Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Selenium Oxides”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 433 records · Page 24Linked to original sources
PubMed2002

Effect of supranutritional level of dietary alpha-tocopheryl acetate and selenium on rabbit semen.

This research examined the effects of dietary alpha-tocopheryl acetate (50 or 200 mg/kg diet) and selenium (Se, 0 or 0.5 ppm) supplementation on motion characteristics, oxidative stability and fertilizing ability of rabbit spermatozoa, fresh and stored for 24 h at 5 degrees C. The higher amount of dietary alpha-tocopheryl acetate increased the level of Vitamin E in the fresh semen (1.75 mmol/l versus 0.95 mmol/l) and its oxidative stability (thiobarbituric acid reactive substances-TBARS 12.44 nmol malondialdehyde/10(8) sperm versus 21.4 nmol malondialdehyde/10(8) sperm). Dietary Se increased gluthatione peroxidase activity (GPx) in erythrocytes (285 U/g Hb versus 207 U/g Hb), seminal plasma (270 U/l versus 190 U/l) and spermatozoa (1338 mU/10(9) sperm versus 1103 mU/10(9) sperm), whereas it did not show any effect on alpha-tocopherol level and TBARS. No synergy between Vitamin E and Se was shown. Storage for 24 h at 5 degrees C increased the TBARS level in all the experimental groups. Neither live and acrosome reacted spermatozoa, nor kinetic parameters, nor fertility rate were modified by dietary supplementation.

Animal Nutritional Physiological Phenomena↗
PubMed2005

The role of selenium, zinc and antioxidant vitamin supplementation in the treatment of bronchial asthma: adjuvant therapy or not?

In the last few years, nutrition has represented an important conditioning factor of many cardiovascular, gastrointestinal and pulmonary chronic diseases. Many published works have documented specific inflammatory abnormalities in the airways of subjects with mild-to-moderate persistent bronchial asthma in which the inflammation state is often associated with an increased generation of reactive oxygen species and free radical-mediated reactions. This evidence has stimulated many researchers to suppose that the oxidative stress could be an important pathogenetic determining factor in the progression of chronic diseases, and the decrease of oxidant insults to the lung can be modified with antioxidant supplementary therapy. There are many studies regarding dietary interventions that confirm the relationship to oxidative stress, bronchial inflammation, the development of asthmatic symptoms and the lowered cellular reducing capacity. Simple dietary and environmental supplementations significantly reduce the oxidant stress, minimise the development of asthmatic symptoms, and should prove to be an effective new approach to asthma management in addition to current pharmacological strategies. Many randomised controlled trials with antioxidant vitamins and trace element supplements have not confirmed the results shown in other clinical trials. The aim of this review is to focus the attention on published works discussing the relationship between asthma and nutritional supplements (some trace elements and vitamins) and the effectiveness of these supplements in the treatment of bronchial asthma.

Adjuvants, Immunologic↗
PubMed2006

Oxidative stress on domestic ducks (Shaoxing duck) chronically exposed in a Mercury-Selenium coexisting mining area in China.

The Wanshan mercury mine is the largest mercury deposit in Guizhou Province, China. Few attempts have been made to study the toxic effects of mercury on biota in this mining area. This study was the first to investigate the oxidative stress on domestic ducks (Shaoxing duck) chronically exposed to mercury in the Wanshan mining area. Chemical analyses revealed higher concentrations of both, mercury and selenium in samples from the Wanshan area. Total mercury and selenium concentrations in duck tissues varied from 0.073 to 4.465 mg/kg and from 1.073 to 6.35 mg/kg, respectively. Analysis of covariance revealed that there were significant effects of zone on accumulation of mercury and selenium in all duck tissues (P<0.01). Moreover, analysis of covariance indicated that mercury content significantly affected the accumulation of selenium in duck muscle, brain, and liver (P<0.01). Mercury and selenium were also highly correlated in Wanshan duck liver, muscle, brain, and lung. The statistical analysis suggested that selenium might be an interactive factor in mercury toxicity. As for the biochemical analyses, it was observed that selenium-dependent glutathione peroxidase and superoxide dismutase activities and glutathione (GSH) content were significantly increased in the livers and brains of Wanshan ducks (P<0.01, 0.05). However, no significant changes were observed in malondialdehyde content (P>0.05). Although the results indicated that adaptive responses of the redox-defense system are associated with the increased enzyme activities and GSH content, the most likely explanation is that selenium plays a critical role. Therefore, the effects of the interaction environmentally occurring selenium and mercury on public health in the Wanshan area should be examined in further studies.

Animals↗
PubMed2006

Genotoxic effects in C57Bl/6J mice chronically exposed to arsenate in drinking water and modulation of the effects by low-selenium diet.

In C57Bl/6J mice chronically exposed to arsenate in drinking water at 50, 200, or 500 microg As/L, genotoxic effects in bone-marrow cells using micronucleus test and in peripheral blood leukocytes using the comet assay were determined after 3, 6 or 12 mo. To assess the modulating role of selenium in development of the effects, the animals were fed a specially prepared low-selenium diet and were supplemented with sodium selenite (200 microg Se/L) in drinking water (supplemented groups) or were without Se supplementation (nonsupplemented groups). Measurements of glutathione peroxidase activity in erythrocytes and plasma as well as selenium concentration in plasma were performed after 3, 6, and 12 mo and showed a marked decrease in values in animals in non-Se supplemented compared to Se-supplemented groups. After 3 mo of arsenic exposure in the Se-supplemented animals the level of DNA fragmentation (without Endo III and Fpg enzymes) did not differ from the control; however, increased oxidative damage of purine and pyrimidine bases was observed. In groups not supplemented with Se, an increase of DNA fragmentation was observed; however, the levels of oxidative DNA damage in these groups did not differ from the control. None of the positive effects observed in the comet assay after 3 mo was related to arsenate concentration. The levels of DNA damage after 6 and 12 mo of exposure to arsenic as well as the frequency of micronuclei after 3, 6, and 12 mo did not differ significantly between exposed and control animals, irrespective of Se supplementation status.

Administration, Oral↗
PubMed2003

[Effect of selenium enriched diet on lipid peroxidation in patients with diabetes mellitus type 2].

It was investigated the influence of a diet supplemented with selenium on the clinicometabolic parameters and the activity of lipid peroxidation in 43 patients with Type 2 diabetes mellitus. It was indicated that under the influence of dietotherapy besides the decrease of glucose levels in capillary and venous blood, improvement of parameters of lipid metabolism, a reduction of malondialdehyde level and tendency to increase of glutathione peroxidase activity were observed. The results of investigations testify about sufficiently expressed efficacy of a diet supplemented with selenium in correction of oxidative stress and clinicometabolic parameters in this contingent of patients.

Adult↗
PubMed1984

Effect of dietary selenium on the metabolism of aflatoxin B1 in turkeys.

To investigate the biochemical mechanism of the previously reported protective effect of dietary selenium against aflatoxin toxicity, the hepatic metabolism of aflatoxin B1 in turkey poults was examined at various dietary selenium concentrations. Diets were supplemented with 0.2, 2.0 or 4.0 ppm selenium (as sodium selenite) and 500 ng aflatoxin B1/g diet in an 18-day trial. Free and conjugated aflatoxin and metabolites were quantified using high-performance liquid chromatography. The proportion of liver aflatoxins in conjugated forms increased and the ratio of free aflatoxin B1/M1 decreased with increasing dietary selenium concentrations. These in vivo results provide evidence of selenium-induced enhancement of aflatoxin detoxification processes. In a similar experiment using 2.0 ppm selenium and 750 ng aflatoxin B1/g diet, the concentration of hepatic reduced glutathione, cytochrome P-450 and the activity of enzymes involved in the metabolism of aflatoxin B1 and glutathione were determined. Although the selenium supplement increased glutathione peroxidase activity, dietary selenium had no effect on reduced glutathione or cytochrome P-450 concentrations or on the activities of glutathione transferase E, glucuronyl transferase and cytochrome c reductase. These data indicate that the protective action of selenium is not mediated by an increase in glutathione availability for aflatoxin conjugation or by effects on the activities of these enzymes as measured in vitro.

Aflatoxin B1↗
PubMed2000

Selenium, the element of the moon, in life on earth.

The present status of selenium biochemistry is reviewed with particular emphasis on biomedical problems related to the selenium status of humans and experimental animals. Historical milestones of selenium biochemistry starting from the identification of the first selenoenzymes up to the elucidation of prokaryotic and eukaryotic selenoprotein biosynthesis are compiled. Topical hypotheses on the biological role of selenium in general and of individual selenoproteins in respect to antioxidant defense, redox regulation of metabolic processes, thyroid function, spermatogenesis, oncogenesis, and atherogenesis are critically evaluated.

Animals↗
PubMed1995

Redox-active chalcogen-containing glutathione peroxidase mimetics and antioxidants inhibit tumour promoter-induced downregulation of gap junctional intercellular communication between WB-F344 liver epithelial cells.

Evidence is mounting supporting a role for oxidative stress in the mechanism of tumour promotion in response to agents such as 12-O-tetradecanoylphorbol-13-acetate (TPA). In this paper we demonstrate that glutathione peroxidase-mimetic xenobiotics, ebselen, ebselen-glutathione, alpha-(phenylselenenyl) acetophenone and bis-(4-aminophenyl) telluride (at concentrations between 10 microM and 50 microM) all demonstrate protective effects on TPA-induced downregulation of gap-junctional intercellular communication (GJIC) between WB-F344 rat liver epithelial cells. These effects were, in each case, diminished if the cells were depleted of their intracellular glutathione, and potentiated if glutathione was supplemented into the incubations. Additionally, bis-(4-aminophenyl) selenide and several N-substituted analogues, possessing potent antioxidant activity but being devoid of GSH peroxidase-mimetic activity, demonstrated remedial activity against TPA-induced downregulation of GJIC. Structure-activity relationships between these molecules showed a strong correlation to the oxidation potential of the selenium atom in the compound as the bis-(4-nitrophenyl)- and bis-(4-cyanophenyl)- derivatives, which possess poor antioxidant capacity and a half-wave redox potential well above +1.0 V, did not affect TPA-induced effects on GJIC. Examination of the mechanism of action of these redox-active compounds demonstrated correlations between their abilities to (i) prevent TPA-induced downregulation of GJIC, (ii) abolish the accumulation of intracellular oxidants and (iii) prevent the hyper-phosphorylation and internalization of connexin 43 in the cells. The active compounds were also able to prevent the rapid, TPA-induced translocation of protein kinase C to the particulate fraction of the cells, without affecting phorbol ester binding. These data support a synergistic role for oxidants and other TPA-dependent responses within the cell in mediating the downregulation of GJIC. Such oxidative metabolism may play a role in the control of translocation of protein kinase C from the cytosol to membranes in response to TPA within these cells. Despite the nature of the in vitro test system studied, the data also clarify the molecular basis for a potential anti-tumour promotive effect of antioxidants, based on established redox chemistries of several series of structurally-related molecules.

Animals↗
PubMed2002

[Microbial reduction of iron, manganese as well as other metals and their individual significance in environmental bioremediation].

In this paper, microbial reduction of iron, manganese and other metals in soils and waters were discussed. Microorganisms reducing to different metals such as iron, manganese and uranium as well as selenium and their enzymatic and non-enzymatic mechanisms for reducing to different metals were summarized. Moreover, the significance of reduction of different microorganisms of metals in the bioremediation of metals-contaminated environment was also evaluated.

Biodegradation, Environmental↗
PubMed2001

ESR studies on reaction of saccharide with the free radicals generated from the xanthine oxidase/hypoxanthine system containing iron.

The free radicals generated from the iron containing system of xanthine oxidase and hypoxanthine (Fe-XO/HX) were directly detected by using spin trapping. It was found that not only superoxide anion (O(2)*-) and hydroxyl radical (OH*), but also alkyl or alkoxyl radicals (R*) were formed when saccharides such as glucose, fructose and sucrose were added into the Fe-XO/HX system. The generated amount of R* was dependent on the kind and concentration of saccharides added into the Fe-XO/HX system and no R* were detected in the absence of saccharides, indicating that there is an interaction between the saccharide molecules and the free radicals generated from the Fe-XO/HX system and saccharide molecules are essential for generating R* in the Fe-XO/HX system. It is expected that the toxicity of R* would be greater than of hydrophilic O(2)*- and OH* because they are liposoluble and their lives are longer and the active sites of biomolecules are closely related with lipophilic phase, thus they can damage cells more seriously than O(2)*- and OH*. The R* generated from the saccharide containing Fe-XO/HX can be effectively scavenged by selenium containing abzyme (Se-abzyme), indicating Se-abzyme is a promising antioxidant.

Animals↗
PubMed1987

Superoxide dismutase isoenzymes, glutathione peroxidase and selenium in blood from HLA-B27-positive and -negative subjects.

We studied the activity of superoxide dismutase (SOD) isoenzymes (CuZnSOD, cyanide-resistant MnSOD and extracellular SOD), the concentration of plasma selenium (P-Se), and the activities of CuZnSOD and glutathione peroxidase (GSHPx) in erythrocytes of 10 HLA-B27-positive and 10 HLA-B27-negative subjects whose sera had shown high and low chemokinetic activity, respectively, on migration of polymorphonuclear leukocytes (PMN) in vitro. No significant difference was found between the groups, suggesting that the enhanced chemokinetic activity of HLA-B27-positive sera does not derive from an aberration in serum anti-oxidant potentials. The results were also analysed on the basis of HLA-DR specificities; HLA-DR4-positive plasma samples had significantly lower levels of Se than HLA-DR4-negative ones. We therefore carried out a second series of experiments with sera of 37 subjects; the levels of P-Se in HLA-DR4-positive and -negative groups were much the same, as were the activities of GSHPx. The data suggest that there is no gross aberration in P-Se concentration in HLA-DR4-positive subjects.

Chemotaxis, Leukocyte↗
PubMed1989

Selenium-independent glutathione peroxidase activity associated with glutathione S-transferase from the housefly, Musca domestica.

1. A glutathione S-transferase having Se-independent glutathione peroxidase activity was isolated from 100,000 g supernatant from housefly homogenate. 2. The specific activity of the partially purified Se-independent glutathione peroxidase was 1776 nmol NADPH oxidized/min/mg protein, representing an 87-fold purification. 3. The Mr of this enzyme was estimated to be 37,000 and 26,000 by gel filtration chromatography and gel electrophoresis, respectively. 4. Selenium-dependent glutathione peroxidase activity could not be detected in this same supernatant. 5. Se-independent glutathione peroxidase activity should be considered in future studies of the insect antioxidant defense system.

Animals↗
PubMed1988

Fluorimetry of selenium in body fluids after digestion with nitric acid, magnesium nitrate hexahydrate, and hydrochloric acid.

A digestion procedure involving nitric acid, magnesium nitrate hexahydrate, and hydrochloric acid suffices for selenium determinations in whole blood, serum, and urine by molecular fluorescence spectrometry. To test the accuracy of the method we compared the results with those from hydride-generation atomic absorption spectrometry, and we also analyzed reference materials.

Humans↗
PubMed1992

Glutathione redox cycle enzymes and selenium in severe rheumatoid arthritis: lack of antioxidative response to selenium supplementation in polymorphonuclear leucocytes.

The antioxidant capacity of the glutathione redox cycle and the concentrations of selenium in serum, red blood cells or whole blood, and polymorphonuclear leucocytes was evaluated in nine patients with severe rheumatoid arthritis (RA) and eight healthy controls receiving daily supplementation with 250 micrograms selenomethionine for six months. Serum and whole blood concentrations of selenium and the activity of the selenium dependent enzyme glutathione peroxidase (GSH-Px) were low in the serum, red blood cells, and polymorphonuclear leucocytes of patients with RA before selenium supplementation. During supplementation serum and whole blood concentrations of selenium and the activity of GSH-Px in serum and red blood cells of patients with RA and serum GSH-Px in controls increased. Selenium and GSH-Px in polymorphonuclear leucocytes were unaffected in patients with RA in contrast with the controls where both were augmented. Glutathione reductase activity in the red blood cells and polymorphonuclear leucocytes of patients with RA was low but increased during selenium supplementation. Whole blood concentrations of glutathione were slightly lower in patients with RA than controls and no difference in the content in polymorphonuclear leucocytes was found between the groups. The activity in red blood cells of glucose-6-phosphate dehydrogenase was high in patients with RA, indicating sufficient function of the hexose monophosphate pathway. The reduced antioxidant activity of the glutathione redox cycle in patients with severe RA was mainly due to the low availability of selenium. This was further supported by the response to selenium supplementation in serum and red blood cells. In the polymorphonuclear leucocytes, however, no biochemical effects of selenium supplementation were seen. This lack of antioxidative response could play a pathogenetic part in inflammation in patients with RA.

Adult↗
PubMed1996

Effect of selenium supplementation on biological constants and antioxidant status in rats.

Oxygen-derived free radicals are currently suspected to be widely involved in the aetiology of several clinical disorders. In animals as well as in man, antioxidant trials are often undertaken to prevent oxidative stress. Among antioxidant molecules selenium has been largely studied. This study shows that plasma Se level is not a good index of Se status in the organism, at least at high levels of selenium. Red blood cell Se seems to be a more reliable index of Se status and could replace plasma Se level in the supplementation trials both in animals and humans. Se supplementation did not result in a significant decrease in oxidative stress markers as evaluated by blood and tissue malondialdehyde contents in healthy animals. Furthermore, heart function was altered and plasma Alanine aminotransferase activity was significantly increased in the selenium-supplemented group, which could reflect a slight subtoxic effect of selenium supplementation at the level used here. In view of the results presented, the maximum selenium content in animal diet in selenium supplementation experiments should not be higher than 2 mg/kg.

Animals↗
PubMed1984

Interaction of gold(I) with the active site of selenium-glutathione peroxidase.

Gold(I) thioglucose in the presence of excess glutathione (GSH) leads to strong and reversible inhibition of selenium-glutathione peroxidase (EC 1.11.1.9) around neutral pH. Binding at equilibrium and competition studies demonstrated that the most reduced form of the active site selenocysteine is the only binding site for gold(I). Steady-state kinetics that gold(I) forms a dead-end complex with glutathione peroxidase in competition with the reduction of hydroperoxide. The apparent Ki is 2.3 microM at pH 7.6, 37 degrees C and 1 mM GSH. Theoretical models of inhibition were assessed by the use of linear least-squares fitting to a generalized integrated rate equation. The results are consistent with trapping of gold(I) at the active site in the form of a mixed bidentate selenolato -thiolate complex involving GSH and the active site selenocysteine. The kinetics of inhibition imply that the resting form of glutathione peroxidase in the presence of excess GSH is also within the enzyme cycle. This rules out the existence of selenium(+IV) species in the redox cycle of the active site when t- butylhydroperoxide is used as a substrate. Electronic properties of selenium and gold as well as a large relief of inhibition by selenocysteine suggest that a very stable interaction should be obtained between Se(-II) and gold(I) through covalent bonding. These results suggest that glutathione peroxidase could be a target of gold drugs used in the treatment of rheumatoid arthritis.

Animals↗
PubMed2006

Involvement of selenoprotein P in protection of human astrocytes from oxidative damage.

Selenoprotein P (SeP) is a highly glycosylated, selenium-rich plasma protein. Aside from its role as selenium carrier protein, an antioxidative function of SeP has been suggested. Astrocytes, which detoxify reactive oxygen species in the brain, were described as potential target cells of SeP. We investigated the expression of SeP in human astrocytes and its involvement in the protection of these cells against tert-butyl hydroperoxide (t-BHP)-induced oxidative damage. We show that primary human astrocytes and the human astrocytoma cell line MOG-G-CCM express SeP as an unglycosylated protein, which is not secreted. SeP expression in astrocytes is constitutive. Preincubation of astrocytes with hepatocyte-derived SeP mimicks the protective effect of low-molecular-weight selenocompounds such as sodium selenite or selenomethionine against oxidative damage, shielding astrocytes from t-BHP-induced cytotoxicity. Selenium supplementation of astrocytes counteracts oxidative stress via an increase in expression and activity of the selenoenzyme cytosolic glutathione peroxidase (cGPx). Furthermore, specific downregulation of SeP expression by small interfering RNA decreases cell viability of human astrocytes and makes them more susceptible to t-BHP-induced cytotoxicity. Our results implicate an antioxidant activity of constitutively expressed SeP in selenium-deficient astrocytes, while during adequate selenium supply the enhanced protection against oxidative stress is exerted by cGPx.

Antioxidants↗