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Selenoprotein W, 1

Selenoprotein W, SelW, SEPW1, selenoprotein W,
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein has been shown to function as a glutathione-dependent antioxidant in vivo. Studies in rat suggest that it may play an important role as an antioxidant in the developing brain and embryo. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ethanolaminephosphotransferase, Thioredoxin, gpx1, ACID, phospholipid hydroperoxide glutathione peroxidase
Papers on Selenoprotein W
Identification of a redox-modulatory interaction between selenoprotein W and 14-3-3 protein.
Kim et al., Seoul, South Korea. In Biochim Biophys Acta, Jan 2016
Selenoprotein W (SelW) contains a selenocysteine (Sec, U) in a conserved CXXU motif corresponding to the CXXC redox motif of thioredoxin, suggesting a putative redox function of SelW.
Effect of Inorganic Dietary Selenium Supplementation on Selenoprotein and Lipid Metabolism Gene Expression Patterns in Liver and Loin Muscle of Growing Lambs.
Pierzchała et al., Poland. In Biol Trace Elem Res, Jan 2016
Significant differences were found in the expression of GPX1, GPX2, SEPM, SEPW1, SEP15, SEPGS2, and TXNRD1 in the liver, and GPX1, SEPP1, SEPN1, SEPW1, SEP15, and MSRB1 in the LD muscle between S and C lambs.
Selenoprotein W was Correlated with the Protective Effect of Selenium on Chicken Myocardial Cells from Oxidative Damage.
Xu et al., Harbin, China. In Biol Trace Elem Res, Nov 2015
Selenoprotein W (SelW), one member of the selenoprotein family, plays important roles in the normal function of the heart.
Selenoprotein Genes Exhibit Differential Expression Patterns Between Hepatoma HepG2 and Normal Hepatocytes LO2 Cell Lines.
Wang et al., Chengdu, China. In Biol Trace Elem Res, Oct 2015
Among the genes investigated, 10 selenoprotein genes (Gpx1, Gpx3, Gpx4, Selx, Sepp, Sepw1, Sepn1, Selt, Seli, Selh) and 3 cancer signaling-related genes (Bcl-2A, caspase-3, and P38) were upregulated (P < 0.05), while Selo and Bcl-2B were downregulated (P < 0.05) in hepatoma HepG2 cells compared to LO2 cells.
Selenium Deficiency Affects the mRNA Expression of Inflammatory Factors and Selenoprotein Genes in the Kidneys of Broiler Chicks.
Shan et al., Harbin, China. In Biol Trace Elem Res, Oct 2015
The mRNA levels of 14 selenoprotein genes (Dio1, Dio2, GPx3, Sepp1, SelH, SelI, SelK, Sepn1, SelO, SelW, Sep15, SelT, SelU, and SelS) decreased, and 9 selenoprotein genes (GPx1, GPx2, GPx4, SelPb, Txnrd1, Txnrd2, Txnrd3, SPS2, and SelM) increased in L group (p < 0.05), but the Dio3 and Sepx1 mRNA levels did not change.
Selenoproteins protect against avian nutritional muscular dystrophy by metabolizing peroxides and regulating redox/apoptotic signaling.
Lei et al., Beijing, China. In Free Radic Biol Med, Jun 2015
Compared with the +Se chicks, the -Se chicks had lower (P < 0.05) muscle mRNA levels of Gpx1, Gpx3, Gpx4, Sepp1, Selo, Selk, Selu, Selh, Selm, Sepw1, and Sep15.
Roles of selenoprotein antioxidant protection in zebrafish, Danio rerio, subjected to dietary oxidative stress.
Tocher et al., Stirling, United Kingdom. In Fish Physiol Biochem, Jun 2015
High dietary DHA decreased selenoprotein W expression in muscle and sps2 expression in liver regardless of the dietary Se content.
Selenoprotein W controls epidermal growth factor receptor surface expression, activation and degradation via receptor ubiquitination.
Hawkes et al., Davis, United States. In Biochim Biophys Acta, May 2015
Selenoprotein W (SEPW1) is a highly conserved, diet-regulated 9kDa thioredoxin-like protein required for normal cell cycle progression.
Evaluation of the selenotranscriptome expression in two hepatocellular carcinoma cell lines.
Costantini et al., Napoli, Italy. In Anal Cell Pathol (amst), 2014
Our data showed that in both cells there are three downregulated (DIO1, DIO2, and SELO) and ten upregulated (GPX4, GPX7, SELK, SELM, SELN, SELT, SELV, SEP15, SEPW1, and TrxR1) genes.
Cloning, Sequencing, and Expression of Selenoprotein Transcripts in the Turkey (Meleagris gallopavo).
Evenson et al., Madison, United States. In Plos One, 2014
GPX3 expression was high in all tissues except kidney, GPX1 expression was high in kidney, SEPW1 expression was high in heart, gizzard and muscle, and SELU expression was high in liver.
Delayed cell cycle progression in selenoprotein W-depleted cells is regulated by a mitogen-activated protein kinase kinase 4-p38/c-Jun NH2-terminal kinase-p53 pathway.
Alkan et al., Davis, United States. In J Biol Chem, 2012
SEPW1 silencing increases MKK4, which activates p38gamma, p38delta, and JNK2 to phosphorylate p53 on Ser-33 and cause a transient G(1) arrest.
Selenoproteins in bladder cancer.
Reszka, Łódź, Poland. In Clin Chim Acta, 2012
Data from the Mammalian Gene Collection (MGC) Project clearly showed that highest mRNA expression in human urinary epithelium for TRXR1 (thioredoxin reductase 1), GPX1 (glutathione peroxidase 1), SEP15 (15 kDa selenoprotein), SELT (selenoprotein T) and SEPW1 (selenoprotein W1).
Selenoprotein W depletion induces a p53- and p21-dependent delay in cell cycle progression in RWPE-1 prostate epithelial cells.
Alkan et al., Davis, United States. In J Cell Biochem, 2012
p53 was increased in SEPW1 silenced cells and was inversely correlated with SEPW1 mRNA in cell lines with altered SEPW1 expression.
Delayed cell cycle progression from SEPW1 depletion is p53- and p21-dependent in MCF-7 breast cancer cells.
Alkan et al., Davis, United States. In Biochem Biophys Res Commun, 2011
The present work shows that SEPW1 facilitates the G1 to S-phase transition by down-regulating expression of the cyclin-dependent kinase inhibitor p21
Transcriptional regulation of selenoprotein W by MyoD during early skeletal muscle differentiation.
Kim et al., Seoul, South Korea. In J Biol Chem, 2011
SelW gene was activated by the binding of MyoD to a specific E-box during early skeletal muscle differentiation.
Selenoprotein W depletion in vitro might indicate that its main function is not as an antioxidative enzyme.
Ou-Jv et al., Taiwan. In Biochemistry (mosc), 2010
The main function of SelW in muscle cells is not in the antioxidative system.
Selenoprotein expression and function-selenoprotein W.
Whanger, Corvallis, United States. In Biochim Biophys Acta, 2009
Selenoprotein W (SeW) is a small selenoprotein (85 to 88 amino acids) first identified in sheep suffering from selenium deficiency.
Selenoprotein function and muscle disease.
Allamand et al., Strasbourg, France. In Biochim Biophys Acta, 2009
Two selenoproteins have mainly been investigated in muscle, namely SelW and SelN.
Selenoproteins and maternal nutrition.
Zervas et al., Athens, Greece. In Comp Biochem Physiol B Biochem Mol Biol, 2008
Sel include but not limited to glutathione peroxidases (GPx1-GPx6), thioredoxin reductases (TrxR1-TrxR3), iodothyronine deiodinases (ID1-ID3), selenophosphate synthetase 2 (SPS2), 15-kDa Sel (Sel15), SelH, SelI, SelK, SelM, SelN, SelO, SelP, SelR, SelS, SelT, SelV, SelW, as well as the 15-kDa Sel (Fep15), SelJ and SelU found in fish.
The facts and controversies about selenium.
Cepelak et al., Zagreb, Croatia. In Acta Pharm, 2004
Selenoproteins are comprised of four glutathione peroxidases, three iodothyronine deiodinases, three thioredoxin reductases, selenoprotein P, selenoprotein W and selenophosphate synthetase.
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