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Loss of activity of the selenoenzyme thioredoxin reductase causes induction of hepatic heme oxygenase-1.
Mostert V, Hill KE, Burk RF
(2003) FEBS Lett 541: 85-8
MeSH Terms: Animals, Aurothioglucose, Dinitrochlorobenzene, Enzyme Inhibitors, Heme Oxygenase (Decyclizing), Heme Oxygenase-1, Liver, Male, Membrane Proteins, Mice, Mice, Inbred C57BL, Proteins, Selenium, Selenoprotein P, Selenoproteins, Thioredoxin-Disulfide Reductase, Tumor Cells, Cultured
Show Abstract · Added March 5, 2014
The stress response enzyme heme oxygenase (HO)-1 is induced in livers of selenium-deficient rodents, probably to compensate for loss of certain selenoproteins. We sought to identify those selenoproteins. Selenium-replete mice with genetic deletion of selenoprotein P or glutathione peroxidase-1 did not have elevated hepatic HO activity, thus ruling out involvement of those selenoproteins in HO-1 induction by selenium deficiency. However, inhibition of thioredoxin reductase (TrxR) by a low dose of gold in the form of aurothioglucose led to induction of hepatic HO activity. Moreover, further induction by phenobarbital was observed. This HO-1 induction pattern is also seen in selenium-deficient mice. In the rat hepatoma cell line H4IIE, inhibition of TrxR by aurothioglucose or by 1-chloro-2,4-dinitrobenzene led to induction of HO-1. We conclude that loss of TrxR is responsible for the induction of HO-1 by selenium deficiency.
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1 Members
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17 MeSH Terms
Reduction of the ascorbyl free radical to ascorbate by thioredoxin reductase.
May JM, Cobb CE, Mendiratta S, Hill KE, Burk RF
(1998) J Biol Chem 273: 23039-45
MeSH Terms: Animals, Aurothioglucose, Cystine, Cytosol, Dehydroascorbic Acid, Electron Spin Resonance Spectroscopy, Free Radicals, Liver, Metalloproteins, Microsomes, Liver, NADP, Organoselenium Compounds, Oxidation-Reduction, Rats, Selenium, Thioredoxin-Disulfide Reductase
Show Abstract · Added December 10, 2013
Recycling of ascorbic acid from its oxidized forms is required to maintain intracellular stores of the vitamin in most cells. Since the ubiquitous selenoenzyme thioredoxin reductase can recycle dehydroascorbic acid to ascorbate, we investigated the possibility that the enzyme can also reduce the one-electron-oxidized ascorbyl free radical to ascorbate. Purified rat liver thioredoxin reductase catalyzed the disappearance of NADPH in the presence of low micromolar concentrations of the ascorbyl free radical that were generated from ascorbate by ascorbate oxidase, and this effect was markedly stimulated by selenocystine. Dehydroascorbic acid is generated by dismutation of the ascorbyl free radical, and thioredoxin reductase can reduce dehydroascorbic acid to ascorbate. However, control studies showed that the amounts of dehydroascorbic acid generated under the assay conditions used were too low to account for the observed loss of NADPH. Electron paramagnetic resonance spectroscopy directly confirmed that the reductase decreased steady-state ascorbyl free radical concentrations, as expected if thioredoxin reductase reduces the ascorbyl free radical. Dialyzed cytosol from rat liver homogenates also catalyzed NADPH-dependent reduction of the ascorbyl free radical. Specificity for thioredoxin reductase was indicated by loss of activity in dialyzed cytosol prepared from livers of selenium-deficient rats, by inhibition with aurothioglucose at concentrations selective for thioredoxin reductase, and by stimulation with selenocystine. Microsomal fractions prepared from rat liver showed substantial NADH-dependent ascorbyl free radical reduction that was not sensitive to selenium depletion. These results suggest that thioredoxin reductase can function as a cytosolic ascorbyl free radical reductase that may complement cellular ascorbate recycling by membrane-bound NADH-dependent reductases.
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16 MeSH Terms
Enzyme-dependent ascorbate recycling in human erythrocytes: role of thioredoxin reductase.
Mendiratta S, Qu ZC, May JM
(1998) Free Radic Biol Med 25: 221-8
MeSH Terms: Arsenicals, Ascorbic Acid, Aurothioglucose, Cell Membrane, Cell-Free System, Dehydroascorbic Acid, Dinitrochlorobenzene, Dose-Response Relationship, Drug, Enzymes, Erythrocytes, Ferricyanides, Glutathione, Glutathione Transferase, Hemolysis, Humans, Ketones, NADP, Thioredoxin-Disulfide Reductase, Vitamin E
Show Abstract · Added December 10, 2013
Human erythrocytes efficiently reduce dehydroascorbic acid (DHA) to ascorbate, which helps to maintain the ascorbate content of blood. Whereas erythrocyte DHA reduction is thought to occur primarily through a direct chemical reaction with GSH, this work addresses the role of enzyme-mediated DHA reduction by these cells. The ability of intact erythrocytes to recycle DHA to ascorbate, estimated as DHA-dependent ferricyanide reduction, was decreased in parallel with GSH depletion by glutathione-S-transferase substrates. In contrast, the sulfhydryl reagent phenylarsine oxide inhibited DHA reduction to a much greater extent than it decreased GSH in intact cells. DHA reduction in excess of that due to a direct chemical reaction with GSH was also observed in freshly prepared hemolysates. Hemolysates likewise showed NADPH-dependent reduction of DHA that appeared due to thioredoxin reductase, because this activity was inhibited 68% by 10 microM aurothioglucose, doubled by 5 microM E. coli thioredoxin, and had an apparent Km for DHA (1.5 mM) similar to that of purified thioredoxin reductase. Additionally, aurothioglucose-sensitive, NADPH-dependent DHA reductase activity was decreased 80% in hemolysates prepared from phenylarsine oxide-treated cells. GSH-dependent DHA reduction in hemolysates was more than 10-fold that of NADPH-dependent reduction. Nonetheless, the ability of phenylarsine oxide to decrease DHA reduction in intact cells with little effect on GSH suggests that enzymes, such as thioredoxin reductase, may contribute more to this activity than previously considered.
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1 Members
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19 MeSH Terms
Determination of thioredoxin reductase activity in rat liver supernatant.
Hill KE, McCollum GW, Burk RF
(1997) Anal Biochem 253: 123-5
MeSH Terms: Animals, Aurothioglucose, Cytosol, Dithionitrobenzoic Acid, Indicators and Reagents, Kinetics, Liver, Oxidation-Reduction, Rats, Reference Values, Reproducibility of Results, Selenium, Sensitivity and Specificity, Spectrophotometry, Thioredoxin-Disulfide Reductase
Added March 5, 2014
0 Communities
1 Members
0 Resources
15 MeSH Terms
Thioredoxin reductase activity is decreased by selenium deficiency.
Hill KE, McCollum GW, Boeglin ME, Burk RF
(1997) Biochem Biophys Res Commun 234: 293-5
MeSH Terms: Animals, Aurothioglucose, Brain, Diet, Enzyme Inhibitors, Glutathione Peroxidase, In Vitro Techniques, Kidney, Liver, Male, Nutritional Status, Proteins, Rats, Rats, Sprague-Dawley, Selenium, Selenoprotein P, Selenoproteins, Thioredoxin-Disulfide Reductase
Show Abstract · Added March 5, 2014
Animal thioredoxin reductase is a selenoprotein. In this study, thioredoxin reductase activities in liver, kidney, and brain have been compared in rats fed selenium-deficient and control diets for 14 weeks following weaning. Selenium deficiency caused a decrease in thioredoxin reductase activity from control to 4.5% in liver and 11% in kidney. However, brain thioredoxin reductase activity was not affected by selenium deficiency of this severity. Gold inhibited thioredoxin reductase activity in the liver in a manner typical of its effect on selenoenzymes. Repletion of selenium-deficient rats with injections of selenium caused thioredoxin reductase activity to increase more rapidly in the liver than glutathione peroxidase activity but more slowly than selenoprotein P. These results indicate that thioredoxin reductase activity in liver and kidney is sensitive to selenium nutritional status but that brain thioredoxin reductase activity is less sensitive.
0 Communities
1 Members
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18 MeSH Terms
Gold pulmonary toxicity in a patient with a normal chest radiograph.
Blackwell TS, Gossage JR
(1995) South Med J 88: 644-6
MeSH Terms: Adult, Aurothioglucose, Drug Hypersensitivity, Humans, Lung, Lung Diseases, Interstitial, Male, Radiography, Still's Disease, Adult-Onset
Show Abstract · Added March 5, 2014
We report a case of gold pulmonary toxicity in a patient with adult-onset Still's disease with dyspnea on exertion and a normal chest radiograph. Withdrawal of gold therapy resulted in complete resolution of pulmonary toxicity in our patient without the need for additional steroid therapy.
1 Communities
1 Members
0 Resources
9 MeSH Terms