Effect of dietary selenium on plasma selenoprotein P, selenoprotein P1 and glutathione peroxidase in the rat

The purpose of this study was to determine the effect of dietary selenium on the abundance of selenium in plasma selenoprotein P, selenoprotein P1 and glutathione peroxidase. Weanling rats were provided water that contained 1.0, 0.1 or 0.01 ppm selenium and 75Se for 21 days. Gel filtration of denatured subunits was used to identify 75Se in the selenoproteins. Rats provided 1.0 ppm selenium accumulated 1.5 times more 75Se in liver cytosolic selenoprotein P1, but not in the two other selenoproteins, than did rats provided 0.1 ppm selenium. Most of the liver and blood selenium in rats provided 1.0 ppm selenium was insoluble and in an unknown chemical form. The tissue accumulation of unrecoverable selenium was apparently a response to the high dietary level of selenium. The proportion of selenium in plasma selenoprotein P, a putative selenium-transport protein, reflected the long-term selenium status of rats and varied from approximately 11-58% depending on the level of selenium supplementation. Turnover of selenium from this protein was affected by the dietary selenium of the rats. The results indicate that selenium incorporation into plasma selenoprotein P and selenoprotein P1 is affected by diet in ways that may reflect their importance to the rat.     

大鼠脑中的硒蛋白

喂Ｗｉｓｔａｒ雄性大鼠以８种不同硒水平的饲料,２０周时每组处死大鼠６只,取其大脑。硒耗竭组再随机分为４组,饲以４种不同硒水平的饲料,分别于不同时间处死,动态观察各种硒蛋白的变化。实验结果表明：细胞内谷胱甘肽过氧化物酶（ｃＧＰＸ）、磷脂氢谷胱甘肽过氧化物酶（ＰＨＧＰＸ）和Ⅱ型脱碘酶（ＩＤⅡ）发挥正常活性所需的最低饲料硒水平分别为０．０５、０．０３和０．０１ｍｇ／ｋｇ,而硒蛋白Ｐ和硒蛋白Ｗ正常表达时所需的最低饲料硒水平分别为０．０１和０．０５ｍｇ／ｋｇ。硒耗竭后补硒时硒蛋白Ｐ和ＩＤⅡ最优先利用硒,ｃＧＰＸ和ＰＨＧＰＸ次之,硒蛋白Ｗ最后。提示在脑中硒蛋白Ｐ和ＩＤⅡ较其余３种硒蛋白更重要。     

Both selenoproteins and low molecular weight selenocompounds reduce colon cancer risk in mice with genetically impaired selenoprotein expression

Selenium has cancer protective effects in a variety of experimental systems. Currently, it is not known whether selenoproteins or low molecular weight selenocompounds are responsible for this activity. To evaluate the contribution of selenoproteins to the cancer protective effects of selenium, we used transgenic mice that carry a mutant selenocysteine transfer RNA gene, which causes reduced selenoprotein synthesis. Selenium homeostasis was characterized in liver and colon of wild-type and transgenic mice fed selenium-deficient diets supplemented with 0, 0.1, or 2.0 microg selenium (as selenite)/g diet. (75)Se-labeling, Western blot analysis, and enzymatic activities revealed that transgenic mice have reduced (P < 0.05) liver and colon glutathione peroxidase expression, but conserved thioredoxin reductase expression compared with wild-type mice, regardless of selenium status. Transgenic mice had more (P < 0.05) selenium in the nonprotein fraction of the liver and colon than wild-type mice, indicating a greater amount of low molecular weight selenocompounds. Compared with wild-type mice, transgenic mice had more (P < 0.05) azoxymethane-induced aberrant crypt formation (a preneoplastic lesion for colon cancer). Supplemental selenium decreased (P < 0.05) the number of aberrant crypts and aberrant crypt foci in both wild-type and transgenic mice. These results provide evidence that a lack of selenoprotein activity increases colon cancer susceptibility. Furthermore, low molecular weight selenocompounds reduced preneoplastic lesions independent of the selenoprotein genotype. These results are, to our knowledge, the first to provide evidence that both selenoproteins and low molecular weight selenocompounds are important for the cancer-protective effects of selenium.     

Selenium from selenium-rich Spirulina is less bioavailable than selenium from sodium selenite and selenomethionine in selenium-deficient rats

The bioavailabilty of selenium (Se) from selenium-rich Spirulina (SeSp) was assessed in Se-deficient rats by measuring tissue Se accumulation and glutathione peroxidase (GSH-Px) activity. For 42 d, rats were subjected to dietary Se depletion by consumption of a Torula yeast (TY)-based diet with no Se; controls were fed the same diet supplemented with 75 microg Se/kg diet as sodium selenite. Se-deficient rats were then repleted with Se (75 microg/kg) by the addition of sodium selenite, selenomethionine (SeMet) or SeSp to the TY basal diet. Selenium speciation in SeSp emphasized the quasi-absence of selenite (2% of total Se); organic Se comprised SeMet (approximately 18%), with the majority present in the form of two selenoproteins (20-30 kDa and 80 kDa). Gross absorption of Se from SeSp was significantly lower than from free SeMet and sodium selenite. SeMet was less effective than sodium selenite in restoring Se concentration in the liver but not in kidney. SeSp was always much less effective. Similarly, Se from SeSp was less effective than the other forms of Se in restoring GSH-Px activity, except in plasma and red blood cells where no differences were noted among the three sources. This was confirmed by measuring the bioavailability of Se by slope-ratio analysis using selenite as the reference form of Se. Although Se from SeSp did not replenish Se concentration and GSH-Px activity in most tissues to the same degree as the other forms of Se, we conclude that it is biologically useful and differently metabolized due to its chemical form.     

The Diverse Role of Selenium within Selenoproteins: A Review

Selenium functions within mammalian systems primarily in the form of selenoproteins. Selenoproteins contain selenium as selenocysteine and perform a variety of physiological roles. Eleven selenoproteins have been identified: cellular or classical glutathione peroxidase; plasma (or extracellular) glutathione peroxidase; phospholipid hydroperoxide glutathione peroxidase; gastrointestinal glutathione peroxidase; selenoprotein P; types 1, 2, and 3 iodothyronine deiodinase; selenoprotein W; thioredoxin reductase; and selenophosphate synthetase. Of these, cellular and plasma glutathione peroxidase are the functional parameters used for the assessment of selenium status. Glutathione peroxidases catalyze the reduction of peroxides that can cause cellular damage. Thioredoxin reductase provides reducing power for several biochemical processes and defends against oxidative stress. Selenoprotein P appears to play a role in oxidant defense. Selenoprotein W may play a role in oxidant defense and be involved with muscle metabolism. Thyroid deiodinases function in the formation and regulation of active thyroid hormone. Selenophosphate synthetase is an enzyme required for the incorporation of selenocysteine into selenoproteins. In addition, a protein in the sperm mitochondrial capsule, which is vital to the integrity of sperm flagella, may be a unique selenoprotein. Recommended intakes, food sources, and status assessment of selenium, as well as selenium's role in health and disease processes, are reviewed.     

Brazil nuts: an effective way to improve selenium status

BACKGROUND: Brazil nuts provide a rich natural source of selenium, yet no studies have investigated the bioavailability of selenium in humans. OBJECTIVE: We investigated the efficacy of Brazil nuts in increasing selenium status in comparison with selenomethionine. DESIGN: A randomized controlled trial was conducted with 59 New Zealand adults. Participants consumed 2 Brazil nuts thought to provide approximately 100 mug Se, 100 mug Se as selenomethionine, or placebo daily for 12 wk. Actual intake from nuts averaged 53 mug Se/d (possible range: 20-84 mug Se). Plasma selenium and plasma and whole blood glutathione peroxidase (GPx) activities were measured at baseline and at 2, 4, 8, and 12 wk, and effects of treatments were compared. RESULTS: Plasma selenium increased by 64.2%, 61.0%, and 7.6%; plasma GPx by 8.3%, 3.4%, and -1.2%; and whole blood GPx by 13.2%, 5.3%, and 1.9% in the Brazil nut, selenomethionine, and placebo groups, respectively. Change over time at 12 wk in plasma selenium (P < 0.0001 for both groups) and plasma GPx activity in the Brazil nut (P < 0.001) and selenomethionine (P = 0.014) groups differed significantly from the placebo group but not from each other. The change in whole blood GPx activity was greater in the Brazil nut group than in the placebo (P = 0.002) and selenomethionine (P = 0.032) groups. CONCLUSION: Consumption of 2 Brazil nuts daily is as effective for increasing selenium status and enhancing GPx activity as 100 mug Se as selenomethionine. Inclusion of this high-selenium food in the diet could avoid the need for fortification or supplements to improve the selenium status of New Zealanders.     

Effect of chemical form of selenium on tissue glutathione peroxidase activity in developing rats

Two experiments were conducted to determine the effect of various forms of selenium (Se) on the activity of glutathione peroxidase (GSHPx) in liver, heart, kidney and eyes of the developing rat. In experiment 1, throughout mating, pregnancy and lactation, female rats consumed one of three diets: basal (less than 0.05 microgram Se/g); selenite (0.15 microgram Se/g) and selenomethionine (0.15 microgram Se/g). Some pups born to dams in the basal group were also given intraperitoneal doses of saline, selenite or selenomethionine. GSHPx activity was measured in tissues from fetuses, 7-d-old and 14-d-old nursing pups and the dams. In all tissues studied, GSHPx activity was highest in the 14-d-old pups whose mothers were in the selenomethionine group. Rat pups given intraperitoneal selenite (3 micrograms/kg body weight) had higher liver and kidney GSHPx activity than pups given the same amount of selenium as intraperitoneal selenomethionine. In experiment 2, all dams were fed the same basal diet, and pups were weaned to diets containing one of two levels of selenium (0.1 or 0.2 microgram/g), one of three forms of selenium (selenite, selenomethionine or selenocystine) or no added selenium. After 14 d of repletion, the highest level of hepatic GSHPx activity occurred in the selenite group and the lowest in the basal diet group. After 21 d of repletion, renal GSHPx activity was lowest in the basal group followed by the selenocystine group. The highest tissue selenium concentration was found in kidney tissues of the selenocystine group. These data support the hypothesis that these dietary forms of selenium are differentially available for GSHPx activity.     

Selenium bioavailability from buckwheat bran in rats fed a modified AIN-93G torula yeast-based diet

Selenium (Se) is an essential nutrient for humans and animals. The Se RDA for adult humans is 55 mug/d; however, dietary amounts as high as 200 mug/d in the highly available form of selenomethionine in yeast were shown to reduce the incidence of certain cancers. A number of natural foods contain relatively high amounts of Se; for the most part, however, the availability of food Se for absorption and utilization is unknown. This experiment was conducted to determine the bioavailability of Se from a high-protein, high-fiber bran-isolate of buckwheat groats that contains Se. The method used was based on the ability of Se from buckwheat bran to restore Se-dependent enzyme activities and tissue Se concentrations in Se-deficient rats. The responses produced from buckwheat bran Se were compared with a standard response curve generated by feeding graded amounts of Se as sodium selenite (Na(2)SeO(3); Na selenite) or selenomethionine (SeMet) in a newly reformulated AIN-93G-Torula yeast diet with a more balanced nutrient composition than older diets of this nature. Relative bioavailability was determined by using the slope-ratio assay method for enzyme data, or the parallel lines assay method for tissue Se concentration data. Results showed that Se availability from buckwheat bran based on the restoration of plasma Se was 70-80% as high as Na selenite or SeMet. However, when based on the restoration of muscle Se, buckwheat bran was 90% as high as Na selenite, but only 60% as high as SeMet. When using the ability of dietary Se to restore whole blood and liver glutathione peroxidase activity, buckwheat bran Se was 75-80% as high as Na selenite or SeMet. However, for the restoration of liver thioredoxin reductase, buckwheat bran Se was only 40% as high as Na selenite and 70% as high as SeMet. The relative bioavailability of Se from buckwheat bran with all variables considered was approximately 73% whether measured against Na selenite or SeMet. Although some variables indicated low bioavailability of Se from buckwheat bran, other factors such as Se speciation in the bran, digestibility of the bran, the cooking process, and combinations with other foods in the diet should be considered and analyzed before firm conclusions can be reached.     

The influence of selenium-enriched milk proteins and selenium yeast on plasma selenium levels and rectal selenoprotein gene expression in human subjects

Certain forms of dietary Se may have advantages for improving human Se status and regulating the risk for disease, such as cancers, including colorectal cancer (CRC). The present study compared the effects of a Se-enriched milk protein (dairy-Se) with a Se-rich yeast (yeast-Se) on plasma Se levels and rectal selenoprotein gene expression since we reasoned that if these genes were not regulated, there was little potential for regulating the risk for CRC in this organ. A total of twenty-three healthy volunteers with plasma Se in the lower half of the population range were supplemented with dairy-Se (150 μg/d) or yeast-Se (150 μg/d) for 6 weeks, followed by 6 weeks of washout period. Blood was sampled every 2 weeks, and rectal biopsies were obtained before and after Se supplementation and after the washout period. Plasma Se levels and glutathione peroxidase (GPx) activity, and rectal mRNA of selenoprotein P (SeP), cytosolic GPx-1 (GPx-1), gastrointestinal GPx-2 (GPx-2) and thioredoxin reductase-1 (TrxR-1) were measured. Plasma Se levels increased rapidly in both Se groups (P < 0·001); plasma GPx activity was not significantly changed. Rectal SeP mRNA increased at 6 weeks compared with baseline in both Se groups (P < 0·05); only dairy-Se resulted in a sustained elevation of SeP after the washout period (P < 0·05). Rectal GPx-1 and GPx-2 mRNA were higher with dairy-Se (P < 0·05) than with yeast-Se at 6 weeks. In conclusion, three rectal selenoprotein mRNA were differentially regulated by dairy-Se and yeast-Se. Changes in rectal selenoproteins are not predicted by changes in plasma Se; dairy-Se effectively regulates the expression of several rectal selenoproteins of relevance to the risk for CRC.     

The link between selenium and chemoprevention: a case for selenoproteins

Selenium is effective in reducing cancer incidence in animal models, and epidemiologic data, as well as supplementation trials, have indicated that selenium is likely to be effective in humans. The mechanism by which selenium prevents cancer remains unknown. The mammalian genome encodes 25 selenoprotein genes, each containing one or more molecules of selenium in the form of the amino acid selenocysteine, translationally inserted into the growing peptide in response to the UGA codon. There is evidence that several of these proteins may be involved with the mechanism by which selenium provides its anticancer effects. Data are reviewed indicating that genetic variants of the cytosolic glutathione peroxidase are associated with increased cancer risk, and that loss of one of the copies of this same gene may be involved with malignant progression. Similarly, allelic differences in the gene for a second selenoprotein, Sep15, may be relevant to the protection provided by selenium, and allelic loss at this locus have been reported as well. These data, along with the differential expression patterns reported for other selenoproteins in tumor vs. normal tissues, support the role of selenoproteins in the chemoprotection by selenium.     

Selenium dietary supplementation as a mechanism to restore hepatic selenoprotein regulation in rat pups exposed to alcohol

Ethanol exposure during gestation and lactation decreases selenium (Se) intake, disrupting body Se balance and inducing oxidative stress in rat offspring. Selenium-supplemented diet (0.5 ppm) was administered to ethanol-exposed (20% v/v) dams during gestation and lactation. When the dams' pups were 21 days old, the pups' levels of the main hepatic selenoproteins glutathione peroxidase (GPx1 and GPx4) and selenoprotein P (SelP) were measured. The pups were divided into control (C), alcohol (A), control-selenium (CS), and alcohol-selenium (AS) groups. The purpose was to evaluate the effect of the selenium-supplemented diet on the levels of Se deposits present in the livers of their pups. Alcohol decreases hepatic Se deposits, GPx activity, and GPx1 expression; alcohol increases GPx4 and SelP expression. Se was measured by furnace graphite atomic absorption spectrometry, the antioxidant activity of GPx and concentration of hepatic phospholipids (PL) were determined by spectrophotometry, and the selenoprotein expressions were detected by Western blotting. Selenite treatment prevented alcohol's effects of diminishing the Se deposits, GPx activity, and GPx1 expression, while maintaining the high levels of the expression of GPx4 and SelP. These results suggest that depletion of hepatic Se levels in rat pups, caused by ethanol exposure to their dams, affects the synthesis of the 3 main hepatic selenoproteins in different ways, which is related to a decrease in GPx activity and PL concentration, and an increase in serum Se levels. Selenium supplementation to the dams increased the expression of GPx1, GPx4, and SelP in their pups.     

Recent developments in trace element metabolism and function: newer roles of selenium in nutrition

Until recently, studies of the function of selenium focused on the selenoenzyme, glutathione peroxidase. However, the recognition that several metabolic effects of selenium are not associated with glutathione peroxidase has forced a re-evaluation of the function of this enzyme and the element. Hepatic glutathione peroxidase contains a significant percentage of the regulated selenium in the rat and is more sensitive to selenium deficiency than other selenoproteins. Thus, in addition to its enzymatic activity, it might have a storage function for the element. Another selenoprotein, designated selenoprotein P, has been found in rat plasma and has been quantitated. Its function is not yet known, but it has been postulated to be a transport protein for selenium and a defense against oxidant stress. Understanding the nutritional effects of selenium will require better characterization of glutathione peroxidase, selenoprotein P and other selenoproteins.     

An estimation of selenium requirements for New Zealanders.

BACKGROUND: Current US dietary recommendations for selenium are based on maximization of plasma glutathione peroxidase (GSHPx) activity according to data from one study of Chinese men. OBJECTIVE: The effect of various amounts of supplemental selenium on GSHPx activities in blood of New Zealand adults was investigated to calculate a selenium requirement for New Zealanders. The effect on plasma selenoprotein P and thyroid hormones was also investigated. DESIGN: Fifty-two adults with low blood selenium concentrations ingested a placebo or 10, 20, 30, or 40 microgram Se as L-selenomethionine daily for 20 wk. RESULTS: Plasma and whole-blood GSHPx activities increased in all supplemented groups but reached a plateau only in the group receiving 40 microgram Se, as determined by statistical analysis. Increases in selenoprotein P were greater than those for selenium and GSHPx at all supplement intakes. Thyroxine concentrations decreased in supplemented groups but the decrease was significantly different from that in the control group only for the 10-microgram group and for all supplemented groups combined. CONCLUSIONS: An upper estimated requirement of 90 microgram Se/d was calculated as the intake necessary for maximization of plasma GSHPx activity, as used in the derivation of the US recommended daily allowance. Our lower estimated requirement of 39 microgram Se/d was the intake necessary to reach two-thirds of maximal GSHPx activity, as was used in calculating the World Health Organization normative requirement. The lower estimate is a realistic goal for New Zealand but the upper estimate could be achieved only with regular inclusion of high-selenium foods.     

Effects of various dietary levels of selenium as selenite or selenomethionine on tissue selenium levels and glutathione peroxidase activity in rats

Weanling rats were fed a basal diet or this diet plus 0.2, 1.0, 2.0 or 4.0 mg/kg selenium (Se) as either selenite or selenomethionine (SeM). Except at the 0.2 mg/kg Se level, Se accumulated in all tissues at higher levels when SeM was fed than when selenite was given, and the magnitude of difference became more pronounced with increasing levels of dietary Se. This was particularly true for muscle and brain. Se levels in whole blood, testes, kidney and lungs were not significantly different between rats fed 0.2 mg/kg Se as selenite or as SeM, but the Se levels in liver, muscle and brain were higher in rats fed SeM. Although the tissue Se concentrations differed markedly, there were no differences in the glutathione peroxidase (GPX) activity in tissues of rats fed SeM rather than selenite. The percentage of Se associated with GPX was lower in all tissues from rats fed SeM than in those from rats fed selenite. These results indicate that the chemical forms of dietary Se can have a marked influence on biological responses, including bioavailability of dietary Se.     

克山病病区粮食中补充蛋氨酸对大鼠膳食硒生物利用的影响

为研究在克山病病区粮食中补充蛋氨酸对大鼠组织硒和谷胱甘肽过氧化物酶 (GPX)活性的影响 ,用克山病病区生产的低硒粮食为主配成低硒基础饲料 ,其硒含量为 0 .0 0 7mg/kg。在此基础上添加不同量的硒蛋氨酸 ,使饲料硒水平分别达到 0 .0 0 7、0 .0 6和 0 .5 0 mg/kg。每一硒水平又分别补充或不补充 4g/kg DL -蛋氨酸 ,配制成含不同硒和蛋氨酸的 6种饲料 ,分别喂养雄性 Wistar断乳大鼠 8周。结果在饲料硒水平为0 .0 0 7mg/kg时 ,补充蛋氨酸组动物除肌肉硒含量低于未补充组外 ,其它组织硒含量和各组织 GPX活力与不补充蛋氨酸动物无显著差异 ;在饲料硒水平为 0 .0 6 mg/kg时 ,补充蛋氨酸组动物组织中的硒含量出现了重新分布 ,最明显的是补充蛋氨酸组动物肌肉的硒含量减少 ,而肝脏和血硒含量增加 ,且各组织中 GPX活力显著大于未补充蛋氨酸组的动物 ;在饲料硒水平为 0 .5 0 mg/kg时 ,补充蛋氨酸组动物组织中硒含量有不同程度下降 ,但 GPX活力仍保持不变。研究结果认为病区粮食中蛋氨酸不足时 ,机体首先利用膳食中的硒蛋氨酸(谷类食物中硒的主要形式 )以替代蛋氨酸参与组织蛋白质的合成。补充蛋氨酸后 ,硒蛋氨酸即可发挥其应有生理功能。进一步提示病区粮食中蛋氨酸不足可能是与克山病发病有关的另一因素。     

Vitamin B6 dependence of selenomethionine and selenite utilization for glutathione peroxidase in the rat.

The biological availability of selenium from sodium selenite and selenomethionine for glutathione peroxidase activity was studied. Rats were fed ad libitum for 2 weeks a basal diet deficient in both selenium and vitamin B6, and then for the subsequent 2 weeks the same diet supplemented with vitamin B6 (2.5 micrograms as pyridoxine-HCl/g diet) or selenium (2 microgram/g diet) or both. In the presence of vitamin B6, selenite and selenomethionine increased equally the glutathione peroxidase activity in both the liver and erythrocytes above that of selenium-unsupplemented controls. In the absence of vitamin B6, selenomethionine was less effective in the liver and ineffective in the erythrocytes while selenite was equally effective in both tissues and was as effective as in the presence of vitamin B6. These results indicate that selenite selenium is readily available for glutathione peroxidase induction as compared with selenomethionine, and establish that vitamin B6 is involved in the metabolism of selenomethionine to supply selenium for glutathione peroxidase.     

Dietary selenium intake controls rat plasma selenoprotein P concentration

The purpose of this study was to determine the effect of dietary selenium on selenoprotein P concentration. Selenoprotein P was quantitated in plasma by radioimmunoassay. Selenium-dependent glutathione peroxidase activity in plasma and liver 105,000 x g supernatant was measured for comparison. Weanling male rats were fed a selenium-deficient diet or a control diet that contained 0.5 mg selenium/kg as Na2SeO4. The concentration of selenoprotein P fell at approximately the same rate in the rats fed the selenium-deficient diet as did plasma glutathione peroxidase activity. Groups of weanling rats were fed different levels of selenium for 8 wk. Selenoprotein P concentration was proportional to dietary selenium level up to 0.1 mg/kg and was a greater percentage of control values than was glutathione peroxidase activity. No increment in selenoprotein P concentration occurred between 0.1 and 0.5 mg selenium/kg diet. These results indicate that the concentration of selenoprotein P in the plasma is directly dependent on selenium supply in the diet up to 0.1 mg/kg. There is overlap between the dietary selenium ranges in which selenoprotein P concentration and glutathione peroxidase activity increase, but the selenoprotein P range is lower than the glutathione peroxidase range.     

Growth characteristics and selenium status changes of yeast cells with inorganic and organic selenium supplementation: selenium,a chemopreventive agent

We attempted to determine the level and form of selenium (Se) that yielded the maximum Se status of yeast cells, for their evaluation as a source of Se for chemopreventive action. The influence of various Se concentrations from organic (selenomethionine) and inorganic (sodium selenite) Se compounds on growth pattern and cell viability and the alterations in the antioxidant enzyme system of yeast were evaluated. A continuous decrease in cell and colony-forming units counts was observed with increasing concentrations of Se from either source. Increasing Se status of yeast cells was found with increasing concentrations of Se with both forms, with much greater uptake for organic Se at maximum Se concentrations. A continuous increase in glutathione peroxidase (GSH-Px) activity with increasing Se concentrations in both forms revealed an active Se response in terms of antioxidant activity, with a more pronounced percentage increase with selenomethionine. A highly significant increase in total glutathione was observed with selenomethionine supplementation, compared with sodium selenite. A decreasing trend in reduced glutathione was observed with increasing organic or inorganic Se concentrations. An increasing trend in glutathione-S-transferase activity was observed with increasing Se concentrations for both forms. Significantly higher values of glutathione-S-transferase were associated with the organic form at higher Se concentrations. There was normal activity of Se in mammalian cells. The results showed that an organic Se source more greatly enhances the Se status of yeast cells and hence could help in chemoprevention if consumed by the population.