Acknowledgement
Supported by : Korea Research Foundation
References
- Aachmann, F.L., Fomenko, D.E., Soragni, A., Gladyshev, V.N., and Dikiy, A. (2007). Structural analysis of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins. J. Biol. Chem. 282, 37036-37044 https://doi.org/10.1074/jbc.M705410200
- Allan, C.B., Lacourciere, G.M., and Stadtman, T.C. (1999). Responsiveness of selenoproteins to dietary selenium. Annu. Rev. Nutr. 19, 1-16 https://doi.org/10.1146/annurev.nutr.19.1.1
- Beilstein, M.A., Vendeland, S.C., Barofsky, E., Jensen, O.N., and Whanger, P.D. (1996). Selenoprotein W of rat muscle binds glutathione and an unknown small molecular weight moiety. J. Inorg. Biochem. 61, 117-124 https://doi.org/10.1016/0162-0134(95)00045-3
- Berry, M.J., Banu, L., Chen, Y.Y., Mandel, S.J., Kieffer, J.D., Harney, J.W., and Larsen, P.R. (1991). Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region. Nature 353, 273-276 https://doi.org/10.1038/353273a0
- Brigelius-Flohe, R. (1999). Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 27, 951-965 https://doi.org/10.1016/S0891-5849(99)00173-2
- Burk, R.F., and Hill, K.E. (2005). Selenoprotein P: an extracellular protein with unique physical characteristics and a role in selenium homeostasis. Annu. Rev. Nutr. 25, 215-235 https://doi.org/10.1146/annurev.nutr.24.012003.132120
- Cohen, G. (1994). Enzymatic/nonenzymatic sources of oxyradicals and regulation of antioxidant defenses. Ann. N Y Acad. Sci. 738, 8-14
- Cone, J.E., Del Rio, R.M., Davis, J.N., and Stadtman, T.C. (1976). Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety. Proc. Natl. Acad. Sci. USA 73, 2659-2663 https://doi.org/10.1073/pnas.73.8.2659
- Dikiy, A., Novoselov, S.V., Fomenko, D.E., Sengupta, A., Carlson, B.A., Cerny, R.L., Ginalski, K., Grishin, N.V., Hatfield, D.L., and Gladyshev, V.N. (2007). SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry 46, 6871-6882 https://doi.org/10.1021/bi602462q
- Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., and Krol, A. (2000). Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J. 19, 4796-4805 https://doi.org/10.1093/emboj/19.17.4796
- Ferreiro, A., Quijano-Roy, S., Pichereau, C., Moghadaszadeh, B., Goemans, N., Bonnemann, C., Jungbluth, H., Straub, V., Villa nova, M., Leroy, J.P., et al. (2002). Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am. J. Hum. Genet. 71, 739-749 https://doi.org/10.1086/342719
- Flohe, L., Gunzler, W.A., and Schock, H.H. (1973). Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32, 132-134 https://doi.org/10.1016/0014-5793(73)80755-0
-
Grumolato, L., Ghzili, H., Montero-Hadjadje, M., Gasman, S., Lesage, J., Tanguy, Y., Galas, L., Ait-Ali, D., Leprince, J., Guerineau, N.C., et al. (2008). Selenoprotein T is a PACAP-regulated gene involved in intracellular
$Ca^{2+}$ mobilization and neuroendocrine secretion. FASEB J. 22, 1756-1768 https://doi.org/10.1096/fj.06-075820 - Gu, Q.P., Beilstein, M.A., Barofsky, E., Ream, W., and Whanger, P.D. (1999). Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle. Arch. Biochem. Biophys. 361, 25-33 https://doi.org/10.1006/abbi.1998.0949
- Gu, Q.P., Sun, Y., Ream, L.W., and Whanger, P.D. (2000). Selenoprotein W accumulates primarily in primate skeletal muscle, heart, brain and tongue. Mol. Cell. Biochem. 204, 49-56 https://doi.org/10.1023/A:1007065829068
- Hill, K.E., McCollum, G.W., Boeglin, M.E., and Burk, R.F. (1997). Thioredoxin reductase activity is decreased by selenium deficiency. Biochem. Biophys. Res. Commun. 234, 293-295 https://doi.org/10.1006/bbrc.1997.6618
- Hubert, N., Walczak, R., Carbon, P., and Krol, A. (1996). A protein binds the selenocysteine insertion element in the 3′-UTR of mammalian selenoprotein mRNAs. Nucleic Acids Res. 24, 464-469 https://doi.org/10.1093/nar/24.3.464
- Jeong, D., Kim, T.S., Chung, Y.W., Lee, B.J., and Kim, I.Y. (2002). Selenoprotein W is a glutathione-dependent antioxidant in vivo. FEBS Lett. 517, 225-228 https://doi.org/10.1016/S0014-5793(02)02628-5
- Jeong, D.W., Kim, E.H., Kim, T.S., Chung, Y.W., Kim, H., and Kim, I.Y. (2004). Different distributions of selenoprotein W and thioredoxin during postnatal brain development and embryogenesis. Mol. Cells 17, 156-159
- Kim, H.Y., and Gladyshev, V.N. (2007). Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem. J. 407, 321-329 https://doi.org/10.1042/BJ20070929
- Korotkov, K.V., Novoselov, S.V., Hatfield, D.L., and Gladyshev, V.N. (2002). Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element. Mol. Cell. Biol. 22, 1402-1411 https://doi.org/10.1128/MCB.22.5.1402-1411.2002
- Kryukov, G.V., Castellano, S., Novoselov, S.V., Lobanov, A.V., Zehtab, O., Guigo, R., and Gladyshev, V.N. (2003). Characterization of mammalian selenoproteomes. Science 300, 1439-1443 https://doi.org/10.1126/science.1083516
- Kumaraswamy, E., Korotkov, K.V., Diamond, A.M., Gladyshev, V.N., and Hatfield, D.L. (2002). Genetic and functional analysis of mammalian Sep15 selenoprotein. Methods Enzymol. 347, 187-197 https://doi.org/10.1016/S0076-6879(02)47017-6
- Lee, B.J., Worland, P.J., Davis, J.N., Stadtman, T.C., and Hatfield, D.L. (1989). Identification of a selenocysteyl-tRNA(Ser) in mammalian cells that recognizes the nonsense codon, UGA. J. Biol. Chem. 264, 9724-9727
- Loflin, J., Lopez, N., Whanger, P.D., and Kioussi, C. (2006). Selenoprotein W during development and oxidative stress. J. Inorg. Biochem. 100, 1679-1684 https://doi.org/10.1016/j.jinorgbio.2006.05.018
- Lovell, M.A., Xie, C., Gabbita, S.P., and Markesbery, W.R. (2000). Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain. Free Radic. Biol. Med. 28, 418-427 https://doi.org/10.1016/S0891-5849(99)00258-0
- Moghadaszadeh, B., Petit, N., Jaillard, C., Brockington, M., Roy, S.Q., Merlini, L., Romero, N., Estournet, B., Desguerre, I., Chaigne, D.I et al. (2001). Mutations in SEPN1 cause congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Nat. Genet. 29, 17-18 https://doi.org/10.1038/ng713
- Moon, I.S., Cho, S.J., Lee, H., Seog, D.H., Jung, Y.W., Jin, I., and Walikonis, R. (2008). Upregulation by KCl treatment of eukaryotic translation elongation factor 1A (eEF1A) mRNA in the dendrites of cultured rat hippocampal neurons. Mol. Cells 25, 538-544
- Mustacich, D., and Powis, G. (2000). Thioredoxin reductase. Biochem. J. 346 Pt 1, 1-8 https://doi.org/10.1042/bj3460001
- Niethammer, M., Smith, D.S., Ayala, R., Peng, J., Ko, J., Lee, M.S., Morabito, M., and Tsai, L.H. (2000). NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein. Neuron 28, 697-711 https://doi.org/10.1016/S0896-6273(00)00147-1
- Novoselov, S.V., Kryukov, G.V., Xu, X.M., Carlson, B.A., Hatfield, D.L., and Gladyshev, V.N. (2007). Selenoprotein H is a nucleolar thioredoxin-like protein with a unique expression pattern. J. Biol. Chem. 282, 11960-11968 https://doi.org/10.1074/jbc.M701605200
- Pellmar, T.C. (1987). Peroxide alters neuronal excitability in the CA1 region of guinea-pig hippocampus in vitro. Neuroscience 23, 447-456 https://doi.org/10.1016/0306-4522(87)90068-6
- Petit, N., Lescure, A., Rederstorff, M., Krol, A., Moghadaszadeh, B., Wewer, U.M., and Guicheney, P. (2003). Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern. Hum. Mol. Genet. 12, 1045-1053 https://doi.org/10.1093/hmg/ddg115
- Rice, M.E. (2000). Ascorbate regulation and its neuroprotective role in the brain. Trends Neurosci. 23, 209-216 https://doi.org/10.1016/S0166-2236(99)01543-X
- Rotruck, J.T., Pope, A.L., Ganther, H.E., Swanson, A.B., Hafeman, D.G., and Hoekstra, W.G. (1973). Selenium: biochemical role as a component of glutathione peroxidase. Science 179, 588-590 https://doi.org/10.1126/science.179.4073.588
- Schweizer, U., Brauer, A.U., Kohrle, J., Nitsch, R., and Savaskan, N.E. (2004). Selenium and brain function: a poorly recognized liaison. Brain Res. Brain Res. Rev. 45, 164-178 https://doi.org/10.1016/j.brainresrev.2004.03.004
- Trepanier, G., Furling, D., Puymirat, J., and Mirault, M.E. (1996). Immunocytochemical localization of seleno-glutathione peroxidase in the adult mouse brain. Neuroscience 75, 231-243 https://doi.org/10.1016/0306-4522(96)00222-9
- Tujebajeva, R.M., Copeland, P.R., Xu, X.M., Carlson, B.A., Harney, J.W., Driscoll, D.M., Hatfield, D.L., and Berry, M.J. (2000). Decoding apparatus for eukaryotic selenocysteine insertion. EMBO Rep. 1, 158-163 https://doi.org/10.1093/embo-reports/kvd033
- Vendeland, S.C., Beilstein, M.A., Chen, C.L., Jensen, O.N., Barofsky, E., and Whanger, P.D. (1993). Purification and properties of selenoprotein W from rat muscle. J. Biol. Chem. 268, 17103-17107
- Yeh, J.Y., Beilstein, M.A., Andrews, J.S., and Whanger, P.D. (1995). Tissue distribution and influence of selenium status on levels of selenoprotein W. FASEB J. 9, 392-396 https://doi.org/10.1096/fasebj.9.5.7896009
- Yeh, J.Y., Gu, Q.P., Beilstein, M.A., Forsberg, N.E., and Whanger, P.D. (1997a). Selenium influences tissue levels of selenoprotein W in sheep. J. Nutr. 127, 394-402 https://doi.org/10.1093/jn/127.3.394
- Yeh, J.Y., Vendeland, S.C., Gu, Q., Butler, J.A., Ou, B.R., and Whanger, P.D. (1997b). Dietary selenium increases selenoprotein W levels in rat tissues. J. Nutr. 127, 2165-2172 https://doi.org/10.1093/jn/127.11.2165
- Zinoni, F., Birkmann, A., Stadtman, T.C., and Bock, A. (1986). Nucleotide sequence and expression of the selenocysteinecontaining polypeptide of formate dehydrogenase (formatehydrogen- lyase-linked) from Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 4650-4654 https://doi.org/10.1073/pnas.83.13.4650
Cited by
- Transcriptional Regulation of Selenoprotein W by MyoD during Early Skeletal Muscle Differentiation vol.285, pp.52, 2009, https://doi.org/10.1074/jbc.m110.152934
- Effects of Dietary Selenium on Selenoprotein W Gene Expression in the Chicken Immune Organs vol.144, pp.1, 2011, https://doi.org/10.1007/s12011-011-9062-5
- The PACAP-Regulated Gene Selenoprotein T Is Highly Induced in Nervous, Endocrine, and Metabolic Tissues during Ontogenetic and Regenerative Processes vol.152, pp.11, 2009, https://doi.org/10.1210/en.2011-1246
- Characterization and expression of chicken selenoprotein W vol.24, pp.2, 2009, https://doi.org/10.1007/s10534-010-9401-6
- Effects of Chicken Selenoprotein W on H2O2-Induced Apoptosis in CHO-K1 Cells vol.147, pp.1, 2009, https://doi.org/10.1007/s12011-011-9311-7
- The Expression of Chicken Selenoprotein W, Selenocysteine-synthase (SecS), and Selenophosphate Synthetase-1 (SPS-1) in CHO-K1 Cells vol.148, pp.1, 2012, https://doi.org/10.1007/s12011-012-9346-4
- Effects of Selenoprotein W gene expression by selenium involves regulation of mRNA stability in chicken embryos neurons vol.25, pp.2, 2009, https://doi.org/10.1007/s10534-012-9517-y
- Antioxidative role of selenoprotein W in oxidant-induced chicken splenic lymphocyte death vol.27, pp.2, 2009, https://doi.org/10.1007/s10534-014-9708-9
- SelW regulates inflammation-related cytokines in response to H2O2in Se-deficient chicken liver vol.5, pp.47, 2015, https://doi.org/10.1039/c4ra16055j
- Definition of transcriptome-based indices for quantitative characterization of chemically disturbed stem cell development: introduction of the STOP-Tox ukn and STOP-Tox ukk tes vol.91, pp.2, 2009, https://doi.org/10.1007/s00204-016-1741-8
- Gene Silencing of Selenoprotein K Induces Inflammatory Response and Activates Heat Shock Proteins Expression in Chicken Myoblasts vol.180, pp.1, 2009, https://doi.org/10.1007/s12011-017-0979-1
- SelW protects against H2O2-induced liver injury in chickens via inhibiting inflammation and apoptosis vol.7, pp.25, 2009, https://doi.org/10.1039/c6ra27911b
- Selenoprotein W as a molecular target of D-amino acid oxidase is regulated by D-amino acid in chicken neurons vol.10, pp.5, 2009, https://doi.org/10.1039/c8mt00042e
- Selenoprotein W deficiency does not affect oxidative stress and insulin sensitivity in the skeletal muscle of high-fat diet-fed obese mice vol.317, pp.6, 2009, https://doi.org/10.1152/ajpcell.00064.2019
- Selenium and Neurological Diseases: Focus on Peripheral Pain and TRP Channels vol.18, pp.6, 2009, https://doi.org/10.2174/1570159x18666200106152631