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Journal articles on the topic 'Selenoprote'

Author: Grafiati

Published: 18 May 2024

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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

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2

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

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3

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

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4

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 microgram

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5

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 selenopr

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6

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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7

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 selecti

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8

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

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9

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 do

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10

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 posi

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11

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 redu

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12

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 a

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13

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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14

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 inve

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15

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 selenopro

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16

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

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17

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 efek

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18

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

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19

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 pla

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20

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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21

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 divi

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22

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 activit

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23

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

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24

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 pl

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25

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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26

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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27

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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28

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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29

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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30

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 p

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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 Proj

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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

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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 i

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34

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

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35

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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36

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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37

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

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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 mi

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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

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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 clo

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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 a

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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 fu

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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 (h

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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 selenocystein

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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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