Infleuce of dietary levels of vitamin E and selenium on tissue and blood parameters in pigs.
(1/2336)
Eighteen barrows approximately three weeks of age were used in a 3 X 3 factorial arrangement to investigate the effect of level of supplemental vitamin E and selenium on tissue and blood parameters. Tissue selenium concentrations increased in a quadratic manner with increased selenium intake with kidney tissue containing considerably greater concentrations than liver, heart or muscle. Supplementation of the diet caused a three-fold increase in serum selenium within the first week with a slight tendency to further increases in subsequent weeks. Serum vitamin E of unsupplemented pigs declined by fifty percent during the experiment, whereas supplemental vitamin E resulted in increased serum vitamin E. There was a considerable viration in percent peroxide hemolysis. Correlation of -0.63 between percent peroxide hemolysis and vitamin E intake and -0.85 between percent peroxide hemolysis and serum vitamin E were observed. (+info)
A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation.
(2/2336)
Several plant species can tolerate high concentrations of selenium in the environment, and they accumulate organoselenium compounds. One of these compounds is Se-methylselenocysteine, synthesized by a number of species from the genus Astragalus (Fabaceae), like A. bisulcatus. An enzyme has been previously isolated from this organism that catalyzes methyl transfer from S-adenosylmethionine to selenocysteine. To elucidate the role of the enzyme in selenium tolerance, the cDNA coding for selenocysteine methyltransferase from A. bisulcatus was cloned and sequenced. Data base searches revealed the existence of several apparent homologs of hitherto unassigned function. The gene for one of them, yagD from Escherichia coli, was cloned, and the protein was overproduced and purified. A functional analysis showed that the YagD protein catalyzes methylation of homocysteine, selenohomocysteine, and selenocysteine with S-adenosylmethionine and S-methylmethionine as methyl group donors. S-Methylmethionine was now shown to be also the physiological methyl group donor for the A. bisulcatus selenocysteine methyltransferase. A model system was set up in E. coli which demonstrated that expression of the plant and, although to a much lesser degree, of the bacterial methyltransferase gene increases selenium tolerance and strongly reduces unspecific selenium incorporation into proteins, provided that S-methylmethionine is present in the medium. It is postulated that the selenocysteine methyltransferase under selective pressure developed from an S-methylmethionine-dependent thiol/selenol methyltransferase. (+info)
Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes.
(3/2336)
Selenium has been increasingly recognized as an essential element in biology and medicine. Its biochemistry resembles that of sulfur, yet differs from it by virtue of both redox potentials and stabilities of its oxidation states. Selenium can substitute for the more ubiquitous sulfur of cysteine and as such plays an important role in more than a dozen selenoproteins. We have chosen to examine zinc-sulfur centers as possible targets of selenium redox biochemistry. Selenium compounds release zinc from zinc/thiolate-coordination environments, thereby affecting the cellular thiol redox state and the distribution of zinc and likely of other metal ions. Aromatic selenium compounds are excellent spectroscopic probes of the otherwise relatively unstable functional selenium groups. Zinc-coordinated thiolates, e.g., metallothionein (MT), and uncoordinated thiolates, e.g., glutathione, react with benzeneseleninic acid (oxidation state +2), benzeneselenenyl chloride (oxidation state 0) and selenocystamine (oxidation state -1). Benzeneseleninic acid and benzeneselenenyl chloride react very rapidly with MT and titrate substoichiometrically and with a 1:1 stoichiometry, respectively. Selenium compounds also catalyze the release of zinc from MT in peroxidation and thiol/disulfide-interchange reactions. The selenoenzyme glutathione peroxidase catalytically oxidizes MT and releases zinc in the presence of t-butyl hydroperoxide, suggesting that this type of redox chemistry may be employed in biology for the control of metal metabolism. Moreover, selenium compounds are likely targets for zinc/thiolate coordination centers in vivo, because the reactions are only partially suppressed by excess glutathione. This specificity and the potential to undergo catalytic reactions at low concentrations suggests that zinc release is a significant aspect of the therapeutic antioxidant actions of selenium compounds in antiinflammatory and anticarcinogenic agents. (+info)
Effects of pre- or postpartum selenium supplementation on selenium status in beef cows and their calves.
(4/2336)
The effect of Se supplementation before or after calving on Se status in deficient cows and their calves was studied using 72 beef cows in two experiments. In Exp. 1, cows calving in February or March 1997 were supplemented orally for 15 d in late pregnancy with 13.0, 32.5, or 45.5 mg of Se/d as sodium selenite. Glutathione peroxidase (GSH-Px) activities were measured in red blood cells (RBC) or plasma of cows and calves at d 15 and between d 17 and 88 after calving. In Exp. 2, cows calving in January 1997 were supplemented orally with .0, 13.0, or 32.5 mg of Se/d for 15 d postpartum, and calves were injected with 1.38 mg of Se when 2 d old and at an average age of 49 d. The GSH-Px activities were measured in 30-d-old calves and in cows and calves between d 77 and 115 after calving. In both experiments, Se supplementation resulted in adequate Se status for the dams. The increase in RBC GSH-Px activity was faster with 45.5 mg of Se/d, and GSH-Px activities remained high for up to 98 d after the end of supplementation. The improvement in Se status in calves as a result of maternal supplementation was greater in Exp. 1 than in Exp. 2, suggesting that the placental transfer of Se is more efficient than milk transfer. Prepartum oral Se supplementation of deficient beef cows with 13.0 mg of Se/d for 15 d allowed adequate Se status of dams and calves, and 45.5 mg of Se/d resulted in a faster improvement of Se status. Parenteral administration of 1.38 mg of Se to newborn calves did not sustain normal Se status in calves issued from deficient cows. (+info)
Selenium toxicosis in a flock of Katahdin hair sheep.
(5/2336)
Selenium supplementation by injection is a common practice. Acute toxicosis from dosaging errors may occur. In this report, 23 of 56 ewes and all 24 lambs injected with selenium died. Tissue, whole blood, and serum concentrations aided in the diagnosis. Caution should be taken when supplementing selenium by injection. (+info)
The role of humic substances in drinking water in Kashin-Beck disease in China.
(6/2336)
We conducted in vitro and in vivo assays in a selenium-deficient system to determine if organic matter (mainly fulvic acid; FA) is involved in a free radical mechanism of action for Kashin-Beck disease. Cartilage cell culture experiments indicated that the oxy or hydroxy functional groups in FA may interfere with the cell membrane and result in enhancement of lipid peroxidation. Experiments with rats demonstrated that toxicity from FA was reduced when the hydroxy group was blocked. Induction of lipid peroxidation by FA in liver and blood of rats was similar to that exhibited by acetyl phenyl hydrazine. FA accumulated in bone and cartilage, where selenium rarely concentrates. In addition, selenium supplementation in rats' drinking water inhibited the generation of oxy-free radicals in bone. We hypothesized that FA in drinking water is an etiological factor of Kashin-Beck disease and that the mechanism of action involves the oxy and hydroxy groups in FA for the generation of free radicals. Selenium was confirmed to be a preventive factor for Kashin-Beck disease. (+info)
Biotransformation of methylmercury in vitro.
(7/2336)
Inorganic mercury formation from methylmercury by the mouse liver and kidney was studied in vitro. With chopped liver or kidney, inorganic mercury was formed from added methylmercury, but when the tissue was homogenized, the activity was diminished. Equimolar addition of selenium had no effect on the reaction. (+info)
The retention and distribution by healthy young men of stable isotopes of selenium consumed as selenite, selenate or hydroponically-grown broccoli are dependent on the isotopic form.
(8/2336)
Twenty-seven healthy young men were randomly assigned to diets that supplied low (32.6 microg/d) or high (226.5 microg/d) levels of selenium for a 105-d study. After consuming the diets for 85 d, subjects were fed a test meal that contained 74Se in the form of selenite or selenate and 82Se incorporated into hydroponically-raised broccoli. Urine, fecal and blood samples were collected daily. Isotope absorption was not different (P > 0.05) for selenate and Se in broccoli; Se absorption from selenite was highly variable and was not included in statistical analyses. Significantly more isotope was absorbed by subjects fed the high Se diet (P = 0. 015). Urinary isotope excretion was greater when selenate was fed than when broccoli was fed (P = 0.0001), and consequently more Se from broccoli (as compared to selenate) was retained (59.2 +/- 2.4 and 36.4 +/- 4.6% for Se in broccoli and selenate, respectively; P = 0.0001). Despite the higher retention, less isotope from broccoli than from selenate was present in the plasma. Plasma proteins separated by gel permeation chromatography showed that most of the isotopes were distributed between two medium molecular weight peaks. Less isotope was found in plasma proteins of subjects fed the high Se diet, but the form of Se had no effect on isotope distribution. These results show that dietary Se intake alters the retention of stable isotopes of Se and that humans retain and distribute Se from broccoli in a different manner than Se from inorganic salts. (+info)