scholarly journals Effects of Dietary Selenium Deficiency or Excess on Selenoprotein Gene Expression in the Spleen Tissue of Pigs

Animals ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 1122 ◽  
Author(s):  
Zhuang Lu ◽  
Pengzu Wang ◽  
Teng Teng ◽  
Baoming Shi ◽  
Anshan Shan ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Thioredoxin Reductase ◽  
Selenium Deficiency ◽  
Type I ◽  
Mrna Levels ◽  
Spleen Tissue ◽  
Selenoprotein K ◽  
Selenoprotein Genes ◽  
Se Deficiency ◽  
Selenoprotein M

To evaluate the effects of dietary Se deficiency and excess on the mRNA levels of selenoproteins in pig spleen tissues, 20 healthy uncastrated boars (Duroc × Landrace × Yorkshire, 10 ± 0.72 kg) were randomly divided into four groups (5 pigs per group). The pigs were fed a Se deficient corn-soybean basal feed (Se content <0.03 mg/kg) or basal feed with added sodium selenite at 0.3, 1.0, or 3.0 mg Se/kg diet, respectively. The experiment lasted 16 weeks. The spleen tissue was collected to examine the mRNA expression levels of 24 selenoprotein genes at the end of the study. Compared with pigs in other groups, those fed with the 1.0 mg Se/kg diet had higher mRNA levels of glutathione peroxidase 1 (Gpx1), glutathione peroxidase 2 (Gpx2), deiodinase type II (Dio2), thioredoxin reductase 3 (Txnrd3), selenoprotein H (Selh), selenoprotein N, 1 (Sepn1), selenoprotein P1 (Sepp1), and selenoprotein V (Selv) in the spleen (p < 0.05). Dietary Se deficiency resulted in lower mRNA levels of Gpx1, Gpx2, glutathione peroxidase 3 (Gpx3), Dio2, thioredoxin reductase 2 (Txnrd2), Txnrd3, Selh, selenoprotein I (Seli), selenoprotein K (Selk), selenoprotein M (Selm), Sepn1, Sepp1, and Selv in the spleen than the other three groups. Dietary Se levels did not affect the mRNA levels of glutathione peroxidase 4 (Gpx4), deiodinase type I (Dio1), deiodinase type III (Dio3), selenophosphate synthetase 2 (Sephs2), thioredoxin reductase 1 (Txnrd1), selenoprotein O (Selo), selenoprotein S (Sels), selenoprotein W (Selw), selenoprotein X (Selx), and selenoprotein 15 (Sel15) in the spleen (p > 0.05). Dietary Se levels can affect the transcription levels of 14 selenoprotein genes in the spleen of pigs.

scholarly journals Role of the 3′ untranslated region in the regulation of cytosolic glutathione peroxidase and phospholipid-hydroperoxide glutathione peroxidase gene expression by selenium supply

1996 ◽  
Vol 320 (3) ◽  
pp. 891-895 ◽  
Author(s):  
Giovanna BERMANO ◽  
John R. ARTHUR ◽  
John E. HESKETH
Keyword(s):  
Gene Expression ◽  
Glutathione Peroxidase ◽  
Selenium Deficiency ◽  
Type I ◽  
Mrna Levels ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Iodothyronine Deiodinase ◽  
Phospholipid Hydroperoxide ◽  
Cytosolic Glutathione

Selenium is an essential nutrient and synthesis of selenoproteins is affected by limited selenium supply. During selenium deficiency there is a differential regulation of selenoprotein synthesis and gene expression; for example, there is a decrease in abundance of mRNA for cytosolic glutathione peroxidase (cGSH-Px) and a preservation of mRNA for phospholipid-hydroperoxide glutathione peroxidase (PHGSH-Px). This difference is not due to an alteration in the rate of transcription but might reflect differences in translation. The aim of the present work was to assess the role of cGSH-Px and PHGSH-Px 3´ untranslated regions (UTRs) in the regulation of selenoprotein mRNA stability and translation by using H4-II-E-C3 cells transfected with different constructs containing a type I iodothyronine deiodinase-coding region linked to different selenoprotein mRNA 3´ UTRs. Translational efficiency results showed that the efficiency of the 3´ UTRs in permitting selenocysteine incorporation is similar in selenium-replete conditions but, when selenium is limiting, the 3´ UTR of cGSH-Px is less efficient than the 3´ UTR of PHGSH-Px. The results suggest that the 3´ UTR of these selenoprotein mRNA species influences their extent of translation when selenium levels are low. The different sensitivity of the 3´ UTRs to selenium deficiency can explain the differential effect that selenium deficiency has on cGSH-Px and PHGSH-Px activity and mRNA levels, stability and translation. This might be partly responsible for channelling selenium for synthesis of PHGSH-Px rather than cGSH-Px.

scholarly journals Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats

1995 ◽  
Vol 311 (2) ◽  
pp. 425-430 ◽  
Author(s):  
G Bermano ◽  
F Nicol ◽  
J A Dyer ◽  
R A Sunde ◽  
G J Beckett ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Transcriptional Control ◽  
Selenium Deficiency ◽  
Mrna Levels ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Tissue Specific ◽  
Run Off ◽  
Cytosolic Glutathione ◽  
Se Deficiency ◽  
Specific Regulation

Regulation of synthesis of the selenoenzymes cytosolic glutathione peroxidase (GSH-Px), phospholipid hydroperoxide glutathione peroxidase (PHGSH-Px) and type-1 iodothyronine 5′-deiodinase (5′IDI) was investigated in liver, thyroid and heart of rats fed on diets containing 0.405, 0.104 (Se-adequate), 0.052, 0.024 or 0.003 mg of Se/kg. Severe Se deficiency (0.003 mg of Se/kg) caused almost total loss of GSH-Px activity and mRNA in liver and heart. 5′IDI activity decreased by 95% in liver and its mRNA by 50%; in the thyroid, activity increased by 15% and mRNA by 95%. PHGSH-Px activity was reduced by 75% in the liver and 60% in the heart but mRNA levels were unchanged; in the thyroid, PHGSH-Px activity was unaffected by Se depletion but its mRNA increased by 52%. Thus there is differential regulation of the three mRNAs and subsequent protein synthesis within and between organs, suggesting both that mechanisms exist to channel Se for synthesis of a particular enzyme and that there is tissue-specific regulation of selenoenzyme mRNAs. During Se depletion, the levels of selenoenzyme mRNA did not necessarily parallel the changes in enzyme activity, suggesting a distinct mechanism for regulating mRNA levels. Nuclear run-off assays with isolated liver nuclei showed severe Se deficiency to have no effect on transcription of the three genes, suggesting that there is post-transcriptional control of the three selenoenzymes, probably involving regulation of mRNA stability.

scholarly journals Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome

2009 ◽  
Vol 29 (5) ◽  
pp. 329-338 ◽  
Author(s):  
Roger A. Sunde ◽  
Anna M. Raines ◽  
Kimberly M. Barnes ◽  
Jacqueline K. Evenson
Keyword(s):  
Thioredoxin Reductase ◽  
Selenium Deficiency ◽  
Underlying Mechanism ◽  
Pcr Analysis ◽  
Mrna Levels ◽  
Nonsense Mediated Decay ◽  
Liver And Kidney ◽  
Se Deficiency ◽  
Selenoprotein Mrnas ◽  
Se Status

Gpx (glutathione peroxidase)-1 enzyme activity and mRNA levels decrease dramatically in Se (selenium) deficiency, whereas other selenoproteins are less affected by Se deficiency. This hierarchy of Se regulation is not understood, but the position of the UGA selenocysteine codon is thought to play a major role in making selenoprotein mRNAs susceptible to nonsense-mediated decay. Thus in the present paper we studied the complete selenoproteome in the mouse to uncover additional selenoprotein mRNAs that are highly regulated by Se status. Mice were fed on Se-deficient, Se-marginal and Se-adequate diets (0, 0.05 and 0.2 μg of Se/g respectively) for 35 days, and selenoprotein mRNA levels in liver and kidney were determined using microarray analysis and quantitative real-time PCR analysis. Se-deficient mice had liver Se concentrations and liver Gpx1 and thioredoxin reductase activities that were 4, 3 and 3% respectively of the levels in Se-adequate mice, indicating that the mice were Se deficient. mRNAs for Selh (selenoprotein H) and Sepw1 (selenoprotein W) as well as Gpx1 were decreased by Se deficiency to <40% of Se-adequate levels. Five and two additional mRNAs were moderately down-regulated in Sedeficient liver and kidney respectively. Importantly, nine selenoprotein mRNAs in liver and fifteen selenoprotein mRNAs in the kidney were not significantly regulated by Se deficiency, clearly demonstrating that Se regulation of selenoprotein mRNAs is not a general phenomenon. The similarity of the response to Se deficiency suggests that there is one underlying mechanism responsible. Importantly, the position of the UGA codon did not predict susceptibility to Se regulation, clearly indicating that additional features are involved in causing selenoprotein mRNAs to be sensitive to Se status.

scholarly journals Neonatal Selenoenzyme Expression Is Variably Susceptible to Duration of Maternal Selenium Deficiency

Antioxidants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 288
Author(s):  
Laura G. Sherlock ◽  
Durganili Balasubramaniyan ◽  
Lijun Zheng ◽  
Miguel Zarate ◽  
Thomas Sizemore ◽  
...  
Keyword(s):  
Thioredoxin Reductase ◽  
Selenium Deficiency ◽  
Deficient Diet ◽  
Hepatic Expression ◽  
Multiple Organs ◽  
Thioredoxin Reductase 1 ◽  
Neonatal Liver ◽  
Se Deficiency ◽  
The Impact ◽  
Gpx Activity

Maternal selenium (Se) deficiency is associated with decreased neonatal Se levels, which increases the risk for neonatal morbidities. There is a hierarchy to selenoprotein expression after Se deficiency in adult rodents, depending on the particular protein and organ evaluated. However, it is unknown how limited Se supply during pregnancy impacts neonatal selenoprotein expression. We used an Se-deficient diet to induce perinatal Se deficiency (SeD), initiated 2–4 weeks before onset of breeding and continuing through gestation. Neonatal plasma, liver, heart, kidney, and lung were collected on the day of birth and assessed for selenoproteins, factors required for Se processing, and non-Se containing antioxidant enzymes (AOE). Maternal SeD reduced neonatal circulating and hepatic glutathione peroxidase (GPx) activity, as well as hepatic expression of Gpx1 and selenophosphate synthetase 2 (Sps2). In contrast, the impact of maternal SeD on hepatic thioredoxin reductase 1, hepatic non-Se containing AOEs, as well as cardiac, renal, and pulmonary GPx activity, varied based on duration of maternal exposure to SeD diet. We conclude that the neonatal liver and circulation demonstrate earlier depletion in selenoenzyme activity after maternal SeD. Our data indicate that prolonged maternal SeD may escalate risk to the neonate by progressively diminishing Se-containing AOE across multiple organs.

scholarly journals Selenoprotein expression and brain development in preweanling selenium- and iodine-deficient rats

1998 ◽  
Vol 20 (2) ◽  
pp. 203-210 ◽  
Author(s):  
JH Mitchell ◽  
F Nicol ◽  
GJ Beckett ◽  
Keyword(s):  
Glutathione Peroxidase ◽  
Brain Development ◽  
Iodine Deficiency ◽  
Selenium Deficiency ◽  
Type I ◽  
Compensatory Mechanisms ◽  
Iodothyronine Deiodinase ◽  
Rat Pups ◽  
Cytosolic Glutathione ◽  
Old Rats

Selenium deficiency causes further impairment of thyroid hormone metabolism in iodine-deficient rats and therefore could have a role in the aetiology of both myxoedematous and neurological cretinism in humans. Thyroidal type I iodothyronine deiodinase (ID-I), cytosolic glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase activities were increased in iodine-deficient adult rats and their offspring at 11 days of age. Thyroidal ID-I activity was unchanged and thyroidal cytosolic glutathione peroxidase activity was decreased by more than 75% by combined selenium and iodine deficiency in 11-day-old rats, indicating that, while the thyroid retained an ability to produce 3,3',5-triiodothyronine (T3), the gland was probably more susceptible to peroxidative damage caused by increased hydrogen peroxide concentrations driven by increased thyrotrophin. Thyroidal atrophy, common in myxoedematous cretinism, did not occur in iodine- or selenium and iodine-deficient rat pups. Iodine deficiency increased brain type II iodothyronine deiodinase activity 1.5-fold in 4-day-old rats and 3-fold in 11-day-old rats, regardless of selenium status. Thus rats were able to activate compensatory mechanisms in brain that would maintain T3 concentrations in selenium and iodine deficiencies. Surprisingly, however, selenium deficiency had a greater effect than iodine deficiency on markers of brain development in rat pups. Expression of the brain-derived neurotrophic factor (BDNF) mRNA was decreased in selenium deficiency in 4- and 11-day-old pups and in combined selenium and iodine deficiency in 4-day-old pups. Iodine deficiency caused an increase in BDNF expression in 11-day-old pups but had no effect on 4-day-old pups. Myelin basic protein mRNA expression in brain was decreased by combined selenium and iodine deficiency in 11-day-old rats.

Selenium regulation of transcript abundance and translational efficiency of glutathione peroxidase-1 and −4 in rat liver

2001 ◽  
Vol 357 (3) ◽  
pp. 851-858 ◽  
Author(s):  
Sherri WEISS SACHDEV ◽  
Roger A. SUNDE
Keyword(s):  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Transcript Abundance ◽  
Translational Efficiency ◽  
Mrna Levels ◽  
Glutathione Peroxidase 1 ◽  
Relative Contribution ◽  
Se Deficiency ◽  
Selenoprotein Mrnas ◽  
Se Status

Glutathione peroxidase (GPX)1 mRNA in rat liver falls dramatically during Se deficiency to levels that are approx. 10% of Se-adequate levels. This regulation is mediated by mRNA stability, and is hypothesized to involve nonsense-mediated mRNA decay. mRNA levels for GPX4 and other selenoproteins are much less regulated by Se status. To evaluate the relative contribution of mRNA abundance versus translational efficiency to overall regulation of GPX1 expression, we quantified GPX1, GPX4 and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) transcripts per cell in rat liver. Surprisingly, we found that GPX1 transcripts in Se deficiency are moderately abundant and similar in abundance to GAPDH and other selenoprotein mRNAs; Se supplementation increases GPX1 mRNA so that it is 30-fold higher than GAPDH mRNA. Translational efficiency of GPX1 mRNA is half of that of GPX4. Translational efficiency of GPX1 mRNA increases approx. 20-fold with Se supplementation and appears to switch GPX1 mRNA from nonsense-mediated degradation to translation. This regulatory switch can explain why GPX1 expression is an excellent parameter for assessment of Se status.

scholarly journals Differential selenium-dependent expression of type I 5′-deiodinase and glutathione peroxidase in the porcine epithelial kidney cell line LLC-PK1

1995 ◽  
Vol 306 (3) ◽  
pp. 851-856 ◽  
Author(s):  
M Gross ◽  
M Oertel ◽  
J Köhrle
Keyword(s):  
Steady State ◽  
Glutathione Peroxidase ◽  
Cell Line ◽  
Kidney Cell ◽  
Maximal Activity ◽  
Transcriptional Level ◽  
Type I ◽  
Mrna Levels ◽  
Kidney Cell Line ◽  
Activity Measurements

The Se-dependent expression of two selenoproteins, cytosolic glutathione peroxidase (cGPx) and type I iodothyronine-5′-deiodinase (5′DI), was investigated in the porcine epithelial kidney cell line LLC-PK1 in serum-free medium. The selenite-dependent expression of cGPx and 5′DI was revealed by enzyme-activity measurements, affinity labelling of 5′DI, metabolic labelling of proteins with 75Se and steady-state mRNA analysis. The expression of the two enzymes strongly depended on selenite concentrations of the culture medium. cGPx required 2-fold higher selenite levels than 5′DI to reach half-maximal activity. The Se-dependent enzyme activities were approximately paralleled by the corresponding steady-state mRNA levels. The response of the two enzymes to Se supply was further characterized by kinetic Se-depletion and -repletion experiments. Upon removal of medium selenite, cGPx activity decreased exponentially, whereas after an initial decrease over 1-2 days, 5′DI levels completely recovered during a further 2 days. These data indicate a differential Se-dependent regulation of the two selenoproteins, with 5′DI being preferentially supplied with the trace element Se, thus ensuring a continuous cellular capacity for thyroid-hormone activation, even under Se-deficient conditions. The abundant cGPx in cells with sufficient Se supply might serve as a cellular Se store which can be mobilized for the synthesis of more vital selenoproteins such as 5′DI under shortage conditions. Thus, a cellular hierarchy of selenoprotein expression, reflected by different individual regulation mechanisms at the transcriptional and post-transcriptional level, adds to the previously recognized tissue-specific hierarchy of Se retention.

scholarly journals Selenium deficiency as a model of experimental pre-eclampsia in rats

Reproduction ◽  
2004 ◽  
Vol 128 (5) ◽  
pp. 635-641 ◽  
Author(s):  
J Vanderlelie ◽  
K Venardos ◽  
A V Perkins
Keyword(s):  
Glutathione Peroxidase ◽  
Complex Disease ◽  
Thioredoxin Reductase ◽  
Selenium Deficiency ◽  
Lipid Peroxides ◽  
Epidemiological Studies ◽  
Protein Carbonyls ◽  
Pregnant Rats ◽  
High Selenium

Epidemiological studies andin vitroanalysis demonstrate correlations between selenium status and human pre-eclampsia (PET). Selenium is an essential component in the anti-oxidant proteins glutathione peroxidase and thioredoxin reductase, which are produced in lower amounts in pre-eclamptic placenta. This study examined the effect of modulating dietary selenium content in pregnant rats. Rats were fed diets containing no selenium, 239 μg/kg selenium or 1000 μg/kg selenium, four weeks prior to and following conception. Significant pregnancy-specific increases in systolic blood pressure (116.4 ± 5.2 mmHg vs 108 ± 6.8 mmHg vs 111.4 ± 4.7 mmHg) and proteinuria (9.68 ± 2.12 μg/ml vs 5.93 ± 1.59 μg/ml vs 4.43 ± 0.96 μg/ml) were demonstrated in animals fed a selenium free-diet when compared with normal or high selenium diets. Placental weight and pup number were not affected by selenium deprivation, however a significant decrease in the pup weight was evident. Selenium deprivation caused dose-dependent decreases in liver glutathione peroxidase (28.55 ± 3.82 mmoles/min/mg vs 34.68 ± 8.64 mmoles/min/mg) and thioredoxin reductase (2.37 ± 1.25 U/mg vs 6.68 ± 1.82 U/mg) activity, whereas superoxide dismutase activity remained constant. Placental activity of these enzymes also decreased leading to oxidative stress as measured by increased lipid peroxides (17.92 ± 1.78 μmoles/mg vs 8.30 ± 5.52 μmoles/mg) and protein carbonyls in tissue extracts from selenium-free animals. These results suggest that selenium deficiency in pregnant rats leads to symptoms similar to those seen in human PET and may provide an experimental model for studying this complex disease.

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