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Journal ArticleDOI

Influence of selenium on glutathione and some associated enzymes in rats with mammary tumor induced by 7,12-Dimethylbenz(a)anthracene

TLDR
Observations clearly demonstrate the influence of dietary selenium supplementation in correcting abnormal changes in glutathione turnover and some associated enzymes in tumor induced rats.
Abstract
A recent finding in epidemiological and laboratory studies suggests that the ratio of selenium to glutathione is lower in breast cancer subjects than its control counterparts. Selenium, an antioxidant and anticarcinogen, can modify the status of glutathione and some associated enzymes by blocking peroxidation of lipids in membranes of cancer subjects. Studies were conducted using female albino rats of Wistar strain bearing mammary tumor induced by 7,12-dimethylbenz(a) anthracene to assess the biological role of selenium on some antioxidant enzymes associated with the maintenance of glutathione status. For induction of mammary tumor, 25 mg DMBA in a 1 ml emulsion of sunflower oil and physiological saline was injected subcutaneously to each rat. One group in each of control and tumor bearing rats, were fed 5 mg sodium selenite/kg diet from the day of tumor induction for 24 weeks. Increase in the reduced glutathione concentration was preceded by significant increase in the oxidized glutathione as well as in the activities of γ-glutamylcysteine synthetase, glutathione peroxidase, glutathione reductase, glutathione S-transferase, and glucose-6-phosphate dehydrogenase by selenium administration in rats bearing tumor. However, selenium administration to rats bearing tumor decreased the activity of γ-glutamyl transpeptidase. These observations clearly demonstrate the influence of dietary selenium supplementation in correcting abnormal changes in glutathione turnover and some associated enzymes in tumor induced rats.

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Citations
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Journal ArticleDOI

Biologic and pharmacologic regulation of mammalian glutathione synthesis.

TL;DR: Because GSH plays a critical role in cellular defenses against electrophiles, oxidative stress and nitrosating species, pharmacologic manipulation of GSH synthesis has received much attention.
Journal ArticleDOI

Estrogen receptor-mediated regulation of oxidative stress and DNA damage in breast cancer

TL;DR: This is the first report indicating that E2 is capable of inducing an increase in sensitivity to oxidative DNA damage through an ER-mediated mechanism, and may explain some of the estrogen-induced pro-oxidant effects previously reported in vivo.

Toxicological profile for selenium

J. Risher
TL;DR: This edition supersedes any previously released draft or final profile for selenium and is a unique compilation of toxicological information on a given hazardous substance.
Journal ArticleDOI

Aryl hydrocarbon receptor/cytochrome P450 1A1 pathway mediates breast cancer stem cells expansion through PTEN inhibition and β-Catenin and Akt activation.

TL;DR: The present study provides the first evidence that AhR/CYP1A1 signaling pathway is controlling breast CSCs proliferation, development, self-renewal and chemoresistance through inhibition of the PTEN and activation of β-Catenin and Akt pathways.
References
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Journal ArticleDOI

The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA.

TL;DR: This article reported the identification of a genomic recombinant as encoding the entire mouse Gutathione peroxidase (GSHPx) gene, which is an important selenium-containing enzyme which protects cells from peroxide damage and also has a role in leukotriene formation.

Thestructure ofthemouse glutathione peroxidase gene:the selenocysteine intheactive site isencoded bythe'termination' codon, TGA

TL;DR: The identification of a genomic recombinant as encoding the entire mouse GSHPx gene is reported, and the selenocysteine in the active site of the enzyme is encoded by TGA.
Journal ArticleDOI

Interaction of γ-Glutamyl Transpeptidase with Amino Acids, Dipeptides, and Derivatives and Analogs of Glutathione

TL;DR: In this article, a rat kidney γ-glutamyl transpeptidase was examined with respect to its γglutamide donor and acceptor specificities.
Journal ArticleDOI

On the reaction mechanism of yeast glutathione reductase.

TL;DR: Some studies with glutathione reductase are reported which indicate that this enzyme does in fact possess a basically identical reaction mechanism to that of lipoyl dehydrogenase.
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