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Journal ArticleDOI

Selenium-mediated biochemical changes in Japanese quails : Tissue uptake and distribution of injected(75)selenium labeled sodium selenite in relation to dietary selenium status.

01 Oct 1987-Biological Trace Element Research (Biol Trace Elem Res)-Vol. 14, pp 87-99
TL;DR: The tissue uptake and distribution of injected [75Se]-sodium selenite as a variance with time and as influenced by dietary selenium status was followed in the tissues of Japanese quails.

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Abstract: The tissue uptake and distribution of injected [(75)Se]-sodium selenite as a variance with time and as influenced by dietary selenium status was followed in the tissues of Japanese quails,Coturnix coturnix japonica. Quails maintained on a low selenium semipurified (basal) diet and basal diets supplemented with 0.2 and 2.0 ppm selenium as sodium selenite were injected intraperitonially with(75)Se as sodium selenite (2.8 microcuries). The injected(75)Se was monitored in blood, liver, kidney, heart, and testis at 24, 72, and 144 h after injection. Maximal uptake of the injected(75)Se was observed in tissues of quails maintained on basal diet. The uptake of(75)Se in tissues in general was determined by the dietary Se status. Among the organs studied, kidney had the maximal level of(75)Se, 0.2 ppm (μg/g wet tissue) followed by liver, testis, and heart, but testis had the maximal level when the level per milligram of protein was considered, about 3.0 ng/mg protein, followed by liver, kidney, and heart. About 10-20% of the tissue(75)Se was located in the mitochondria and 50-60% in the post-mitochondrial supernatant fractions in all dietary Se levels. Significant incorporation of(75)Se in the mitochondrial membrane was observed. The percent distribution ratio between the membrane and matrix fractions of the mitochondria remained constant at all dietary Se levels which, in liver was 65∶35, in kidney 55∶45, and in testis 75∶25. However, in heart mitochondria, the distribution of(75)Se between membrane and matrix varied with dietary Se status, the ratio being 82∶18 in the basal group, and 72∶28 and 41∶59 in the 0.2 and 2.0 ppm Se-supplemented groups, respectively. This is indicative of a preferential uptake of(75)Se in the mitochondrial membrane in conditions of deficiency. About 40-60% of the mitochondrial membrane-associated(75)Se was released upon Triton treatment in all the organs. Of the membrane-bound(75)Se, about 10-15% was acid-labile in liver and kidney and 25% in the heart tissue. Possibilities of tissue specific roles, especially in the heart mitochondrial membrane-related processes, are indicated for selenium.

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Topics: Selenium (54%)
Citations
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Journal ArticleDOI
P. Rani1, K. Lalitha1Institutions (1)
TL;DR: Electron microscopic observations revealed structural changes such as loss of cristae with proliferative and degenerative changes of the mitochondria in Se deficiency and involvement of Se in maintaining structure and functional efficiency of mitochondria is evident from the present study.

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Abstract: Selenium (Se) deficiency in the experimental models, Coturnix coturnix japonica and Corcyra cephalonica, resulted in impaired mitochondrial substrate oxidations and lowered thiol levels. Studies with respiratory inhibitors confirmed reduced mitochondrial electron transport enzyme activities, especially at cytochrome c oxidase (COX), the terminal segment. Enhanced mitochondrial lipid peroxidation in Se deficiency was more pronounced in the heart tissue of the quail compared to other tissues. Glutathione peroxidase (GSH-Px) activity toward H2O2 and cumene hydroperoxide were generally low in the insect muscle tissue and activity toward H2O2 was maximal in the quail heart mitochondria that was not very sensitive to Se status. Lowered COX activity in Se deficiency was more directly correlated with the increased level of lipid peroxidation than with the GSH-Px activity measured, suggestive of Se mediated protective mechanisms independent of GSH-Px. Electron microscopic observations revealed structural changes such as loss of cristae with proliferative and degenerative changes of the mitochondria in Se deficiency. Involvement of Se in maintaining structure and functional efficiency of mitochondria is evident from the present study.

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33 citations


Journal ArticleDOI
T. R. Santosh1, M. Sreekala1, K. Lalitha1Institutions (1)
TL;DR: The results including the differential response of GR activity to Se or mimosine supplementation are reflective of an effective reductive environment in Se groups and increased turnover of GSH in the presence of Mimosine.

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Abstract: Actaptive alterations in glutathione (GSH) metabolism were studied during oxidative stress induced by selenium (Se) deficiency in germinating seedlings ofTrigonella foenum- graecum grown for 72 h and the response to supplementation individually of Se or mimosine was explored. Growth enhancement with improved mitochondrial efficiency was elicited by supplementation of Se at 0.5-0.75 ppm or mimosine at 0.1-0.2 mM. Total thiol and protein levels of mitochondrial and soluble fractions, in general, did not vary significantly with supplementation of either Se or mimosine except that the mitochondrial protein levels in mimosine groups (0.1-0.2 mM) decreased by 20–30%. Mitochondrial glutathione peroxidase (GSH-Px) increased by twofold in activity toward H2O2, cumene hydroperoxide (CHP), and t-butyl hydroperoxide (tBHP) in Se groups, and by 50–60% increase toward H2O2 and CHP but by a twofold enhancement in enzyme activity with tBHP in mimosine groups. Soluble GSH-Px activity increased by 30–40% only in mimosine groups and remained unaltered in Se groups. Glutathione S-transferase activity (GST) in the soluble fraction of both Se and mimosine groups increased dramatically by fivefold to sixfold. Distinct differences were noted in the response of the stressed seedlings toward exposure to Se or mimosine and included a decline in glutathione reductase (GR) activity by 50–60% in both mitochondria and soluble fractions of Se groups and an increase in GR activity of the mitochondria by twofold and of the soluble enzyme activity by 30% in the mimosine groups. Mimosine exposure resulted in a dose-dependent decrease in the γ-glutamyl transpeptidase levels, but, in contrast, a significant enhancement by 50% was noted in the Se group at 0.75 ppm. The results including the differential response of GR activity to Se or mimosine supplementation are reflective of an effective reductive environment in Se groups and increased turnover of GSH in the presence of mimosine.

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22 citations


Cites background from "Selenium-mediated biochemical chang..."

  • ...The severe symptoms of oxidative stress prevalent in Se deficiency, well studied in animal systems (13-15), are coincidental with altered glutathione metabolism, including elevation of glutathione S-transferase (GST), a nonselenoenzyme, involved in detoxication mechanisms....

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Journal ArticleDOI
M. Sreekala1, T. R. Santosh1, K. Lalitha1Institutions (1)
TL;DR: It is demonstrated for the first time that mimosine, a naturally occuring toxic amino acid, could be a beneficial growth factor in concentrations between 0.1 and 0.2 mM.

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Abstract: Oxidative stress during selenium (Se) deficiency in the seedlings ofTrigonella foenum-graecum grown for 72 h was investigated and the response to supplemented levels of Se (0.5-1 ppm) and mimosine (0.05-1 mM) was evaluated. Beneficial effects of Se was maximal at 0.75 ppm. Mimosine, a toxic amino acid, was also found to be beneficial to the growth of the seedlings exposed up to 0.2 mM. When compared to the stressed seedlings, mitochondrial oxygen uptake from seedlings of Se (0.75 ppm) group and mimosine (0.2 mM) group exhibited threefold enhancement in state 3 respiration rate and a controlled state 4 rate, with respiratory control ratios of 5–8. Upon supplementation at the optimal levels, Superoxide dismutase (SOD) activities were enhanced fourfold with Se and eightfold with mimosine in the mitochondria. The soluble activity in mimosine groups increased twofold, but only by 75% in Se groups. Peroxidase activity registered a significant increase by threefold in mitochondria and fourfold in soluble fraction in both Se and mimosine groups. Exposure to Se or mimosine exhibited a differential response in the mitochondrial catalase and ascorbate peroxidase (Asc-Px) activities. In the Se groups, both catalase and Asc-Px in mitochondria decreased by 50–60%, which was contrasted by 60% increase in Asc-Px activity and 40% in catalase activity in mimosine groups. Supplementation with either Se or mimosine evoked similar responses of increases with respect to soluble catalase by twofold to threefold and Asc-Px by 90%. The results of the present study reveal (1) the Prevalence of oxidative stress inT. foenum-graecum during Se deficiency, (2) enhanced mitochondrial functional efficiency mediated by Se and mimosine independently, and (3) an antitoxidative role for mimosine during Se deficiency. The study demonstrates for the first time that mimosine, a naturally occuring toxic amino acid, could be a beneficial growth factor in concentrations between 0.1 and 0.2 mM.

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17 citations


Cites background from "Selenium-mediated biochemical chang..."

  • ...Experimental Se deficiency in animals has been widely studied (14-17), which indicates reversible and specific Se-dependent enzyme modulation in a variety of species....

    [...]


Journal ArticleDOI
K. Lalitha1, P. Rani1, Vasanthy Narayanaswami2Institutions (2)
Abstract: Requirement, uptake, and subcellular distribution of Na2 75SeO3 in the larvae of the insectC. cephalonica was investigated. That Se is well tolerated byC. cephalonica upto an added level of 2 ppm in the diet is suggested by the observed increase in body weight, total protein, and succinate dehydrogenase levels. Significant increases in the State 3 respiration ensued with Se supplementation up to 2 ppm in the mitochondrial oxidation of D-glycerol 1-phosphate, succinate and NADH, along with concomitant unaltered State 4 respiration, leading to enhanced RCR values. Maximal uptake of75Se was registered in the larvae maintained on basal diet when subjected to short-term exposure to 0.5 ppm75Se level. When exposure level was further increased up to 20 ppm, the observed decrease in the uptake of75Se suggested that Se status of larvae itself controlled the tissue uptake. Subcellular distribution pattern revealed maximal incorporation of75Se (cpm/g tissue) in the supernatant fraction, whereas, maximal specific75Se activity (cpm/mg protein) was associated with the mitochondrial fraction. Autoradiography of the soluble fractions indicated the presence of single selenoprotein in the larval group with short term 2 ppm75Se exposure. Inherent Se controls both the extent and the nature of distribution of mitochondrial75Se incorporation. Uptake of45Ca by the insect mitochondria was enhanced by dietary Se up to 2 ppm but was unaffected by addition ofin vitro 75Se in the medium. A more fundamental role for Se in the mitochondrial energy metabolism emerges from these studies.

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12 citations


Journal ArticleDOI
M. Sreekala1, K. Lalitha2Institutions (2)
TL;DR: The study reveals a differential response to Se among the β-galactosidase and β-glucosid enzyme of T. foenumgraecum with increase in the levels of β-GalactOSidase activity.

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Abstract: Beta-glucosidase and beta-galactosidase activity profile tested in different seeds during 24 h germination revealed reasonably high levels of activity in Vigna radiata, Cicer arietinum, and Trigonella foenum-graecum. In all seeds tested, beta-galactosidase activity was, in general, higher than that of beta-glucosidase. T. foenum-graecum seedlings exhibited maximal total and specific activities for both the enzymes during 72 h germination. Se supplementation as Na2SeO3 up to 0.75 ppm was found to be beneficial to growth and revealed selective enhancement of beta-galactosidase activity by 40% at 0.5 ppm Se. The activities of both the enzymes drastically decreased at 1.0 ppm level of Se supplementation. On the contrary, addition of Na2SeO3 in vitro up to 1 ppm to the enzyme extracts did not influence these activities. Hydrolytic rates of beta-glucosidase in both control and Se-supplemented groups were enhanced by 20% with 0.05 M glycerol in the medium and 30% at 0.1 M glycerol. The rates were marginally higher in Se-supplemented seedlings than the controls, irrespective of added glycerol in the medium. In contrast, hydrolysis by beta-galactosidase showed a trend of decrease in Se-supplemented seedlings compared to the control, when glycerol was present in the medium. Addition of Se in vitro in the assay medium showed no difference in the hydrolytic rate by beta-galactosidase when compared to control, while the activity of beta-glucosidase declined by 50%. Se-grown seedlings showed an enhancement of transglucosidation rate by 40% in the presence of 0.1 M glycerol. The study reveals a differential response to Se among the beta-galactosidase and beta-glucosidase of T. foenum-graecum with increase in the levels of beta-galactosidase activity.

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5 citations


References
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Journal Article
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.

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Abstract: Since 1922 when Wu proposed the use of the Folin phenol reagent for the measurement of proteins, a number of modified analytical procedures utilizing this reagent have been reported for the determination of proteins in serum, in antigen-antibody precipitates, and in insulin. Although the reagent would seem to be recommended by its great sensitivity and the simplicity of procedure possible with its use, it has not found great favor for general biochemical purposes. In the belief that this reagent, nevertheless, has considerable merit for certain application, but that its peculiarities and limitations need to be understood for its fullest exploitation, it has been studied with regard to effects of variations in pH, time of reaction, and concentration of reactants, permissible levels of reagents commonly used in handling proteins, and interfering substances. Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.

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285,427 citations


Journal ArticleDOI
Baruch J. Davis1Institutions (1)
TL;DR: The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.

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Abstract: Summary The technique of disc electrophoresis has been presented, including a discussion of the technical variables with special reference to the separation of protein fractions of normal human serum.

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17,697 citations


Journal ArticleDOI
09 Feb 1973-Science
TL;DR: When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H2O2, added glutathione failed to protect the hemoglobin from oxidative damage.

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Abstract: When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H(2)O(2), added glutathione failed to protect the hemoglobin from oxidative damage. This occurred because the erythrocytes were practically devoid of glutathione-peroxidase activity. Extensively purified preparations of glutathione peroxidase contained a large part of the (75)Se of erythrocytes labeled in vivo. Many of the nutritional effects of selenium can be explained by its role in glutathione peroxidase.

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6,444 citations


Journal ArticleDOI
TL;DR: Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration chromatogram of rat liver supernatant when 1.5 mM cumene hydroperoxide was used as substrate, and the second peak represents a second glutathienase activity which catalyzes the destruction of organic hydroperoxides but has little activity toward H 2 O 2 and which persists in severe selenium deficiency.

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Abstract: Glutathione peroxidase activity in the liver supernatant from rats fed a Se-deficient diet for 2 weeks was 8% of control when measured with H 2 O 2 but 42% of control when assayed with cumene hydroperoxide. Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration chromatogram of rat liver supernatant when 1.5 mM cumene hydroperoxide was used as substrate. Only the first peak was detected when 0.25 mM H 2 O 2 was used as substrate. The first peak was absent from chromatograms of Se-deficient rat liver supernatants; but the second peak, which eluted at a position corresponding to M.W. = 39,000, appeared unchanged. The second peak thus represents a second glutathione peroxidase activity which catalyzes the destruction of organic hydroperoxides but has little activity toward H 2 O 2 and which persists in severe selenium deficiency.

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3,026 citations


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01 Jan 1980-

696 citations