Knockout of Selenoprotein V Affects Regulation of Selenoprotein Expression by Dietary Selenium and Fat Intakes in Mice

ABSTRACT Background The metabolic function of selenoprotein V (SELENOV) remains unknown. Objectives Two experiments were conducted to determine effects of the Selenov knockout (KO) on selenium concentration and mRNA, protein, and/or activity of 4 major selenoproteins [glutathione peroxidase (GPX) 1, GPX4, thioredoxin reductase-1 (TXNRD1), and selenoprotein P (SELENOP)] in the serum, liver, testis, and/or white adipose tissue (WAT) of mice fed different dietary selenium and fat concentrations. Methods In Experiment (Expt) 1, 40 KO and 40 wild-type (WT) mice (males, 8 wk old) were fed (n = 10/genotype) a casein-sucrose basal diet plus 0, 0.3, 1, or 3 mg Se/kg (as sodium selenite) for 32 wk . In Expt 2, 20 KO and 20 WT mice (males, 8 wk old) were fed (n = 10/genotype) a normal-fat diet (NF; 10% calories from fat) or a high-fat diet (HF; 60% calories from fat) for 19 wk. Results In Expt 1, the KO caused consistent or substantial decreases (P < 0.05) of mRNA amounts of Gpx1, Txnrd1, and Selenop in the testis (≤52%), but selenium concentrations (19–29%) and GPX activities (≤ 50%) were decreased in the liver across different dietary selenium concentrations . Hepatic and testis GPX1 protein was elevated (≤31%) and decreased (≤45%) by the KO, respectively. In Expt 2, the genotype and dietary fat intake exerted interaction effects ( P < 0.05) on Gpx1 mRNA amounts in the WAT; Gpx1, Txnrd1, and Selenop mRNA amounts and TXNRD activities in the testis; and selenium concentrations in the serum and liver. However, these 2 treatments produced largely independent or additive effects (P < 0.05) on the GPX1 and SELENOP protein amounts in the liver and testis (up to ± 50% changes). Conclusions The KO-mediated changes in the tissue selenium concentrations and functional expression of 3 major selenoproteins implied potential for SELENOV in regulating body selenium metabolism in the mouse.

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Effects of Time and Dietary Selenium Concentration as Sodium Selenite on Tissue Selenium Uptake by Sheep

Journal of Animal Science ◽

10.2527/jas1988.6692299x ◽

1988 ◽

Vol 66 (9) ◽

pp. 2299 ◽

Cited By ~ 17

Author(s):

M. G. Echevarria ◽

P. R. Henry ◽

C. B. Ammerman ◽

P. V. Rao

Keyword(s):

Sodium Selenite ◽

Selenium Concentration ◽

Dietary Selenium ◽

Selenium Uptake ◽

Tissue Selenium

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The effects of dietary selenium on growth performances, oxidative stress and tissue selenium concentration of gibel carp (Carassius auratus gibelio)

Aquaculture Nutrition ◽

10.1111/j.1365-2095.2010.00841.x ◽

2011 ◽

Vol 17 (3) ◽

pp. e741-e749 ◽

Cited By ~ 66

Author(s):

D. HAN ◽

S. XIE ◽

M. LIU ◽

X. XIAO ◽

H. LIU ◽

...

Keyword(s):

Oxidative Stress ◽

Carassius Auratus ◽

Selenium Concentration ◽

Gibel Carp ◽

Carassius Auratus Gibelio ◽

Dietary Selenium ◽

Growth Performances ◽

Tissue Selenium

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Dietary selenium requirements based on tissue selenium concentration and glutathione peroxidase activities in old female rats

Journal of Trace Elements in Medicine and Biology ◽

10.1016/j.jtemb.2009.02.002 ◽

2009 ◽

Vol 23 (2) ◽

pp. 132-137 ◽

Cited By ~ 15

Author(s):

Roger A. Sunde ◽

Kevin M. Thompson

Keyword(s):

Glutathione Peroxidase ◽

Selenium Concentration ◽

Female Rats ◽

Dietary Selenium ◽

Tissue Selenium

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Comparison of different forms of dietary selenium supplementation on gene expression of cytoplasmic thioredoxin reductase, selenoprotein P, and selenoprotein W in broilers

Czech Journal of Animal Science ◽

10.17221/7797-cjas ◽

2014 ◽

Vol 59 (No. 12) ◽

pp. 571-578 ◽

Cited By ~ 6

Author(s):

X.A. Zhan ◽

H.F. Wang ◽

D. Yuan ◽

Y.X. Wang ◽

F. Zhu

Keyword(s):

Gene Expression ◽

Mrna Level ◽

Thioredoxin Reductase ◽

Basal Diet ◽

Selenoprotein P ◽

Mrna Levels ◽

Selenoprotein W ◽

Dietary Selenium ◽

Liver And Kidney ◽

Similar Body

Effects of different forms of dietary selenium (Se) supplementation on gene expression of cytoplasmic thioredoxin reductase (TrxR1), selenoprotein P (SelP), and selenoprotein W (SelW) in broilers were investigated. A total of six hundred Ross 308 broilers (1-day-old) with similar body weight were randomly divided into three groups, each of which included 5 replicates of 40 birds. These three treatments received the same basal diet with only background Se level of 0.04 mg Se/kg, supplemented with 0.15 mg Se/kg as sodium selenite (SS) or l-selenomethionine (l-Se-Met) or d-selenomethionine (d-Se-Met) for 42 days. The SS supplemented diet increased TrxR1 activity in liver (P < 0.01) and kidney (P < 0.01) as well as SelP concentration in serum (P < 0.05) and liver (P < 0.01) more than the d-Se-Met supplemented diet. The addition of SS also highly increased liver (P < 0.01) and kidney (P < 0.01) TrxR1 activities of broilers in comparison with broilers fed l-Se-Met diet. In addition, liver TrxR1 activity in l-Se-Met group was higher than that in d-Se-Met group (P < 0.05). Liver and kidney mRNA levels of TrxR1 and SelP as well as breast muscle SelW mRNA level were significantly increased by l- and d-Se-Met supplementation in comparison with SS supplementation (P < 0.01), while the d-Se-Met group showed more effective (P < 0.01) than the l-Se-Met group in increasing the mRNA levels of TrxR1 and SelP in liver and kidney. Therefore, dietary l-Se-Met and d-Se-Met supplementation could improve mRNA levels of different selenoproteins studied and reduce amounts of TrxR1 and SelP in broilers compared with SS. Besides, l-Se-Met is more effective than d-Se-Met in raising TrxR1 activity and decreasing mRNA abundance of TrxR1 and SelP in broilers.  

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System-wide identification and prioritization of enzyme substrates by thermal analysis

Nature Communications ◽

10.1038/s41467-021-21540-6 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Amir Ata Saei ◽

Christian M. Beusch ◽

Pierre Sabatier ◽

Juan Astorga Wells ◽

Hassan Gharibi ◽

...

Keyword(s):

Thermal Analysis ◽

Thioredoxin Reductase ◽

Structural Level ◽

Post Translational Modification ◽

Post Translational Modifications ◽

Enzyme Substrate ◽

Thioredoxin Reductase 1 ◽

Enzyme Substrates ◽

Substrate Proteins

AbstractDespite the immense importance of enzyme–substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.

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Oxidative stress response in regulatory and conventional T cells: a comparison between patients with chronic coronary syndrome and healthy subjects

Journal of Translational Medicine ◽

10.1186/s12967-021-02906-2 ◽

2021 ◽

Vol 19 (1) ◽

Author(s):

Anna K. Lundberg ◽

Rosanna W. S. Chung ◽

Louise Zeijlon ◽

Gustav Fernström ◽

Lena Jonasson

Keyword(s):

Oxidative Stress ◽

T Cells ◽

Mononuclear Cells ◽

Ex Vivo ◽

Thioredoxin Reductase ◽

Healthy Controls ◽

Antioxidant Genes ◽

Consistent Finding ◽

Coronary Syndrome ◽

Thioredoxin Reductase 1

Abstract Background Inflammation and oxidative stress form a vicious circle in atherosclerosis. Oxidative stress can have detrimental effects on T cells. A unique subset of CD4+ T cells, known as regulatory T (Treg) cells, has been associated with atheroprotective effects. Reduced numbers of Treg cells is a consistent finding in patients with chronic coronary syndrome (CCS). However, it is unclear to what extent these cells are sensitive to oxidative stress. In this pilot study, we tested the hypothesis that oxidative stress might be a potential contributor to the Treg cell deficit in CCS patients. Methods Thirty patients with CCS and 24 healthy controls were included. Treg (CD4+CD25+CD127−) and conventional T (CD4+CD25−, Tconv) cells were isolated and treated with increasing doses of H2O2. Intracellular ROS levels and cell death were measured after 2 and 18 h, respectively. The expression of antioxidant genes was measured in freshly isolated Treg and Tconv cells. Also, total antioxidant capacity (TAC) was measured in fresh peripheral blood mononuclear cells, and oxidized (ox) LDL/LDL ratios were determined in plasma. Results At all doses of H2O2, Treg cells accumulated more ROS and exhibited higher rates of death than their Tconv counterparts, p < 0.0001. Treg cells also expressed higher levels of antioxidant genes, including thioredoxin and thioredoxin reductase-1 (p < 0.0001), though without any differences between CCS patients and controls. Tconv cells from CCS patients were, on the other hand, more sensitive to oxidative stress ex vivo and expressed more thioredoxin reductase-1 than Tconv cells from controls, p < 0.05. Also, TAC levels were lower in patients, 0.97 vs 1.53 UAE/100 µg, p = 0.001, while oxLDL/LDL ratios were higher, 29 vs 22, p = 0.006. Conclusion Treg cells isolated from either CCS patients or healthy controls were all highly sensitive to oxidative stress ex vivo. There were signs of oxidant-antioxidant imbalance in CCS patients and we thus assume that oxidative stress may play a role in the reduction of Treg cells in vivo.

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