscine micronucleus test in erythrocytes, comet assay in blood, liver and gill cells, glutathione S–transferase (GST) activity in the liver, and accumulation of naphthalene in the bile were performed. The susceptibility of the two species was similar and naphthalene was not genotoxic in all tested tissues. The liver GST activity may have been responsible for less damage observed in the liver while the highest DNA damage occurred in blood cells. However, low concentrations of naphthalene in water can stimulate apparent benefits, such as less DNA damage, which would be a compensatory response to an imbalance of homeostasis. The naphthalene is absorbed and can accumulate in the gall bladder, a greater accumulation of PAH was observed in A. lacustris, while G. brasiliensis did not differ from the control. The naphthalene concentrations are not genotoxic to the tested species, although they can potentially accumulate into the body.Keywords: Comet assay. Ecotoxicology. Fish. Genotoxicity. Hormesis.

Glutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung

1988 ◽  
Vol 9 (9) ◽  
pp. 1617-1621 ◽  
Author(s):  
James Carmichael ◽  
Lesley M. Forrester ◽  
Alexander D. Lewis ◽  
John D. Hayes ◽  
Peter C. Hayes ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Human Lung ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

scholarly journals Effect of selenium deficiency on hepatic type I 5-iodothyronine deiodinase activity and hepatic thyroid hormone levels in the rat

1992 ◽  
Vol 282 (2) ◽  
pp. 483-486 ◽  
Author(s):  
G J Beckett ◽  
A Russell ◽  
F Nicol ◽  
P Sahu ◽  
C R Wolf ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Selenium Deficiency ◽  
Type I ◽  
Hepatic Enzymes ◽  
Glutathione S Transferase ◽  
Iodothyronine Deiodinase ◽  
Hepatic Glutathione ◽  
Liver Homogenates ◽  
Thyroid Hormone Levels ◽  
Gst Activity

Selenium deficiency in rats for a period of up to 6 weeks inhibited both the production of 3,3′, 5-tri-iodothyronine (T3) from thyroxine (T4) (5′-deiodination) and also the catabolism of T3 to 3,3′-di-iodothyronine (5-deiodination) in liver homogenates. The hepatic stores of T3 were decreased by only 8% in selenium deficiency, despite the T3 production rate from T4 being only 7% of the rate found in selenium-supplemented rats. Hepatic glutathione S-transferase (GST) activity was increased in both hypothyroidism and selenium deficiency, but apparently by different mechanisms, since mRNA expression for this family of enzymes was lowered by hypothyroidism and increased in selenium deficiency. It is concluded that, since both T3 production and catabolism are inhibited by selenium deficiency, there is little change in hepatic T3 stores, and therefore the changes in the activity of certain hepatic enzymes, such as GST, that are found in selenium deficiency are not the result of tissue hypothyroidism.

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