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 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.

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 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 Distribution and Possible Novel Role of Phospholipid Hydroperoxide Glutathione Peroxidase in Rat Epididymal Spermatozoa1

1997 ◽  
Vol 57 (6) ◽  
pp. 1502-1508 ◽  
Author(s):  
Cristiana Godeas ◽  
Federica Tramer ◽  
Fulvio Micali ◽  
Mariarosa Soranzo ◽  
Gabriella Sandri ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide

scholarly journals The Role of Phospholipid Hydroperoxide Glutathione Peroxidase Isoforms in Murine Embryogenesis

2006 ◽  
Vol 281 (28) ◽  
pp. 19655-19664 ◽  
Author(s):  
Astrid Borchert ◽  
Chi Chiu Wang ◽  
Christoph Ufer ◽  
Heike Schiebel ◽  
Nicolai E. Savaskan ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide ◽  
Peroxidase Isoforms
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