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PubMed1993

Microscopic localization of mercury-selenium interaction products in liver, kidney, lung and brain of Mediterranean striped dolphins (Stenella Coeruleoalba) by silver enhancement kit.

Microscopic observation, using physical development of silver, was carried out to localize the mercury-selenium interaction products in the organs of Mediterranean striped dolphins. The silver-metal reaction products were located mainly in hepatocytes and macrophages for liver, in proximal tubules for kidney. They were less abundant in lung than in liver and kidney. The result of semi-quantitative histochemistry tests showed that silver staining deposits were more abundant at relatively high metal concentrations than low metal contents, but independent of the metal contents. Comparisons with the most concentrated metal contents suggested that there might be a new complex of mercury and selenium, which could not be stainable by physical silver development.

Animals↗
PubMed2005

Analysis of the selenium species distribution in cow blood by size exclusion liquid chromatography-inductively coupled plasma collision cell mass spectrometry (SEC-ICPccMS).

A method for performing rapid semiquantitative screening of the distribution of Se species in the blood of cows fed with a diet enriched in selenized yeast was optimized. The method was based on direct injection of a blood sample onto a high resolution size exclusion chromatographic column and fractionation of the selenium species. Selenium was detected on-line by ICP-MS with a collision cell. The concentrations of selenized haemoglobin and free selenomethionine were estimated using the chromatogram. The method was applied to a study involving 15 control and 15 treated dairy cows at four different supplementation time points. The increase in the selenomethionine and selenized haemoglobin was a linear function of the total selenium concentration. A threshold value of 600 ng ml(-1) of total Se was established beyond which selenomethionine could not be incorporated into the protein. No inorganic selenium was found to be present. The total selenium in cow blood correlated well with that in milk. The selenium supplementation did not change the protein distribution profiles for other essential elements (Cu, Fe, Mn, Zn).

Animals↗
PubMed1996

Micronucleus induction by chromium and selenium, and suppression by metallothionein inducer.

The clastogenic effects of chromium compounds (CrCl3 and K2CrO4) and selenium compounds (H2SeO3 and Na2SeO4) in mouse bone marrow cells have been investigated. K2CrO4 induced significant, dose-related increases in micronuclei. H2SeO3 also showed a significant micronucleus induction at the highest dose. CrCl3 and Na2SeO4 were negative for micronuclei induction in mice. The suppressive effect of Bi(NO3)3, a metallothionein inducer, on the micronucleus induction by K2CrO4 and H2SeO3 has been also investigated. Pretreatment with Bi(NO3)3 suppressed the micronucleus induction by K2CrO4 and H2SeO3. In addition, the incidence of micronucleus induction seemed to be reduced by double dosing with K2CrO4 and H2SeO3, compared to single dosing. It is generally recognized that a number of metal compounds induce metallothionein synthesis. These results suggest that the mechanism of suppression of micronucleus induction by K2CrO4 and H2SeO3 involve possible participation of metallothionein in mouse bone marrow.

Animals↗
PubMed2000

Synthesis and characterization of selenotrisulfide-derivatives of lipoic acid and lipoamide.

Thiol-containing compounds, such as glutathione and cysteine, react with selenite under specific conditions to form selenotrisulfides. Previous studies have focused on isolation and characterization of intermolecular selenotrisulfides. This study describes the preparation and characterization of intramolecular selenotrisulfide derivatives of lipoic acid and lipoamide. These derivatives, after separation from other reaction products by reverse-phase HPLC, exhibit an absorbance maximum at 288 nm with an extinction coefficient of 1,500 M(-1) small middle dotcm(-1). The selenotrisulfide derivative of lipoic acid was significantly stable at or below pH 8.0 in contrast to several other previously studied selenotrisulfides. Mass spectral analysis of the lipoic acid and lipoamide derivatives confirmed both the expected molecular weights and also the presence of a single atom of selenium as revealed by its isotopic distribution. The selenotrisulfide derivative of lipoic acid was found to serve as an effective substrate for recombinant human thioredoxin reductase as well as native rat thioredoxin reductase in the presence of NADPH. Likewise, the lipoamide derivative was efficiently reduced by NADH-dependent bovine lipoamide dehydrogenase. The significant in vitro stability of these intramolecular selenotrisulfide derivatives of lipoic acid can serve as an important asset in the study of such selenium adducts as model selenium donor compounds for selenophosphate biosynthesis and as rate enhancement effectors in various redox reactions.

Animals↗
PubMed1996

Attenuation of oxidation and nitration reactions of peroxynitrite by selenomethionine, selenocystine and ebselen.

The effect of the selenium-containing compounds selenomethionine, selenocystine and ebselen [2-phenyl-1,2-benzisoselenazol-3(2H)-one] on the oxidation of dihydrorhodamine 123 caused by peroxynitrite and on the nitration of 4-hydroxyphenylacetate by peroxynitrite was studied in comparison with their sulphur analogues methionine, cystine and ebsulfur [2-phenyl-1,2-benzisothiazol-3(2H)-one]. The selenocompounds protected dihydrorhodamine 123 from oxidation and 4-hydroxyphenylacetate from nitration more effectively than their sulphur analogues. Sodium selenite exhibited no effect. These observations are corollaries to the recent finding [Roussyn, Briviba, Masumoto and Sies (1996) Arch. Biochem. Biophys. 330, 216-218] that selenium-containing compounds are efficient in protecting against peroxynitrite-induced DNA single-strand breaks.

Azoles↗
PubMed2001

Selenoxidation by flavin-containing monooxygenases as a novel pathway for beta-elimination of selenocysteine Se-conjugates.

Previously, it was shown that beta-elimination of selenocysteine Se-conjugates by rat renal cytosol leading to pyruvate formation was not solely catalyzed by pyridoxal phosphate-dependent enzymes. It was hypothesized that selenoxidation of the selenocysteine Se-conjugates, followed by syn-elimination, may be an alternative mechanism for pyruvate formation. In this study, selenoxidation of selenocysteine Se-conjugates was studied using rat liver microsomes and recombinant human oxidative enzymes. For all six selenocysteine Se-conjugates that were tested, it was found that rat liver microsomal incubations led to the formation of pyruvate, whereas the corresponding selenoxides were not observed. Microsomal pyruvate formation from Se-benzyl-L-selenocysteine (SeBC) was NADPH-dependent, but only marginally inhibited by several P450 inhibitors. Inhibition by methimazole and by heat pretreatment and stimulation by n-octylamine indicated that flavin-containing monooxygenases are mainly responsible for pyruvate formation from the selenocysteine Se-conjugates in rat liver microsomes. In the case of S-benzyl-L-cysteine, the sulfur analogue of SeBC, pyruvate formation was not observed. For this substrate, a chemically stable sulfoxide could be observed, as previously described. By using recombinantly expressed human flavin-containing monooxygenases and P450 enzymes, it was delineated that SeBC is selenoxidized by human FMOs, but not by human P450s. The k(cat)/K(m) of selenoxidation was 3.8-fold higher for FMO-1 than for FMO-3. In conclusion, selenoxidation of selenocysteine Se-conjugates catalyzed by FMOs and subsequently syn-elimination has taken place as an alternative route for the formation of pyruvate from selenocysteine Se-conjugates. Although selenoxides are known to be easily reduced by thiol compounds, microsomal pyruvate formation from SeBC was only 75% inhibited in the presence of an excess of glutathione. This indicates that even in the presence of physiological concentrations of reducing thiol compounds, selenoxides of selenocysteine Se-conjugates may undergo syn-elimination to some extent. Whether selenoxides and/or selenenic acids that are formed are involved in the activity of chemopreventive selenocysteine Se-conjugates remains to be established.

Animals↗
PubMed1975

Interrelationships of selenium with other trace elements.

Biological interactions between selenium and a number of other elements occur that render selenium much less toxic than when it is present alone. These elements are arsenic, mercury, cadmium, and copper. Furthermore, the presence of selenium reduces the toxicity of mercury and cadmium. These are general biological interactions and have been found to occur in a number of animal species under a variety of conditions. It has been shown that the reaction products of selenium with mercury and cadmium are less toxic than an equal amount of selenium fed alone to chicks. The presence of arsenic shifts the excretion of selenium to the bile. There is no conclusive evidence that the presence of other elements reduces the absorption or retention of selenium. It is possible that some of the interactions are caused by the formation of a compound by selenium and other elements which has less affinity for active groups on biologically active compounds.--Hill, C.H. Interrelationships of selenium with other trace elements.

Animals↗
PubMed2005

Efficient synthesis of the glucosidase inhibitor blintol, the selenium analogue of the naturally occurring glycosidase inhibitor salacinol.

An efficient synthesis of blintol, the selenium congener of the naturally occurring glycosidase inhibitor salacinol, and a potent glucosidase inhibitor itself, is described. Unlike our previously reported synthesis, this improved route makes use of p-methoxybenzyl ether protecting groups in the synthesis of one of the two key intermediates, 2,3,5-tri-O-p-methoxybenzyl-1,4-anhydro-4-seleno-D-arabinitol, from L-xylose. The other key intermediate, 2,4-O-benzylidene-L-erythritol-1,3-cyclic sulfate, was successfully prepared from D-glucose instead of the expensive L-glucose. All protecting groups in the resulting adducts were removed with trifluoroacetic acid to yield a mixture of stereoisomers, thereby obviating the problematic deprotection of benzyl ethers by hydrogenolysis. The major stereoisomer, blintol, was then obtained by fractional crystallization.

Celastraceae↗
PubMed2004

Influences of different selenium species on the uptake and assimilation of Hg(II) and methylmercury by diatoms and green mussels.

We examined the influences of different concentrations and species of Se (selenite, selenate, and seleno-l-methionine) in the ambient environment on the accumulation of inorganic Hg(II) and methylmercury (MeHg) by the diatom Thalassiosira pseudonana and the green mussel Perna viridis. At the experimental concentrations tested (< 500 microgl(-1)), selenite and selenate did not significantly affect the uptake of either mercury species by the diatoms and the green mussels. The assimilation efficiency of Hg(II) and MeHg by the mussels from ingested diatoms was also independent of the inorganic Se loadings in the food particles. In contrast, selenomethionine significantly inhibited the uptake of MeHg and enhanced the uptake of Hg(II) by the diatoms and the mussels, but it did not affect the assimilation from the ingested diatoms. The influence of tissue body burden of Se in the green mussels following pre-exposure to selenite and selenomethionine for different periods (1-5 weeks) on the accumulation of Hg(II) and MeHg was further investigated. Our results showed that tissue Se concentrations did not significantly affect the dietary assimilation of mercury, but the influences on the aqueous uptake were variable. Our study thus, strongly highlights the specificity of the Se-Hg interaction in marine mussels for different Se and Hg species. Both dissolved and dietary uptake appeared to be equally important in the accumulation of Hg(II) and MeHg in the green mussels.

Animals↗
PubMed1992

Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide.

Synthesis of a labile selenium donor compound, selenophosphate, from selenide and ATP by the Escherichia coli SELD enzyme was reported previously from this laboratory. From the gene sequence, SELD is a 37-kDa protein that contains 7 cysteine residues, 2 of which are located at positions 17 and 19 in the sequence -Gly-Ala-Cys-Gly-Cys-Lys-Ile- (Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E., and Böck, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 73, 543-547). Inactivation of the enzyme by alkylation with iodoacetamide indicated that at least 1 cysteine residue in the protein is essential for enzyme activity. To test the possibility that the Cys17 and/or Cys19 residue might be essential, these were changed to serine residues by site-specific mutagenesis. The biological activities of the wild type and mutant proteins were studied using E. coli MB08 (selD-) transformed with plasmids containing the selD genes. The plasmid containing the Cys17-mutated gene failed to complement MB08, whereas the Cys19-mutated gene was indistinguishable from wild type. The mutant proteins, like the wild type enzyme, bound to an ATP-agarose matrix, showing that their affinities for ATP were unimpaired. Selenide-dependent formation of AMP from ATP was abolished by mutation of Cys17, but the Cys19 mutation had no effect on the ability of the enzyme to catalyze the reaction. These results indicate that Cys17 has an essential role in the catalytic process that leads to the formation of selenophosphate from ATP and selenide.

Adenosine Triphosphate↗
PubMed2006

Individual and joint actions of selenate and methylmercury on the development and survival of insect detritivore Megaselia scalaris (Diptera: Phoridae).

Despite the important roles played by insects in most ecosystems, surprisingly little is known about how anthropogenic pollutants or their mixtures interact to affect insect populations. The independent and joint actions of selenate and methylmercury on a ubiquitous insect detritivore, Megaselia scalaris (Loew), were determined in this study. Ovipositing females did not distinguish between untreated food sources and those contaminated with toxic concentrations of selenate, methylmercury, or both chemicals in combination. Even at the highest concentrations of pollutants, no negative effects were observed for the egg stage. However, larval survival was significantly decreased and development significantly prolonged by selenate and methylmercury individually at low or intermediate ecologically relevant treatment levels. Potentiation was strongly evident because mixtures containing concentrations as little as only 1% of the respective individual median lethal tolerances (LC(50)s) caused significantly more mortality and delayed larval development than would be expected from the responses selenate and methylmercury elicit individually. However, survival and pupal development was not affected at any rate tested. Female fecundity was significantly decreased by methylmercury but not by selenate or mixture treatments. The relative toxicity to M. scalaris of each of the individual and joint treatments was selenate (LC(50) = 260 microg/g) < methylmercury (LC(50) = 22 microg/g) < the mixture at approximately 5% of the LC(50) concentration of each of the components (12 microg/g selenate plus 1.0 microg/g methylmercury). The increased mortality and delayed larval development within sites contaminated by selenate, methylmercury, or combination of the two have substantial implications for the ecology, population dynamics, and sustainability of M. scalaris populations. If these results can be extrapolated to other arthropod detritivores, ecosystem food-web function may be substantially affected.

Animals↗
PubMed2003

Intestinal absorption in health and disease: micronutrients.

The main theme of this chapter concerns the precise biochemical mechanisms involved in stages up to, and including, gastrointestinal absorption of vitamins and certain selected minerals. Essential data regarding sequential events, immediately following absorption of these micronutrients, are also included. There is reference to water-soluble vitamins that are, in general, either coenzymes in various metabolic reactions or carriers of certain biochemical groupings. In contrast, fat-soluble vitamins frequently function as integral components of cell membranes; they, too, receive ample attention. It is appropriate, nevertheless, to recognize that some minerals required in very small amounts are closely allied biochemically with particular vitamins; these specific associations are apportioned emphasis at relevant places in the text. Although predominant discussion centres on the physiological state, clinical reference is necessarily made to gastrointestinal disorders in which imbalance of vitamins and minerals consequently results in an additional detrimental impact on health.

Ascorbic Acid↗
PubMed2004

Isolation of a Se-nitrososelenol: a new class of reactive nitrogen species relevant to protein Se-nitrosation.

Nitric oxide (NO) is a messenger molecule implicated in a number of physiological processes. Nitrosation of selenoproteins has been suggested as playing an important role in NO-mediated cellular functions such as the inactivation of glutathione peroxidase (GPx), but no chemical information about Se-nitrosated species has been available to date. Here a stable Se-nitrososelenol (RSeNO), a new class of NO derivative, was synthesized and fully characterized by X-ray crystallography and spectroscopic methods. This Se-nitrososelenol can be formed by direct transnitrosation from an S-nitrosothiol to a selenol, as is the case in the proposed mechanism for the NO-mediated inactivation of GPx.

Crystallography, X-Ray↗
PubMed2005

Photophysical properties of biologically compatible CdSe quantum dot structures.

The photophysical properties of CdSe and ZnS(CdSe) semiconductor quantum dots in nonpolar and aqueous solutions were examined with steady-state (absorption and emission) and time-resolved (time-correlated single-photon-counting) spectroscopy. The CdSe structures were prepared from a single CdSe synthesis, a portion of which were ZnS-capped, thus any differences observed in the spectral behavior between the two preparations were due to changes in the molecular shell. Quantum dots in nonpolar solvents were surrounded with a trioctylphosphine oxide (TOPO) coating from the initial synthesis solution. ZnS-capped CdSe were initially brighter than bare uncapped CdSe and had overall faster emission decays. The dynamics did not vary when the solvent was changed from hexane to dichloromethane; however, replacement of the TOPO cap by pyridine affected CdSe but not ZnS(CdSe). CdSe was then solubilized in water with mercapto-acetic acid or dihydrolipoic acid, whereas ZnS(CdSe) could be solubilized only with dihydrolipoic acid. Both solubilization agents quenched the nanocrystal emission, though with CdSe the quenching was nearly complete. Additional quenching of the remaining emission was observed when the redox-active molecule adenine was conjugated to the water-soluble CdSe but was not seen with ZnS(CdSe). The emission of aqueous CdSe could be enhanced under prolonged exposure to room light and resulted in a substantial increase of the emission lifetimes; however, the enhancement occurred concurrently with precipitation of the nanocrystals, which was possibly caused by photocatalytic destruction of the mercaptoacetic acid coating. These results are the first presented on aqueous CdSe quantum dot structures and are presented in the context of designing better, more stable biological probes.

Cadmium Compounds↗