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1
Mahmoud, Kholoud Gamal, Rasha Mohamed Gamal Elshafiey, Radwa Mahmoud Elsharaby, and Amany Mahmoud Elbarky. "Selenoprotein-p as Biomarker of Selenium Status in Obese Children and Adolescents." Asian Journal of Pediatric Research 13, no. 4 (2023): 169–79. http://dx.doi.org/10.9734/ajpr/2023/v13i4306.
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Background: The child and adolescent obesity have become a major public health problem. Selenoprotien p1 (SEPP1) is widely acknowledged to be among the most delicate functional indicators of Se status and it plays a role in the metabolism of Se and in anti-oxidative defense. So, we aimed to assess Selenoprotein-p level in obese children and adolescents.
 Methods: This cross-sectional comparative work included 60 children: 30 obese children and the control group consisted of 30 children who were healthy and matched in terms of gender and age. A comprehensive taking of history and clinical assessment with anthropometric measurements were conducted on all children and adolescents. Basic investigations and serum selenoprotien-p1 level were performed.
 Results: Serum selenoprotien-p1 (SEPP1) levels were substantially decreased in obese children contrasted to controls.
 Conclusions: Selenoprotien p1 levels were substantially decreased in obese children and adolescent. Selenoprotien p1 could be a sensitive functional biomarker of selenium status.
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Zhang, Chi, and Qi Bin Huang. "A Preliminary Study on the Antioxidant Activity of Selenoprotein in Cordyceps militaris Rich in Selenium." Advanced Materials Research 396-398 (November 2011): 157–61. http://dx.doi.org/10.4028/www.scientific.net/amr.396-398.157.
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Utilize different solvents to extract and salt out soluble protein from the Cordyceps rich in selenium which is artificially cultivated, thus obtaining different types of selenoproteins contained in it, and then pyrogallol autoxidation method is applied to determine their antioxidant activity, meanwhile, double-channel atomic fluorescence is used to detect the materials and their selenium content. The results show that: various proteins of Cordyceps rich in selenium all contain selenium, followed by alkali-soluble selenoprotein > alcohol-soluble selenoprotein > salt-soluble selenoprotein > water-soluble selenoprotein; their ability to remove superoxide anion is followed by water-soluble protein> alkali-soluble protein > salt-soluble protein> alcohol-soluble protein, the clearance rate of selenoprotein with different salting points on superoxide anion is shown as follows: salting selenoprotein with the rate of 70% > salting selenoprotein with the rate of 100% > salting selenoprotein with the rate of 90% > salting selenoprotein with the rate of 80%> salting selenoprotein with the rate of 50%> salting selenoprotein with the rate of 60% ; therefore, selenoprotein of Cordyceps rich in selenium is a kind of natural resource with good antioxidant activity as well as broad application prospects.
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Lu, Zhuang, Pengzu Wang, Teng Teng, Baoming Shi, Anshan Shan, and Xin Gen Lei. "Effects of Dietary Selenium Deficiency or Excess on Selenoprotein Gene Expression in the Spleen Tissue of Pigs." Animals 9, no. 12 (2019): 1122. http://dx.doi.org/10.3390/ani9121122.
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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.
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Burk, R. F., K. E. Hill, R. Read, and T. Bellew. "Response of rat selenoprotein P to selenium administration and fate of its selenium." American Journal of Physiology-Endocrinology and Metabolism 261, no. 1 (1991): E26—E30. http://dx.doi.org/10.1152/ajpendo.1991.261.1.e26.
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Selenoprotein P is a glycoprotein that contains greater than 60% of the selenium in rat plasma. Physiological experiments were undertaken to gain insight into selenoprotein P function. Selenium-deficient rats were injected with doses of selenium ranging from 25 to 200 micrograms/kg, and the appearance of selenoprotein P was compared with the appearance of glutathione peroxidase activity in plasma and in liver. Selenoprotein P concentration increased to 35% of control by 6 h, whereas glutathione peroxidase activity increased minimally or not at all. Moreover, in rats given 100 and 200 micrograms selenium/kg, selenoprotein P reached 75% of its concentration in control rats at 24 h, whereas glutathione peroxidase activity reached only 6% of control. Cycloheximide pretreatment blocked the appearance of selenoprotein P in response to selenium injection. Male and female rats had similar concentrations of selenoprotein P. Partially purified selenoprotein P and plasma glutathione peroxidase labeled with 75Se were administered intravenously to selenium-deficient and control rats. 75Se given as selenoprotein P disappeared more rapidly from plasma than did 75Se given as glutathione peroxidase. Selenium deficiency did not significantly affect 75Se disappearance from plasma. At 2 h, brain, but not other tissues, took up more 75Se in selenium-deficient rats than in control rats when 75Se was given as selenoprotein P. This suggests that brain has a specific uptake mechanism for selenium given in the form of selenoprotein P. These results demonstrate that several physiological properties distinguish selenoprotein P from glutathione peroxidase. However, they do not clearly indicate its function.
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Squires, Jeffrey E., Ilko Stoytchev, Erin P. Forry, and Marla J. Berry. "SBP2 Binding Affinity Is a Major Determinant in Differential Selenoprotein mRNA Translation and Sensitivity to Nonsense-Mediated Decay." Molecular and Cellular Biology 27, no. 22 (2007): 7848–55. http://dx.doi.org/10.1128/mcb.00793-07.
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ABSTRACT Selenoprotein mRNAs are potential targets for degradation via nonsense-mediated decay due to the presence of in-frame UGA codons that can be decoded as either selenocysteine or termination codons. When UGA decoding is inefficient, as occurs when selenium is limiting, termination occurs at these positions. Based on the predicted exon-intron structure, 14 of the 25 human selenoprotein mRNAs are predicted to be sensitive to nonsense-mediated decay. Among these, sensitivity varies widely, resulting in a hierarchy of preservation or degradation of selenoprotein mRNAs and, thus, of selenoprotein synthesis. Potential factors in dictating the hierarchy of selenoprotein synthesis are the Sec insertion sequence RNA-binding proteins, SBP2 and nucleolin. To investigate the mechanistic basis for this hierarchy and the role of these two proteins, we carried out knockdowns of SBP2 expression and assessed the effects on selenoprotein mRNA levels. We also investigated in vivo binding of selenoprotein mRNAs by SBP2 and nucleolin via immunoprecipitation of the proteins and quantitation of bound mRNAs. We report that SBP2 exhibits strong preferential binding to some selenoprotein mRNAs over others, whereas nucleolin exhibits minimal differences in binding. Thus, SBP2 is a major determinant in dictating the hierarchy of selenoprotein synthesis via differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay.
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Whanger, P. D. "Selenoprotein expression and function—Selenoprotein W." Biochimica et Biophysica Acta (BBA) - General Subjects 1790, no. 11 (2009): 1448–52. http://dx.doi.org/10.1016/j.bbagen.2009.05.010.
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Hayek, Hassan, Gilbert Eriani, and Christine Allmang. "eIF3 Interacts with Selenoprotein mRNAs." Biomolecules 12, no. 9 (2022): 1268. http://dx.doi.org/10.3390/biom12091268.
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The synthesis of selenoproteins requires the co-translational recoding of an in-frame UGASec codon. Interactions between the Selenocysteine Insertion Sequence (SECIS) and the SECIS binding protein 2 (SBP2) in the 3′untranslated region (3′UTR) of selenoprotein mRNAs enable the recruitment of the selenocysteine insertion machinery. Several selenoprotein mRNAs undergo unusual cap hypermethylation and are not recognized by the translation initiation factor 4E (eIF4E) but nevertheless translated. The human eukaryotic translation initiation factor 3 (eIF3), composed of 13 subunits (a-m), can selectively recruit several cellular mRNAs and plays roles in specialized translation initiation. Here, we analyzed the ability of eIF3 to interact with selenoprotein mRNAs. By combining ribonucleoprotein immunoprecipitation (RNP IP) in vivo and in vitro with cross-linking experiments, we found interactions between eIF3 and a subgroup of selenoprotein mRNAs. We showed that eIF3 preferentially interacts with hypermethylated capped selenoprotein mRNAs rather than m7G-capped mRNAs. We identified direct contacts between GPx1 mRNA and eIF3 c, d, and e subunits and showed the existence of common interaction patterns for all hypermethylated capped selenoprotein mRNAs. Differential interactions of eIF3 with selenoprotein mRNAs may trigger specific translation pathways independent of eIF4E. eIF3 could represent a new player in the translation regulation and hierarchy of selenoprotein expression.
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Sunde, Roger A., Anna M. Raines, Kimberly M. Barnes, and Jacqueline K. Evenson. "Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome." Bioscience Reports 29, no. 5 (2009): 329–38. http://dx.doi.org/10.1042/bsr20080146.
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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.
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Fatoki, Toluwase Hezekiah, Omodele Ibraheem, Amos Olalekan Abolaji, and David Morakinyo Sanni. "In Silico study of anticarcinogenic potential of the selenoprotein BthD from Drosophila melanogaster. Identifying the anticancer peptide CRSUR from the conserved region." Nova Biotechnologica et chimica 19, no. 1 (2020): 37–51. http://dx.doi.org/10.36547/nbc.v19i1.576.
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Drosophila melanogaster is used as a model system in biomedical studies. Selenoprotein is the major biological form of selenium in eukaryotes. Selenoproteins are generally involved in catabolic pathways in bacteria and archaea, whereas it participates in anabolic and antioxidant processes in eukaryotic. In this study, anticancer potential of selenoprotein BthD of D. melanogaster was investigated using bioinformatics methods. Results showed that selenoprotein BthD of D. melanogaster may have dual properties as evident by its orthology with selenoprotein H (SelH) of Homo sapiens and conserved domain of fructokinase-like protein 2 of Vitis vinifera. These dual properties were also revealed in the phylogenetic analysis, while further structural modeling showed that selenoprotein BthD possibly exists as homotetramer in the native functional structure. The anticancer property of selenoprotein BthD was proposed to be by synergy of antioxidant or redox activities of thioredoxin and glutathione reductase (TGR) domain and the signaling function of fructokinase-like protein 2 domain both in Golgi apparatus and cytoplasm, through energy deprivation. The anticancer peptide CRSUR was identified from conserved region of selenoprotein BthD, of which its cyclic form showed potential anticancer properties predictively through E3 ubiquitin-protein ligase regulating NF-kappa-B signaling by unleashing cells for spontaneous formation of the ripoptosome.
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Urbano, Teresa, Marco Vinceti, Jessica Mandrioli, et al. "Selenoprotein P Concentrations in the Cerebrospinal Fluid and Serum of Individuals Affected by Amyotrophic Lateral Sclerosis, Mild Cognitive Impairment and Alzheimer’s Dementia." International Journal of Molecular Sciences 23, no. 17 (2022): 9865. http://dx.doi.org/10.3390/ijms23179865.
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Selenoprotein P, a selenium-transporter protein, has been hypothesized to play a role in the etiology of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and Alzheimer’s dementia (AD). However, data in humans are scarce and largely confined to autoptic samples. In this case–control study, we determined selenoprotein P concentrations in both the cerebrospinal fluid (CSF) and the serum of 50 individuals diagnosed with ALS, 30 with AD, 54 with mild cognitive impairment (MCI) and of 30 controls, using sandwich enzyme-linked immunosorbent assay (ELISA) methods. We found a positive and generally linear association between CSF and serum selenoprotein P concentrations in all groups. CSF selenoprotein P and biomarkers of neurodegeneration were positively associated in AD, while for MCI, we found an inverted-U-shaped relation. CSF selenoprotein P concentrations were higher in AD and MCI than in ALS and controls, while in serum, the highest concentrations were found in MCI and ALS. Logistic and cubic spline regression analyses showed an inverse association between CSF selenoprotein P levels and ALS risk, and a positive association for AD risk, while an inverted-U-shaped relation with MCI risk emerged. Conversely, serum selenoprotein P concentrations were positively associated with risk of all conditions but only in their lower range. Overall, these findings indicate some abnormalities of selenoprotein P concentrations in both the central nervous system and blood associated with ALS and neurocognitive disorders, though in different directions. These alterations may reflect either phenomena of etiologic relevance or disease-induced alterations of nutritional and metabolic status.
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Stanishevska, N. V. "Modern concept of biological identification of selenoproteins." Regulatory Mechanisms in Biosystems 9, no. 4 (2018): 553–60. http://dx.doi.org/10.15421/021883.
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Humans possess 25 selenoproteins, approximately half of which are enzymes (selenoenzymes) required for preventing, regulating, or reversing oxidative damage, while others participate in providing calcium metabolism, thyroid hormone maintenance, protein synthesis, cytoskeletal structure etc. This review examines the latest evidences of the biological effects of selenoproteins according to the method of complex analysis of the material. Selenoprotein P promotes insulin resistance in type 2 diabetes, mediates myocardial ischemic-reperfusion injuries and provides protection against disease by reducing chronic oxidative stress. Selenoprotein T is expressed at the endoplasmic reticulum membrane in all cells during development, but is confined to endocrine tissues in adulthood, controls homeostasis of glucose and prevents neurodegeneration by reducing oxidative stress factors. Expression of selenoprotein K is required for efficient Ca2+ flux into melanoma cancer cells, tumour growth and metastasic potential depend on SelK but it suppresses human choriocarcinoma cells. SelK also serves to maintain the normal physiological functions of skeletal muscle. Selenoprotein N deficiency, caused by mutations in the human gene, promotes myopathy characterized by muscle weakness, spinal rigidity, respiratory insufficiency. Sel N participates in normal physiology of skeletal and smooth muscle tissues. Selenoprotein M is located in the endoplasmic reticulum, characterized by high expression in the brain, antioxidative, neuroprotective activity and regulates intracellular Ca2+ levels. Also, the overexpression of SelM was detected in human hepatocellular carcinoma. Selenoprotein S is mentioned as a regulator of ER stress and inflammatory processes. Selenoprotein F controls cell proliferation by the impact on G1period of the cell cycle. Moreover, it is implicated in the pathogenesis of some types of cancer. The Sel F deficiency reduces the migration and invasive ability of the cells. Knockdown of selenoprotein W in rodents leads to increased release of Ca2+, causes oxidative ultramicroscopic injuries of the endoplasmic reticulum and mitochondria ultrastructure, which in turn increases the levels of inflammatory factors. Selenoprotein H is involved in redox regulation, in tumourogenesis. Knockdown of selenoprotein H decreases cellular differentiation and increases proliferation and migration of cells. Selenoproteins U, V, I, O, R are recently identified and their functions are not clearly known. The data analyzed in the review help determine promising directions in the study of the selenoproteins.
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Mattmiller, Sarah, Lorraine Sordillo, and Bradley Carlson. "Selenoprotein activity alters eicosanoid biosynthesis in macrophages (P5042)." Journal of Immunology 190, no. 1_Supplement (2013): 180.4. http://dx.doi.org/10.4049/jimmunol.190.supp.180.4.
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Abstract Selenium (Se) exerts anti-inflammatory properties largely through the activity of antioxidant selenoproteins. However, the effect of reduced selenoprotein activity on the eicosanoid signaling network is unknown. Therefore, the objective of this study was to characterize the biosynthesis of eicosanoids that enhance or resolve inflammation as a function of selenoprotein activity. Macrophages cultured in Se-sufficient or Se-deficient media or macrophages obtained from selenoprotein conditional knockout mice were used to assess inflammatory markers and eicosanoids. Reduced selenoprotein activity significantly increased free radical accumulation, pro-inflammatory cytokines, and cyclooxygenase and lipoxygenase enzyme expression. Reduced selenoprotein activity significantly diminished the production of anti-inflammatory eicosanoids, lipoxin A4 and protectin, hydroxyl eicosanoids from arachidonic acid, and hydroxyl and ketone eicosanoids from linoleic acid (LA). Since LA is a predominant lipid in the western diet and LA-derived metabolites were produced in substantial amounts by macrophages, studies are currently underway to determine the inflammatory effect of the LA ketone, 9oxoODE. Future studies aim at determining if LA eicosanoids are oxidized by lipoxygenases or by non-enzymatic means when selenoprotein activity is reduced. A better understanding of how Se regulates eicosanoid biosynthesis may uncover nutritional intervention strategies to counteract uncontrolled inflammation.
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Persson Moschos, M. "Selenoprotein P." Cellular and Molecular Life Sciences 57, no. 13 (2000): 1836–45. http://dx.doi.org/10.1007/pl00000665.
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Tarek, Marwa, Manal Louis Louka, Eman Khairy, Randa Ali-Labib, Doaa Zakaria Zaky, and Iman F. Montasser. "Role of microRNA-7 and selenoprotein P in hepatocellular carcinoma." Tumor Biology 39, no. 5 (2017): 101042831769837. http://dx.doi.org/10.1177/1010428317698372.
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There is an obvious need to diagnose hepatocellular carcinoma using novel non-invasive and sensitive biomarkers. In this regard, the aim of this study was to evaluate and correlate both relative quantification of microRNA-7 using quantitative real time polymerase chain reaction and quantitative analysis of selenoprotein P using enzyme-linked immunosorbent assay in sera of hepatocellular carcinoma patients, chronic liver disease patients, as well as normal healthy subjects in order to establish a new diagnostic biomarker with a valid non-invasive technique. In addition, this study aimed to investigate whether changes in selenium supply affect microRNA-7 expression and selenoprotein P levels in human hepatocarcinoma cell line (HepG2). The results showed a highly significant decrease in serum microRNA-7 relative quantification values and selenoprotein P levels in malignant group in comparison with benign and control groups. The best cutoff for serum microRNA-7 and selenoprotein P to discriminate hepatocellular carcinoma group from benign and control groups was 0.06 and 4.30 mg/L, respectively. Furthermore, this study showed that changes in selenium supply to HepG2 cell line can alter the microRNA-7 profile and are paralleled by changes in the concentration of its target protein (selenoprotein P). Hence, serum microRNA-7 and selenoprotein P appear to be potential non-invasive diagnostic markers for hepatocellular carcinoma. Moreover, the results suggest that selenium could be used as an anticancer therapy for hepatocellular carcinoma by affecting both microRNA-7 and selenoprotein P.
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Xu, Xue-Ming, Bradley A. Carlson, Robert Irons, et al. "Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis." Biochemical Journal 404, no. 1 (2007): 115–20. http://dx.doi.org/10.1042/bj20070165.
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Selenophosphate synthetase (SelD) generates the selenium donor for selenocysteine biosynthesis in eubacteria. One homologue of SelD in eukaryotes is SPS1 (selenophosphate synthetase 1) and a second one, SPS2, was identified as a selenoprotein in mammals. Earlier in vitro studies showed SPS2, but not SPS1, synthesized selenophosphate from selenide, whereas SPS1 may utilize a different substrate. The roles of these enzymes in selenoprotein synthesis in vivo remain unknown. To address their function in vivo, we knocked down SPS2 in NIH3T3 cells using small interfering RNA and found that selenoprotein biosynthesis was severely impaired, whereas knockdown of SPS1 had no effect. Transfection of SPS2 into SPS2 knockdown cells restored selenoprotein biosynthesis, but SPS1 did not, indicating that SPS1 cannot complement SPS2 function. These in vivo studies indicate that SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals, whereas SPS1 probably has a more specialized, non-essential role in selenoprotein metabolism.
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Baclaocos, Janinah, and John James Mackrill. "Why Multiples of 21? Why does Selenoprotein P Contain Multiple Selenocysteine Residues?" Current Nutraceuticals 1, no. 1 (2020): 42–53. http://dx.doi.org/10.2174/2665978601666200213120929.
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Background: In animals, the 21st amino acid selenocysteine is incorporated into a restricted subset of proteins by recoding of a UGA stop codon. This recoding requires a distinctive selenocysteine insertion sequence in selenoprotein encoding mRNAs, trans-acting factors and in most cases, adequate dietary intake of selenium. With one exception, selenoproteins contain a single selenocysteine, which is incorporated with low translational efficiency. The exception is selenoprotein P, which in some species is predicted to contain as many as 132 selenocysteines and which is considered to play roles in selenium transport and storage. Objective: This study aimed to develop comparative physiological and evolutionary perspectives on the function(s) of selenoprotein P. Method: The review of the literature on the roles of selenoprotein P in diverse animals. Results: Selenoprotein P contains multiple selenocysteines, making it energetically costly to produce. Furthermore, it is often associated with detrimental effects to the animals that produce it. Possible benefits that outweigh these costs include the general storage and transport of selenium; the transport of both toxic and useful metal ions; and specific functions in reproduction and in the nervous system. Conclusion: A probable reconciliation of the negative effects of producing Selenoprotein P is its benefit in terms of promoting reproductive success.
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Mirdayani, Eli, Irma M. Puspitasari, Rizky Abdulah, and Anas Surbanas. "Selenium sebagai Suplemen Terapi Kanker: Sebuah Review." Indonesian Journal of Clinical Pharmacy 8, no. 4 (2019): 301. http://dx.doi.org/10.15416/ijcp.2019.8.4.301.
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Selenium merupakan unsur mikronutrien yang penting bagi kesehatan manusia. Di dalam tubuh, selenium tersebar di semua organ dalam bentuk senyawa terkonjugasi protein (selenoprotein). Senyawa selenoprotein setidaknya mengandung selenosistein yang terdiri dari asam amino sistein. Senyawa selenoprotein pada umumnya bersifat antioksidan. Selenium dihubungkan dengan pengaruhnya terhadap kesehatan manusia termasuk beberapa jenis penyakit kanker. Studi penggunaan suplementasi selenium pada terapi kanker dengan radiasi dan kemoterapi menunjukan peningkatan kadar selenium pada plasma, meningkatkan efektivitas terapi, menurunkan efek samping dari terapi, dan meningkatkan kualitas hidup pasien kanker. Artikel review ini bertujuan untuk menggali dan mengevaluasi pemanfaatan selenium sebagai suplemen terapi pada pasien kanker yang menjalani radioterapi dan kemoterapi. Penelusuran referensi dilakukan melalui database PubMed, Science Direct dan Google Scholar dengan menggunakan kata kunci “Selenium”, “Selenoprotein”, “Selenium and cancer therapy”, “Selenium and Chemotherapy” dan “Selenium and Radiotherapy”. Hasil penelusuran menunjukkan bahwa selenium merupakan unsur mikronutrien yang dapat dikembangkan sebagai komponen suplemen dalam pencegahan penyakit kanker dengan dosis umum 100–400 mikrogram per hari.Kata kunci: Selenium, selenoprotein, terapi kanker Selenium As a Cancer Therapy Supplement: A ReviewAbstractSelenium is an essential element of micronutrients for human health. In the body, selenium is spread in all organs in the form of a conjugated protein compound (selenoprotein). The compound contains at least a selenocysteine consisting of cysteine. Selenoprotein compounds are generally antioxidants. Selenium is linked to its effects on human health including some types of cancer. Studies on the use of selenium supplementation in cancer therapy with radiation and chemotherapy showed elevated plasma selenium levels, increased therapeutic efficacy, reduced side effects, and improved quality of life for cancer patients. This review aimed to investigate and evaluate the utilization of selenium as a supplement in cancer treatment for patients who undergoing radiotherapy and chemotherapy. Database searching was performed through PubMed, Science Direct and Google Scholar using the keywords “Selenium”, “Selenoprotein”, “Selenium and cancer therapy”, “Selenium and Chemotherapy” and “Selenium and Radiotherapy”. The results showed that selenium is a micronutrient that can be developed as a supplement component in the prevention of cancer with a therapeutic dose of 100–400 micrograms per day.Keywords: Cancer therapy, selenium, selenoprotein
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Kemal, Rafi, Ichsan Achmad Fauzi, Sri Nuryati, Wira Wisnu Wardani, and Muhammad Agus Suprayudi. "Evaluation of Selenoprotein Supplementation on Digestibility, Growth, and Health Performance of Pacific White Shrimp Litopenaeus vannamei." Aquaculture Nutrition 2023 (January 5, 2023): 1–12. http://dx.doi.org/10.1155/2023/2008517.
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Selenoprotein is a feed additive that can overcome oxidative stress in intensive Pacific white shrimp (Litopenaeus vannamei) culture. This study evaluated the effects of selenoprotein supplementation at various doses on Pacific white shrimp’s digestibility, growth, and health performance. The experimental design used was a completely randomized design consisting of four feed treatments, namely, control and treatments with selenoprotein supplementation of 2.5, 5, and 7.5 g kg feed-1 with four replications. Shrimps (1.5 g) were reared for 70 days and challenged for 14 days by the bacteria Vibrio parahaemolyticus (107 CFU mL-1). Shrimps used in the digestibility performance evaluation (6.1 g) were reared until sufficient quantities of feces were collected for analysis. Shrimp supplemented with selenoprotein exhibited superior digestibility, growth, and health performance compared to the control ( P < 0.05 ). The use of selenoprotein at a dose of 7.5 g kg of feed-1 (2.72 mg Se kg of feed-1) was considered the most effective for increasing productivity and preventing disease attacks in intensive shrimp culture.
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Huang, W., B. Åkesson, B. G. Svensson, A. Schütz, R. F. Burk, and S. Skerfving. "Selenoprotein P and glutathione peroxidase (EC1·11·1·9) in plasma as indices of selenium status in relation to the intake of fish." British Journal of Nutrition 73, no. 3 (1995): 455–61. http://dx.doi.org/10.1079/bjn19950047.
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Department of Occupational and Environmental Medicine, University of Lund, Lund, Sweden In Sweden fish is considered to be an important source of dietary Se. Therefore Se status was assessed in forty-one middle-aged men with widely varying fish consumption. Glutathione peroxidase (EC1·11·1·9) and selenoprotein P in plasma were measured by radioimmunoassay. Plasma Se among the men increased slightly with increasing consumption of fish, but no such increases in the concentrations of glutathione peroxidase and selenoprotein P in plasma were observed. Moreover, no correlation was found between plasma Se and glutathione peroxidase or selenoprotein P. Instead, glutathione peroxidase was significantly correlated with selenoprotein P (r0·73,P<0·001), indicating that both glutathione peroxidase and selenoprotein P were functional indicators of Se status in this group. The proportion of plasma Se located in glutathione peroxidase decreased with increasing plasma Se. The results suggest that the Se consumed from fish had no apparent effect on the amount of Se incorporated into the functional selenoproteins of plasma. It is concluded that in some cases selenoproteins may be better biological markers of Se status than the total concentration of Se.
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Dery, L., P. Sai Reddy, S. Dery, et al. "Accessing human selenoproteins through chemical protein synthesis." Chemical Science 8, no. 3 (2017): 1922–26. http://dx.doi.org/10.1039/c6sc04123j.
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The human body contains 25 selenoproteins, but challenges in their preparations have prevented biological characterizations thus far. Here we report the first total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW).
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Stanishevska, N. V. "Selenoproteins and their emerging roles in signaling pathways." Regulatory Mechanisms in Biosystems 11, no. 2 (2020): 186–99. http://dx.doi.org/10.15421/022028.
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The functional activity of selenoproteins has a wide range of effects on complex pathogenetic processes, including teratogenesis, immuno-inflammatory, neurodegenerative. Being active participants and promoters of many signaling pathways, selenoproteins support the lively interest of a wide scientific community. This review is devoted to the analysis of recent data describing the participation of selenoproteins in various molecular interactions mediating important signaling pathways. Data processing was carried out by the method of complex analysis. For convenience, all selenoproteins were divided into groups depending on their location and function. Among the group of selenoproteins of the ER membrane, selenoprotein N affects the absorption of Ca2+ by the endoplasmic reticulum mediated by oxidoreductin (ERO1), a key player in the CHOP/ERO1 branch, a pathogenic mechanism that causes myopathy. Another selenoprotein of the ER membrane selenoprotein K binding to the DHHC6 protein affects the IP3R receptor that regulates Ca2+ flux. Selenoprotein K is able to affect another protein of the endoplasmic reticulum CHERP, also appearing in Ca2+ transport. Selenoprotein S, associated with the lumen of ER, is able to influence the VCP protein, which ensures the incorporation of selenoprotein K into the ER membrane. Selenoprotein M, as an ER lumen protein, affects the phosphorylation of STAT3 by leptin, which confirms that Sel M is a positive regulator of leptin signaling. Selenoprotein S also related to luminal selenoproteins ER is a modulator of the IRE1α-sXBP1 signaling pathway. Nuclear selenoprotein H will directly affect the suppressor of malignant tumours, p53 protein, the activation of which increases with Sel H deficiency. The same selenoprotein is involved in redox regulation. Among the cytoplasmic selenoproteins, abundant investigations are devoted to SelP, which affects the PI3K/Akt/Erk signaling pathway during ischemia/reperfusion, is transported into the myoblasts through the plasmalemma after binding to the apoER2 receptor, and into the neurons to the megaline receptor and in general, selenoprotein P plays the role of a pool that stores the necessary trace element and releases it, if necessary, for vital selenoproteins. The thioredoxin reductase family plays a key role in the invasion and metastasis of salivary adenoid cystic carcinoma through the influence on the TGF-β-Akt/GSK-3β pathway during epithelial-mesenchymal transition. The deletion of thioredoxin reductase 1 affects the levels of messengers of the Wnt/β-catenin signaling pathway. No less studied is the glutathione peroxidase group, of which GPX3 is able to inhibit signaling in the Wnt/β-catenin pathway and thereby inhibit thyroid metastasis, as well as suppress protein levels in the PI3K/Akt/c-fos pathway. A key observation is that in cases of carcinogenesis, a decrease in GPX3 and its hypermethylation are almost always found. Among deiodinases, deiodinase 3 acts as a promoter of the oncogenes BRAF, MEK or p38, while stimulating a decrease in the expression of cyclin D1. The dependence of the level of deiodinase 3 on the Hedgehog (SHH) signaling pathway is also noted. Methionine sulfoxide reductase A can compete for the uptake of ubiquitin, reduce p38, JNK and ERK promoters of the MAPK signaling pathway; methionine sulfoxide reductase B1 suppresses MAPK signaling messengers, and also increases PARP and caspase 3.
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Fradejas-Villar, Noelia, Simon Bohleber, Wenchao Zhao, et al. "The Effect of tRNA[Ser]Sec Isopentenylation on Selenoprotein Expression." International Journal of Molecular Sciences 22, no. 21 (2021): 11454. http://dx.doi.org/10.3390/ijms222111454.
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Transfer RNA[Ser]Sec carries multiple post-transcriptional modifications. The A37G mutation in tRNA[Ser]Sec abrogates isopentenylation of base 37 and has a profound effect on selenoprotein expression in mice. Patients with a homozygous pathogenic p.R323Q variant in tRNA-isopentenyl-transferase (TRIT1) show a severe neurological disorder, and hence we wondered whether selenoprotein expression was impaired. Patient fibroblasts with the homozygous p.R323Q variant did not show a general decrease in selenoprotein expression. However, recombinant human TRIT1R323Q had significantly diminished activities towards several tRNA substrates in vitro. We thus engineered mice conditionally deficient in Trit1 in hepatocytes and neurons. Mass-spectrometry revealed that hypermodification of U34 to mcm5Um occurs independently of isopentenylation of A37 in tRNA[Ser]Sec. Western blotting and 75Se metabolic labeling showed only moderate effects on selenoprotein levels and 75Se incorporation. A detailed analysis of Trit1-deficient liver using ribosomal profiling demonstrated that UGA/Sec re-coding was moderately affected in Selenop, Txnrd1, and Sephs2, but not in Gpx1. 2′O-methylation of U34 in tRNA[Ser]Sec depends on FTSJ1, but does not affect UGA/Sec re-coding in selenoprotein translation. Taken together, our results show that a lack of isopentenylation of tRNA[Ser]Sec affects UGA/Sec read-through but differs from a A37G mutation.
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de Jesus, Lucia A., Peter R. Hoffmann, Tanya Michaud, et al. "Nuclear Assembly of UGA Decoding Complexes on Selenoprotein mRNAs: a Mechanism for Eluding Nonsense-Mediated Decay?" Molecular and Cellular Biology 26, no. 5 (2006): 1795–805. http://dx.doi.org/10.1128/mcb.26.5.1795-1805.2006.
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ABSTRACT Recoding of UGA from a stop codon to selenocysteine poses a dilemma for the protein translation machinery. In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding protein of the Sec insertion sequence, SBP2, and the specialized elongation factor, EFsec. We sought to determine the subcellular localization of these selenoprotein synthesis factors in mammalian cells and thus gain insight into how selenoprotein mRNAs might circumvent nonsense-mediated decay. Intriguingly, both EFsec and SBP2 localization differed depending on the cell line but significant colocalization of the two proteins was observed in cells where SBP2 levels were detectable. We identify functional nuclear localization and export signals in both proteins, demonstrate that SBP2 undergoes nucleocytoplasmic shuttling, and provide evidence that SBP2 levels and localization may influence EFsec localization. Our results suggest a mechanism for the nuclear assembly of the selenocysteine incorporation machinery that could allow selenoprotein mRNAs to circumvent nonsense-mediated decay, thus providing new insights into the mechanism of selenoprotein translation.
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Sunde, Roger A., Elaine Paterson, Jacqueline K. Evenson, Kimberly M. Barnes, Julie A. Lovegrove, and Michael H. Gordon. "Longitudinal selenium status in healthy British adults: assessment using biochemical and molecular biomarkers." British Journal of Nutrition 99, S3 (2008): S37—S47. http://dx.doi.org/10.1017/s0007114508006831.
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Human selenium (Se) requirements are currently based on biochemical markers of Se status. In rats, tissue glutathione peroxidase-1 (Gpx1) mRNA levels can be used effectively to determine Se requirements; blood Gpx1 mRNA levels decrease in Se-deficient rats, so molecular biology-based markers have potential for human nutrition assessment. To study the efficacy of molecular biology markers for assessing Se status in humans, we conducted a longitudinal study on 39 subjects (age 45 ± 11) in Reading, UK. Diet diaries (5 day) and blood were obtained from each subject at 2, 8, 17 and 23 weeks, and plasma Se, glutathione peroxidase (Gpx3) enzyme activity, and selenoprotein mRNA levels were determined. There were no significant longitudinal effects on Se biomarkers. Se intake averaged 48 ± 14 μg/d. Plasma Se concentrations averaged 1·13 ± 0·16 μmol/l. Plasma Se v. energy-corrected Se intake (ng Se/kJ/d) was significantly correlated, but neither Gpx3 activity v. Se intake (ng Se/kJ/d) nor Gpx3 activity v. plasma Se was significantly correlated. Collectively, this indicates that subjects were on the plateaus of the response curves. Selenoprotein mRNAs were quantitated in total RNA isolated from whole blood, but mRNA levels for Gpx1, selenoprotein H, and selenoprotein W (all highly regulated by Se in rodents), as well selenoprotein P, Gpx3, and phospholipid hydroperoxide glutathione peroxidase were also not significantly correlated with plasma Se. Thus selenoprotein molecular biomarkers, as well as traditional biochemical markers, are unable to further distinguish differences in Se status in these Se replete subjects. The efficacy of molecular biomarkers to detect Se deficiency needs to be tested in Se-deficient populations.
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Li, Wei, Milton Talukder, Xue-Tong Sun, et al. "Selenoprotein W as a molecular target of d-amino acid oxidase is regulated by d-amino acid in chicken neurons." Metallomics 10, no. 5 (2018): 751–58. http://dx.doi.org/10.1039/c8mt00042e.
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Selenoprotein W (SelW), an important member of the avian selenoprotein family, can combine with d-amino acid oxidase (DAAO). Selenium (Se) can inhibit the toxicity of d-serine and maybe has a detoxifying ability by increasing the expression of SelW and decreasing the activity of DAAO.
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Ramadan, Shadia E., and A. A. Razak. "Selenoprotein inAspergillus terreus." Biological Trace Element Research 18, no. 1 (1988): 171–78. http://dx.doi.org/10.1007/bf02917501.
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Gladyshev, Vadim N., Elias S. Arnér, Marla J. Berry, et al. "Selenoprotein Gene Nomenclature." Journal of Biological Chemistry 291, no. 46 (2016): 24036–40. http://dx.doi.org/10.1074/jbc.m116.756155.
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Jun, Liu, zhengqi Zhang, and Sharon Rozovsky. "The Intrinsically Disordered Membrane Enzymes Selenoprotein S and Selenoprotein K." Biophysical Journal 108, no. 2 (2015): 496a. http://dx.doi.org/10.1016/j.bpj.2014.11.2715.
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Wang, Fu-han, Xiao Peng, Yu Chen, Ying Wang, Mei Yang, and Meng-yao Guo. "Se Regulates the Contractile Ability of Uterine Smooth Musclevia Selenoprotein N, Selenoprotein T, and Selenoprotein Win Mice." Biological Trace Element Research 192, no. 2 (2019): 196–205. http://dx.doi.org/10.1007/s12011-019-1647-4.
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Vindry, Caroline, Olivia Guillin, Philippe E. Mangeot, Théophile Ohlmann, and Laurent Chavatte. "A Versatile Strategy to Reduce UGA-Selenocysteine Recoding Efficiency of the Ribosome Using CRISPR-Cas9-Viral-Like-Particles Targeting Selenocysteine-tRNA[Ser]Sec Gene." Cells 8, no. 6 (2019): 574. http://dx.doi.org/10.3390/cells8060574.
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The translation of selenoprotein mRNAs involves a non-canonical ribosomal event in which an in-frame UGA is recoded as a selenocysteine (Sec) codon instead of being read as a stop codon. The recoding machinery is centered around two dedicated RNA components: The selenocysteine insertion sequence (SECIS) located in the 3′ UTR of the mRNA and the selenocysteine-tRNA (Sec-tRNA[Ser]Sec). This translational UGA-selenocysteine recoding event by the ribosome is a limiting stage of selenoprotein expression. Its efficiency is controlled by the SECIS, the Sec-tRNA[Ser]Sec and their interacting protein partners. In the present work, we used a recently developed CRISPR strategy based on murine leukemia virus-like particles (VLPs) loaded with Cas9-sgRNA ribonucleoproteins to inactivate the Sec-tRNA[Ser]Sec gene in human cell lines. We showed that these CRISPR-Cas9-VLPs were able to induce efficient genome-editing in Hek293, HepG2, HaCaT, HAP1, HeLa, and LNCaP cell lines and this caused a robust reduction of selenoprotein expression. The alteration of selenoprotein expression was the direct consequence of lower levels of Sec-tRNA[Ser]Sec and thus a decrease in translational recoding efficiency of the ribosome. This novel strategy opens many possibilities to study the impact of selenoprotein deficiency in hard-to-transfect cells, since these CRISPR-Cas9-VLPs have a wide tropism.
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Korotkov, Konstantin V., Sergey V. Novoselov, Dolph L. Hatfield, and Vadim N. Gladyshev. "Mammalian Selenoprotein in Which Selenocysteine (Sec) Incorporation Is Supported by a New Form of Sec Insertion Sequence Element." Molecular and Cellular Biology 22, no. 5 (2002): 1402–11. http://dx.doi.org/10.1128/mcb.22.5.1402-1411.2002.
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ABSTRACT Selenocysteine (Sec), the 21st amino acid in protein, is encoded by UGA. The Sec insertion sequence (SECIS) element, which is the stem-loop structure present in 3′ untranslated regions (UTRs) of eukaryotic selenoprotein-encoding genes, is essential for recognition of UGA as a codon for Sec rather than as a stop signal. We now report the identification of a new eukaryotic selenoprotein, designated selenoprotein M (SelM). The 3-kb human SelM-encoding gene has five exons and is located on chromosome 22 but has not been correctly identified by either Celera or the public Human Genome Project. We characterized human and mouse SelM cDNA sequences and expressed the selenoprotein in various mammalian cell lines. The 3" UTR of the human, mouse, and rat SelM-encoding genes lacks a canonical SECIS element. Instead, Sec is incorporated in response to a conserved mRNA structure, in which cytidines are present in place of the adenosines previously considered invariant. Substitution of adenosines for cytidines did not alter Sec incorporation; however, other mutant structures did not support selenoprotein synthesis, demonstrating that this new form of SECIS element is functional. SelM is expressed in a variety of tissues, with increased levels in the brain. It is localized to the perinuclear structures, and its N-terminal signal peptide is necessary for protein translocation.
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Kiledjian, Nora T., Rushvi Shah, Michael B. Vetick, and Paul R. Copeland. "The expression of essential selenoproteins during development requires SECIS-binding protein 2–like." Life Science Alliance 5, no. 5 (2022): e202101291. http://dx.doi.org/10.26508/lsa.202101291.
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The dietary requirement for selenium is based on its incorporation into selenoproteins, which contain the amino acid selenocysteine (Sec). The Sec insertion sequence (SECIS) is an RNA structure found in the 3′ UTR of all selenoprotein mRNAs, and it is required to convert in-frame UGA codons from termination to Sec-incorporating codons. SECIS-binding protein 2 (Sbp2) is required for Sec incorporation, but its paralogue, SECIS-binding protein 2–like (Secisbp2l), while conserved, has no known function. Here we determined the relative roles of Sbp2 and Secisbp2l by introducing CRISPR mutations in both genes in zebrafish. By monitoring selenoprotein synthesis with 75Se labeling during embryogenesis, we found that sbp2−/− embryos still make a select subset of selenoproteins but secisbp2l−/− embryos retain the full complement. Abrogation of both genes completely prevents selenoprotein synthesis and juveniles die at 14 days post fertilization. Embryos lacking Sbp2 are sensitive to oxidative stress and express the stress marker Vtg1. We propose a model where Secisbp2l is required to promote essential selenoprotein synthesis when Sbp2 activity is compromised.
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ÖĞÜT, Selim, Sevgin DEĞİRMENCİOĞLU, Nurten BAHTİYAR, et al. "The Role of Some Selenoproteins in the Etiopathogenesis of Breast Cancer." İstanbul Gelişim Üniversitesi Sağlık Bilimleri Dergisi, no. 17 (August 29, 2022): 381–90. http://dx.doi.org/10.38079/igusabder.1152514.
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Amaç: Meme kanseri, kadınlarda kanser kaynaklı ölümlerde akciğer kanserinden sonra ikinci sırada yer alır. Çeşitli çalışmalarda, selenoproteinlerin kanserogenezin bazı evrelerini baskıladığı ve kanser hücrelerinin çoğalma hızını azalttığı gösterilmiştir. Ancak bu mekanizmalar tam olarak açıklanamamıştır. Kanser tedavisinde radyoterapi, kemoterapiyle birlikte en çok tercih edilen tedavi yöntemlerindendir. Çalışmanın amacı, radyoterapi alan meme kanserli hastaların tedavi öncesi ve sonrası selenoprotein düzeylerindeki değişiklikleri değerlendirerek hastalığın etiyopatogenezine olası etkilerini incelemektir.Yöntem: Çalışmamıza meme kanseri teşhisi konmuş, radyoterapi öncesi ve radyoterapi sonrası örnekleri alınan 35 kadın hasta ile herhangi bir ilaç tedavisi almayan 25 sağlıklı kadın gönüllü dahil edildi. Hasta ve sağlıklı kontrol gruplarını oluşturan bireylerden kan örnekleri alındı. Serum örneklerinde selenoprotein K (Sel-K), selenoprotein W1 (Sel-W1) ve selenoprotein P (Sel-P) düzeyleri ELISA (Enzyme-Linked Immunosorbent Assay) yöntemi ile ölçüldü. İstatistiksel analiz, Wilcoxon ve Mann-Whitney U testleri kullanılarak yapıldı. Hesaplamalar için Statistical Package for the Social Sciences – SPSS 21.0 for Windows (SPSS Inc, Chicago, IL, ABD) kullanıldı. p&lt;0.05, istatistiksel olarak anlamlı bir farkı belirtmek için kabul edildi.Bulgular: Serum Sel-K düzeyleri tedavi öncesi ve kontrol grubu karşılaştırıldığında, tedavi öncesi grupta anlamlı olarak düşük bulundu. Sel- P düzeyleri hem tedavi öncesi hem de tedavi sonrasında kontrol grubu ile karşılaştırıldığında her iki grupta da kontrol grubuna göre düşük bulundu. Sel-W1 düzeylerinde gruplar arasında herhangi bir anlamlılık bulunmadı.Sonuç: Meme kanserinde bazı selenoproteinlerin hastalığın etiyopatogenezinde önemli bir rolü olmakla birlikte daha fazla örneklem grubu ve ileri çalışmalar ile hastalığın progresyonu ve selenoprotein düzeyleri arasındaki ilişkinin araştırılmasına ihtiyaç duyulmaktadır.
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Tverezovska, Iryna I., and Natalia M. Zhelezniakova. "SELENIUM-ASSOCIATED MECHANISMS OF PROGRESSION OF NONALCOHOLIC FATTY LIVER DISEASE IN HYPERTENSIVE PATIENTS." Wiadomości Lekarskie 75, no. 11 (2022): 2671–76. http://dx.doi.org/10.36740/wlek202211121.
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The aim: To determine the role of selenium and Selenoprotein P in the intensification of inflammation processes, deviations of the functional state of the liver and the progression of changes in its parenchyma in patients with NAFLD and hypertension. Material and methods: Study included 100 gender and age matched NAFLD patients: 49 (67.3 % women) hypertensive (main group) and 51 (58.8 % women) non-hypertensive NAFLD patients. 20 individuals (55.0 % women) formed control group. Diagnosis of NAFLD and hypertension was made according to respective guidelines. All patients underwent measurement of liver transferases, selenium, Selenoprotein P, IL-8 and IL-10. Results: In both study groups, ALT and AST levels were significantly predominant in patients with steatohepatitis than steatosis. Increase in IL-8 and IL-10 was found in main study groups but not in subgroup analysis. In hypertensive NAFLD patients with steatosis, ALT correlated with selenium and Selenoprotein P. A direct correlation was between the de Ritis index and IL-8. Selenium correlated with IL-8 but not IL-10. Selenoprotein P correlated inversely with IL-8 and directly with IL-10. Conclusions: Intensification of inflammation and depletion of antioxidant protection under presence of hypertension deepen redox violations in NAFLD patients. Such changes can be only partially compensated by anti-inflammatory and antioxidative activity. Selenium and Selenoprotein P are important substances in progression of NAFLD and should be assessed regarding diagnosis and treatment of NAFLD patients.
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KORPAL, Agnieszka, Katarzyna WOŹNIAK, and Arkadiusz TERMAN. "SELENOPROTEIN P GENE (SEPP1) AS A SELENIUM MARKER CONCENTRATION." Folia Pomeranae Universitatis Technologiae Stetinensis Agricultura, Alimentaria, Piscaria et Zootechnica 328, no. 39 (2016): 117–22. http://dx.doi.org/10.21005/aapz2016.39.3.11.
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Reeves, Mariclair A., Frederick P. Bellinger, and Marla J. Berry. "P2-260: The neuroprotective functions of selenoprotein M and selenoprotein I." Alzheimer's & Dementia 6 (July 2010): S390. http://dx.doi.org/10.1016/j.jalz.2010.05.1310.
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Schriever, Sonja C., Kimberly M. Barnes, Jacqueline K. Evenson, Anna M. Raines, and Roger A. Sunde. "Selenium Requirements Are Higher for Glutathione Peroxidase-1 mRNA than Gpx1 Activity in Rat Testis." Experimental Biology and Medicine 234, no. 5 (2009): 513–21. http://dx.doi.org/10.3181/0812-rm-369.
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Selenium (Se) plays a critical role in testis, sperm, and reproduction, and testis Se levels are remarkably maintained in Se deficiency. In most other tissues, Se levels decrease dramatically as do levels of most selenoproteins and levels of a subset of Se-regulated selenoprotein mRNAs. Because of the recent identification of key molecules in the targeted trafficking of Se to the testis, we examined the hierarchy of Se regulation in testis by determining the dietary Se regulation of the full testis selenoproteome in rats fed graded levels of Se (0 to 0.8 μg Se/g) as Na2SeO3 for 28 d. Se status did not significantly affect testis weight or glutathione peroxidase 4 (Gpx4) activity ( P > 0.05). qRT-PCR analysis of selenoprotein mRNA expression revealed that 21 of the 24 selenoprotein mRNAs and ApoER2 mRNA (the selenoprotein P [Sepp1] receptor) were also not regulated significantly by dietary Se status. In contrast, Gpx1 activity decreased to 28% of Se-adequate levels, and mRNA levels for Gpx1, Sepp1, and Sepw1 (selenoprotein W) decreased significantly in Se-deficient rats to 45, 46, and 55%, respectively, of Se-adequate plateau levels. Overlap of hyperbolic Gpx4 activity and Sepw1 mRNA response curves with testis Se concentration, all with minimum dietary Se requirements <0.016 μg Se/g, showed the priority for synthesis of Gpx4. Higher minimum dietary Se requirements of 0.04 μg Se/g for Gpx1 activity and Sepp1 mRNA, and the even higher minimum dietary Se requirement of 0.08 μg Se/g for Gpx1 mRNA, suggest that the hierarchy of these biomarkers reflects distinct, lower priority pools, cell types, and roles for Se within the testis.
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Moustafa, Mohamed E., Bradley A. Carlson, Muhammad A. El-Saadani, et al. "Selective Inhibition of Selenocysteine tRNA Maturation and Selenoprotein Synthesis in Transgenic Mice Expressing Isopentenyladenosine-Deficient Selenocysteine tRNA." Molecular and Cellular Biology 21, no. 11 (2001): 3840–52. http://dx.doi.org/10.1128/mcb.21.11.3840-3852.2001.
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ABSTRACT Selenocysteine (Sec) tRNA (tRNA[Ser]Sec) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein biosynthesis of overexpressing either the wild type or a mutant tRNA[Ser]Sec lacking the modified base, isopentenyladenosine, in its anticodon loop were examined by introducing multiple copies of the corresponding tRNA[Ser]Sec genes into the mouse genome. Overexpression of wild-type tRNA[Ser]Sec did not affect selenoprotein synthesis. In contrast, the levels of numerous selenoproteins decreased in mice expressing isopentenyladenosine-deficient (i6A−) tRNA[Ser]Sec in a protein- and tissue-specific manner. Cytosolic glutathione peroxidase and mitochondrial thioredoxin reductase 3 were the most and least affected selenoproteins, while selenoprotein expression was most and least affected in the liver and testes, respectively. The defect in selenoprotein expression occurred at translation, since selenoprotein mRNA levels were largely unaffected. Analysis of the tRNA[Ser]Sec population showed that expression of i6A− tRNA[Ser]Sec altered the distribution of the two major isoforms, whereby the maturation of tRNA[Ser]Sec by methylation of the nucleoside in the wobble position was repressed. The data suggest that the levels of i6A− tRNA[Ser]Sec and wild-type tRNA[Ser]Sec are regulated independently and that the amount of wild-type tRNA[Ser]Sec is determined, at least in part, by a feedback mechanism governed by the level of the tRNA[Ser]Sec population. This study marks the first example of transgenic mice engineered to contain functional tRNA transgenes and suggests that i6A−tRNA[Ser]Sec transgenic mice will be useful in assessing the biological roles of selenoproteins.
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Tang, Jiayong, Lei Cao, Gang Jia, et al. "The protective effect of selenium from heat stress-induced porcine small intestinal epithelial cell line (IPEC-J2) injury is associated with regulation expression of selenoproteins." British Journal of Nutrition 122, no. 10 (2019): 1081–90. http://dx.doi.org/10.1017/s0007114519001910.
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AbstractThe present study compared the protective effect of sodium selenite (SS) and selenomethionine (SeMet) on heat stress (HS)-invoked porcine IPEC-J2 cellular damage and integrate potential roles of corresponding selenoprotein. Cells were cultured at 37°C until 80 % confluence and then subjected to four different conditions for 24 h: at 37°C (control), 41·5°C (HS), 41·5°C supplied with 0·42 µmol Se/L SS (SS), or SeMet (SeMet). HS significantly decreased cell viability, up-regulated mRNA and protein levels of heat shock protein 70 (HSP70) and down-regulated mRNA and protein levels of tight junction-related proteins (claudin-1 (CLDN-1) and zonula occludens-1 (ZO-1)). HS-induced cell injury was associated with the up-regulation (P < 0·05) of six inflammation-related genes and fourteen selenoprotein encoding genes and down-regulation (P < 0·05) of two inflammation-related genes and five selenoprotein encoding genes. Compared with the HS group, SS and SeMet supplementation resulted in an increase (P < 0·05) in cell viability, decreased (P < 0·05) mRNA expression of HSP70 and six inflammation-related genes and rescue (P < 0·05) of mRNA and protein levels of CLDN-1 and ZO-1. SS and SeMet supplementation changes the expressions of nineteen selenoprotein encoding genes in cells affected by HS. Both Se supplementation significantly recovered the protein level of glutathione peroxidase-1 and increased selenoprotein P in the IPEC-J2 cells under HS, respectively. In summary, Se supplementation alleviated the negative impact of HS on IPEC-J2 cells, and their cellular protective effect was associated with regulation expression of selenoproteins, and SeMet exhibited a better protective effect.
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SCHOMBURG, Lutz, Ulrich SCHWEIZER, Bettina HOLTMANN, Leopold FLOHÉ, Michael SENDTNER, and Josef KÖHRLE. "Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues." Biochemical Journal 370, no. 2 (2003): 397–402. http://dx.doi.org/10.1042/bj20021853.
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Selenoprotein P (SePP), the major selenoprotein in plasma, has been implicated in selenium transport, selenium detoxification or antioxidant defence. We generated SePP-knockout mice that were viable, but exhibited reduced growth and developed ataxia. Selenium content was elevated in liver, but low in plasma and other tissues, and selenoenzyme activities changed accordingly. Our data reveal that SePP plays a pivotal role in delivering hepatic selenium to target tissues.
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Mohamed, Dalia A., Awis Qurni Sazili, Loh Teck Chwen, and Anjas Asmara Samsudin. "Effect of Microbiota-Selenoprotein on Meat Selenium Content and Meat Quality of Broiler Chickens." Animals 10, no. 6 (2020): 981. http://dx.doi.org/10.3390/ani10060981.
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Selenium (Se) is able to transform from inorganic to organic forms via many bacterial species. This feature is being considered for delivering more bioavailable selenium compounds such as selenocysteine and selenomethionine for human and animal diet. This study investigated the effects of bacterial selenoprotein versus inorganic Se on the carcass characteristics, breast meat selenium content, antioxidant status, and meat quality of broiler chickens. One hundred and eighty chicks were randomly allotted to five treatments of a basal diet supplemented with no Se, sodium selenite, Enterobacter cloacae Selenium (ADS1-Se), Klebsiella pneumoniae-Selenium (ADS2-Se), and Stenotrophomonas maltophilia-Selenium (ADS18-Se). The results showed that bacterial selenoprotein has the ability to deposit more Se in the breast meat compared to sodium selenite. Both Se sources reduced breast meat drip loss, cooking loss, shear force, and 2-thiobarbituric acid reactive substances (TBARS) significantly. It also increased total antioxidant (TAC) and glutathione peroxidase (GSH-Px) in comparison with the negative control. The highest activity of (GSH-Px), catalase (CAT), and superoxide dismutase (SOD) was found in bacterial selenoprotein. In conclusion, bacterial selenoprotein is more efficient than sodium selenite in increasing the breast meat Se deposition and oxidative capacity of broiler chickens. Therefore, it can be effectively used to produce Se-rich meat as a functional food.
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Zhang, Yan, Jiao Jin, Biyan Huang, Huimin Ying, Jie He, and Liang Jiang. "Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective." Biomolecules 12, no. 7 (2022): 917. http://dx.doi.org/10.3390/biom12070917.
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Selenium (Se) is an important trace element that mainly occurs in the form of selenocysteine in selected proteins. In prokaryotes, Se is also required for the synthesis of selenouridine and Se-containing cofactor. A large number of selenoprotein families have been identified in diverse prokaryotic organisms, most of which are thought to be involved in various redox reactions. In the last decade or two, computational prediction of selenoprotein genes and comparative genomics of Se metabolic pathways and selenoproteomes have arisen, providing new insights into the metabolism and function of Se and their evolutionary trends in bacteria and archaea. This review aims to offer an overview of recent advances in bioinformatics analysis of Se utilization in prokaryotes. We describe current computational strategies for the identification of selenoprotein genes and generate the most comprehensive list of prokaryotic selenoproteins reported to date. Furthermore, we highlight the latest research progress in comparative genomics and metagenomics of Se utilization in prokaryotes, which demonstrates the divergent and dynamic evolutionary patterns of different Se metabolic pathways, selenoprotein families, and selenoproteomes in sequenced organisms and environmental samples. Overall, bioinformatics analyses of Se utilization, function, and evolution may contribute to a systematic understanding of how this micronutrient is used in nature.
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Shetty, Sumangala P., Nora T. Kiledjian, and Paul R. Copeland. "The selenoprotein P 3’ untranslated region is an RNA binding protein platform that fine tunes selenocysteine incorporation." PLOS ONE 17, no. 7 (2022): e0271453. http://dx.doi.org/10.1371/journal.pone.0271453.
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Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3’ UTR. Aside from the SECIS, selenoprotein mRNA 3’ UTRs are not conserved between different selenoproteins within a species. In contrast, the 3’-UTR of a given selenoprotein is often conserved across species, which supports the hypothesis that cis-acting elements in the 3’-UTR other than the SECIS exert post-transcriptional control on selenoprotein expression. In order to determine the function of one such SECIS context, we chose to focus on the plasma selenoprotein, SELENOP, which is required to maintain selenium homeostasis as a selenium transport protein that contains 10 Sec residues. It is unique in that its mRNA contains two SECIS elements in the context of a highly conserved 843-nucleotide 3’ UTR. Here we have used RNA affinity chromatography and identified PTBP1 as the major RNA binding protein that specifically interacts with the sequence between the two SECIS elements. We then used CRISPR/Cas9 genome editing to delete two regions surrounding the first SECIS element. We found that these sequences are involved in regulating SELENOP mRNA and protein levels, which are inversely altered as a function of selenium concentrations.
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Haruna, Ken-ichi, Muhammad H. Alkazemi, Yuchen Liu, Dieter Söll, and Markus Englert. "Engineering the elongation factor Tu for efficient selenoprotein synthesis." Nucleic Acids Research 42, no. 15 (2014): 9976–83. http://dx.doi.org/10.1093/nar/gku691.
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Abstract Selenocysteine (Sec) is naturally co-translationally incorporated into proteins by recoding the UGA opal codon with a specialized elongation factor (SelB in bacteria) and an RNA structural signal (SECIS element). We have recently developed a SECIS-free selenoprotein synthesis system that site-specifically—using the UAG amber codon—inserts Sec depending on the elongation factor Tu (EF-Tu). Here, we describe the engineering of EF-Tu for improved selenoprotein synthesis. A Sec-specific selection system was established by expression of human protein O6-alkylguanine-DNA alkyltransferase (hAGT), in which the active site cysteine codon has been replaced by the UAG amber codon. The formed hAGT selenoprotein repairs the DNA damage caused by the methylating agent N-methyl-N′-nitro-N-nitrosoguanidine, and thereby enables Escherichia coli to grow in the presence of this mutagen. An EF-Tu library was created in which codons specifying the amino acid binding pocket were randomized. Selection was carried out for enhanced Sec incorporation into hAGT; the resulting EF-Tu variants contained highly conserved amino acid changes within members of the library. The improved UTu-system with EF-Sel1 raises the efficiency of UAG-specific Sec incorporation to >90%, and also doubles the yield of selenoprotein production.
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Stoytcheva, Zoia, Rosa M. Tujebajeva, John W. Harney, and Marla J. Berry. "Efficient Incorporation of Multiple Selenocysteines Involves an Inefficient Decoding Step Serving as a Potential Translational Checkpoint and RibosomeBottleneck." Molecular and Cellular Biology 26, no. 24 (2006): 9177–84. http://dx.doi.org/10.1128/mcb.00856-06.
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ABSTRACT Selenocysteine is incorporated into proteins via “recoding” of UGA from a stop codon to a sense codon, a process that requires specific secondary structures in the 3′ untranslated region, termed selenocysteine incorporation sequence (SECIS) elements, and the protein factors that they recruit. Whereas most selenoprotein mRNAs contain a single UGA codon and a single SECIS element, selenoprotein P genes encode multiple UGAs and two SECIS elements. We have identified evolutionary adaptations in selenoprotein P genes that contribute to the efficiency of incorporating multiple selenocysteine residues in this protein. The first is a conserved, inefficiently decoded UGA codon in the N-terminal region, which appears to serve both as a checkpoint for the presence of factors required for selenocysteine incorporation and as a“ bottleneck,” slowing down the progress of elongating ribosomes. The second adaptation involves the presence of introns downstream of this inefficiently decoded UGA which confer the potential for nonsense-mediated decay when factors required for selenocysteine incorporation are limiting. Third, the two SECIS elements in selenoprotein P mRNA function with differing efficiencies, affecting both the rate and the efficiency of decoding different UGAs. The implications for how these factors contribute to the decoding of multiple selenocysteine residues are discussed.
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Hou, Qintang, Shi Qiu, Qiong Liu, Jing Tian, Zhangli Hu, and Jiazuan Ni. "Selenoprotein-Transgenic Chlamydomonas reinhardtii." Nutrients 5, no. 3 (2013): 624–36. http://dx.doi.org/10.3390/nu5030624.
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Kaindl, Angela M. "Selenoprotein N Muscular Dystrophy." Journal of Child Neurology 21, no. 4 (2006): 316–20. http://dx.doi.org/10.1177/08830738060210041401.
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Riddihough, Guy. "Clearing out selenoprotein garbage." Science Signaling 8, no. 384 (2015): ec184-ec184. http://dx.doi.org/10.1126/scisignal.aac9401.
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Whanger, P. D. "Selenoprotein W: a review." Cellular and Molecular Life Sciences 57, no. 13 (2000): 1846–52. http://dx.doi.org/10.1007/pl00000666.
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Riddihough, Guy. "Clearing out selenoprotein garbage." Science 349, no. 6243 (2015): 42.15–42. http://dx.doi.org/10.1126/science.349.6243.42-o.
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