Dietary factors in the regulation of selenoprotein biosynthesis

Dietary Modulation of Cell Signaling Pathways

Volumn , Issue , 2008, Pages 251-272

  Brigelius Flohé, Regina ^a   Banning, Antje ^a  

^a GERMAN INSTITUTE OF HUMAN NUTRITION   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84871711718     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (120)

1. Kryukov, G.V., Castellano, S., Novoselov, S.V., Lobanov, A.V., Zehtab, O., Guigó, R., and Gladyshev, V.N., Characterization of mammalian selenoproteomes, Science, 300, 1439, 2003.
2. Hatfield, D.L. and Gladyshev, V.N., How selenium has altered our understanding of the genetic code, Mol. Cell. Biol., 22, 3565, 2002.
3. Driscoll, D.M. and Copeland, P.R., Mechanism and regulation of selenoprotein synthesis, Annu. Rev. Nutr., 23, 17, 2003.
4. Chavatte, L., Brown, B.A., and Driscoll, D.M., Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes, Nat. Struct. Mol. Biol., 12, 408, 2005.
5. Kinzy, S.A., Caban, K., and Copeland, P.R., Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals, Nucleic Acids Res., 33, 5172, 2005.
6. Brigelius-Flohé, R., Tissue-specific functions of individual glutathione peroxidases, Free Radic. Biol. Med., 27, 951, 1999.
7. Allan, C.B., Lacourciere, G.M., and Stadtman, T.C., Responsiveness of selenoproteins to dietary selenium, Annu. Rev. Nutr., 19, 1, 1999.
8. Sun, X., Moriarty, P.M., and Maquat, L.E., Nonsense-mediated decay of glutathione peroxidase 1 mRNA in the cytoplasm depends on intron position, EMBO J., 19, 4734, 2000.
9. Weiss, S.L. and Sunde, R.A., Cis-acting elements are required for selenium regulation of glutathione peroxidase-1 mRNA levels, RNA, 4, 816, 1998.
10. Müller, C., Wingler, K., and Brigelius-Flohé, R., 3′UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stabilities and selenocysteine incorporation efficiency, Biol. Chem., 384, 11, 2003.
11. Copeland, P.R. and Driscoll, D.M., Purification, redox sensitivity, and RNA binding properties of SECIS-binding protein 2, a protein involved in selenoprotein biosynthesis, J. Biol. Chem., 274, 25447, 1999.
12. Lescure, A., Allmang, C., Yamada, K., Carbon, P., and Krol, A., cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2, Gene, 291, 279, 2002.
13. Fletcher, J.E., Copeland, P.R., Driscoll, D.M., and Krol, A., The selenocysteine incorporation machinery. Interactions between the SECIS RNA and the SECISbinding protein SBP2, RNA, 7, 1442, 2001.
14. de Jesus, L.A., Hoffmann, P.R., Michaud, T., Forry, E.P., Small-Howard, A., Stillwell, R.J., Morozova, N., Harney, J.W., and Berry, M.J., Nuclear assembly of UGA decoding complexes on selenoprotein mRNAs: a mechanism for eluding nonsense-mediated decay? Mol. Cell. Biol., 26, 1795, 2006.
15. Shen, Q., Fan, L., and Newburger, P.E., Nuclease sensitive element binding protein 1 associates with the selenocysteine insertion sequence and functions in mammalian selenoprotein translation, J. Cell. Physiol., 207, 775, 2006.
16. Thanbichler, M. and Böck, A., The function of SECIS RNA in translational control of gene expression in Escherichia coli, EMBO J., 21, 6925, 2002.
17. Neve, J., Human selenium supplementation as assessed by changes in blood selenium concentration and glutathione peroxidase activity, J. Trace Elem. Med. Biol., 9, 65, 1995.
18. Xia, Y., Hill, K.E., Byrne, D.W., Xu, J., and Burk, R.F., Effectiveness of selenium supplements in a low-selenium area of China, Am. J. Clin. Nutr., 81, 829, 2005.
19. Ip, C., Lessons from basic research in selenium and cancer prevention, J. Nutr., 128, 1845, 1998.
20. Combs, G.F., Jr., Clark, L.C., and Turnbull, B.W., An analysis of cancer prevention by selenium, Biofactors, 14, 153, 2001.
21. Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E., and Bock, A., In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product, Proc. Natl. Acad. Sci. USA, 87, 543, 1990.
22. Lacourciere, G.M., Biosynthesis of selenophosphate, Biofactors, 10, 237, 1999.
23. (Ser)Sec kinase, Proc. Natl. Acad. Sci. USA, 101, 12848, 2004.
24. Soda, K., Esaki, N., Nakamura, T., Karai, N., Chocat, P., and Tanaka, H., Selenocysteine beta-lyase: a novel pyridoxal enzyme, Prog. Clin. Biol. Res., 144A, 319, 1984.
25. Combs, G.F., Jr., Selenium in foods, Adv. Food Res., 32, 85, 1988.
26. Birringer, M., Pilawa, S., and Flohé, L., Trends in selenium biochemistry, Nat. Prod. Rep., 19, 693, 2002.
27. Kotrebai, M., Birringer, M., Tyson, J.F., Block, E., and Uden, P.C., Selenium speciation in enriched and natural samples by HPLC-ICP-MS and HPLC-ESI-MS with perfluorinated carboxylic acid ion-pairing agents, Analyst, 125, 71, 2000.
28. Kotrebai, M., Birringer, M., Tyson, J.F., Block, E., and Uden, P.C., Identification of the principal selenium compounds in selenium-entriched natural sample extracts by ion-pair liquid chromatography with inductively coupled plasma- and electrospray ionization-mass spectrometric detection, Anal. Commun., 36, 249, 1999.
29. Arnault, I. and Auger, J., Seleno-compounds in garlic and onion, J. Chromatogr. A., 1112, 23, 2006.
30. Ip, C., Thompson, H.J., Zhu, Z., and Ganther, H.E., In vitro and in vivo studies of methylseleninic acid: evidence that a monomethylated selenium metabolite is critical for cancer chemoprevention, Cancer Res., 60, 2882, 2000.
31. Ip, C. and Ganther, H.E., Activity of methylated forms of selenium in cancer prevention, Cancer Res., 50, 1206, 1990.
32. Ip, C., Hayes, C., Budnick, R.M., and Ganther, H.E., Chemical form of selenium, critical metabolites, and cancer prevention, Cancer Res., 51, 595, 1991.
33. Ip, C., Zhu, Z., Thompson, H.J., Lisk, D., and Ganther, H.E., Chemoprevention of mammary cancer with Se-allylselenocysteine and other selenoamino acids in the rat, Anticancer Res., 19, 2875, 1999.
34. Rayman, M.P., Selenium in cancer prevention: a review of the evidence and mechanism of action, Proc. Nutr. Soc., 64, 527, 2005.
35. Ganther, H.W. and Lawrence, J.R., Chemical transformations of selenium in living organisms. Improved forms of selenium for cancer prevention, Tetrahedron, 53, 12299, 1997.
36. ‘t Hoen, P.A., Rooseboom, M., Bijsterbosch, M.K., van Berkel, T.J., Vermeulen, N.P., and Commandeur, J.N., Induction of glutathione-S-transferase mRNA levels by chemopreventive selenocysteine Se-conjugates, Biochem. Pharmacol., 63, 1843, 2002.
37. Lu, J. and Jiang, C., Selenium and cancer chemoprevention: hypotheses integrating the actions of selenoproteins and selenium metabolites in epithelial and non-epithelial target cells, Antioxid. Redox Signal., 7, 1715, 2005.
38. Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., Yamamoto, M., and Nabeshima, Y., An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements, Biochem. Biophys. Res. Commun., 236, 313, 1997.
39. Dinkova-Kostova, A.T., Holtzclaw, W.D., Cole, R.N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., and Talalay, P., Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants, Proc. Natl. Acad. Sci. USA, 99, 11908, 2002.
40. Dinkova-Kostova, A.T., Holtzclaw, W.D., and Wakabayashi, N., Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein, Biochemistry, 44, 6889, 2005.
41. Kang, M.I., Kobayashi, A., Wakabayashi, N., Kim, S.G., and Yamamoto, M., Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes, Proc. Natl. Acad. Sci. USA, 101, 2046, 2004.
42. Chen, C. and Kong, A.N., Dietary chemopreventive compounds and ARE/EpRE signaling, Free Radic. Biol. Med., 36, 1505, 2004.
43. Prochaska, H.J., De Long, M.J., and Talalay, P., On the mechanisms of induction of cancer-protective enzymes: a unifying proposal, Proc. Natl. Acad. Sci. USA, 82, 8232, 1985.
44. Talalay, P., De Long, M.J., and Prochaska, H.J., Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis, Proc. Natl. Acad. Sci. USA, 85, 8261, 1988.
45. Spencer, S.R., Xue, L.A., Klenz, E.M., and Talalay, P., The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations, Biochem. J., 273, 711, 1991.
46. Gromer, S., Urig, S., and Becker, K., The thioredoxin system-from science to clinic, Med. Res. Rev., 24, 40, 2004.
47. Zhong, L., Arner, E.S., Ljung, J., Aslund, F., and Holmgren, A., Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue, J. Biol. Chem., 273, 8581, 1998.
48. Holmgren, A., Thioredoxin, Annu. Rev. Biochem., 54, 237, 1985.
49. Liu, H., Nishitoh, H., Ichijo, H., and Kyriakis, J.M., Activation of apoptosis signalregulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin, Mol. Cell. Biol., 20, 2198, 2000.
50. Ueda, S., Masutani, H., Nakamura, H., Tanaka, T., Ueno, M., and Yodoi, J., Redox control of cell death, Antioxid. Redox Signal., 4, 405, 2002.
51. Yamauchi, A., Masutani, H., Tagaya, Y., Wakasugi, N., Mitsui, A., Nakamura, H., Inamoto, T., Ozawa, K., and Yodoi, J., Lymphocyte transformation and thiol compounds; the role of ADF/thioredoxin as an endogenous reducing agent, Mol. Immunol., 29, 263, 1992.
52. Hofmann, B., Hecht, H.J., and Flohé, L., Peroxiredoxins, Biol. Chem., 383, 347, 2002.
53. Zhang, J., Svehlikova, V., Bao, Y., Howie, A.F., Beckett, G.J., and Williamson, G., Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation, Carcinogenesis, 24, 497, 2003.
54. Hintze, K.J., Wald, K.A., Zeng, H., Jeffery, E.H., and Finley, J.W., Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element, J. Nutr., 133, 2721, 2003.
55. Hintze, K.J., Keck, A.S., Finley, J.W., and Jeffery, E.H., Induction of hepatic thioredoxin reductase activity by sulforaphane, both in Hepa1c1c7 cells and in male Fisher 344 rats, J. Nutr. Biochem., 14, 173, 2003.
56. Wang, W., Wang, S., Howie, A.F., Beckett, G.J., Mithen, R., and Bao, Y., Sulforaphane, erucin, and iberin up-regulate thioredoxin reductase 1 expression in human MCF-7 cells, J. Agric. Food Chem., 53, 1417, 2005.
57. Hayes, J.D. and McMahon, M., Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention, Cancer Lett., 174, 103, 2001.
58. Eftekharpour, E., Holmgren, A., and Juurlink, B.H., Thioredoxin reductase and glutathione synthesis is upregulated by t-butylhydroquinone in cortical astrocytes but not in cortical neurons, Glia, 31, 241, 2000.
59. Kim, Y.C., Yamaguchi, Y., Kondo, N., Masutani, H., and Yodoi, J., Thioredoxindependent redox regulation of the antioxidant responsive element (ARE) in electrophile response, Oncogene, 22, 1860, 2003.
60. Berggren, M., Gallegos, A., Gasdaska, J.R., Gasdaska, P.Y., Warneke, J., and Powis, G., Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia, Anticancer Res., 16, 3459, 1996.
61. Lincoln, D.T., Ali Emadi, E.M., Tonissen, K.F., and Clarke, F.M., The thioredoxinthioredoxin reductase system: over-expression in human cancer, Anticancer Res., 23, 2425, 2003.
62. Becker, K., Gromer, S., Schirmer, R.H., and Muller, S., Thioredoxin reductase as a pathophysiological factor and drug target, Eur. J. Biochem., 267, 6118, 2000.
63. Flohé, L. and Brigelius-Flohé, R., Selenoproteins of the glutathione system, in Selenium: Its Molecular Biology and Role in Human Health, Hatfield, D.L., Ed., Kluwer Academic Publishers, Boston, 161-172, 2006.
64. Cheng, W.H., Ho, Y.S., Valentine, B.A., Ross, D.A., Combs, G.F., Jr., and Lei, X.G., Cellular glutathione peroxidase is the mediator of body selenium to protect against paraquat lethality in transgenic mice, J. Nutr., 128, 1070, 1998.
65. Ursini, F., Heim, S., Kiess, M., Maiorino, M., Roveri, A., Wissing, J., and Flohé, L., Dual function of the selenoprotein PHGPx during sperm maturation, Science, 285, 1393, 1999.
66. Brigelius-Flohé, R., Glutathione peroxidases and redox-regulated transcription factors, Biol. Chem., 387, 1329, 2006.
67. Serewko, M.M., Popa, C., Dahler, A.L., Smith, L., Strutton, G.M., Coman, W., Dicker, A.J., and Saunders, N.A., Alterations in gene expression and activity during squamous cell carcinoma development, Cancer Res., 62, 3759, 2002.
68. Florian, S., Wingler, K., Schmehl, K., Jacobasch, G., Kreuzer, O.J., Meyerhof, W., and Brigelius-Flohé, R., Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue, Free Radic. Res., 35, 655, 2001.
69. Esworthy, R.S., Mann, J.R., Sam, M., and Chu, F.F., Low glutathione peroxidase activity in Gpx1 knockout mice protects jejunum crypts from gamma-irradiation damage, Am. J. Physiol. Gastrointest. Liver Physiol., 279, G426, 2000.
70. Esworthy, R.S., Aranda, R., Martin, M.G., Doroshow, J.H., Binder, S.W., and Chu, F.F., Mice with combined disruption of Gpx1 and Gpx2 genes have colitis, Am. J. Physiol. Gastrointest. Liver Physiol., 281, G848, 2001.
71. Chu, F.F., Esworthy, R.S., Chu, P.G., Longmate, J.A., Huycke, M.M., Wilczynski, S., and Doroshow, J.H., Bacteria-induced intestinal cancer in mice with disrupted Gpx1 and Gpx2 genes, Cancer Res., 64, 962, 2004.
72. Esworthy, R.S., Binder, S.W., Doroshow, J.H., and Chu, F., Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression, Biol. Chem., 384, 597, 2003.
73. Chu, F.F., Esworthy, R.S., and Doroshow, J.H., Role of Se-dependent glutathione peroxidases in gastrointestinal inflammation and cancer, Free Radic. Biol. Med., 36, 1481, 2004.
74. Thimmulappa, R.K., Mai, K.H., Srisuma, S., Kensler, T.W., Yamamoto, M., and Biswal, S., Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray, Cancer Res., 62, 5196, 2002.
75. Cho, H.Y., Reddy, S.P., Debiase, A., Yamamoto, M., and Kleeberger, S.R., Gene expression profiling of NRF2-mediated protection against oxidative injury, Free Radic. Biol. Med., 38, 325, 2005.
76. Banning, A., Deubel, S., Kluth, D., Zhou, Z., and Brigelius-Flohé, R., The GI-GPx gene is a target for Nrf2, Mol. Cell. Biol., 25, 4914, 2005.
77. Esworthy, R.S., Yang, L., Frankel, P.H., and Chu, F.F., Epithelium-specific glutathione peroxidase, Gpx2, is involved in the prevention of intestinal inflammation in selenium-deficient mice, J. Nutr., 135, 740, 2005.
78. Cowan, D.B., Weisel, R.D., Williams, W.G., and Mickle, D.A., Identification of oxygen responsive elements in the 5′-flanking region of the human glutathione peroxidase gene, J. Biol. Chem., 268, 26904, 1993.
79. Merante, F., Altamentova, S.M., Mickle, D.A., Weisel, R.D., Thatcher, B.J., Martin, B.M., Marshall, J.G., Tumiati, L.C., Cowan, D.B., and Li, R.K., The characterization and purification of a human transcription factor modulating the glutathione peroxidase gene in response to oxygen tension, Mol. Cell. Biochem., 229, 73, 2002.
80. Cowan, D.B., Weisel, R.D., Williams, W.G., and Mickle, D.A., The regulation of glutathione peroxidase gene expression by oxygen tension in cultured human cardiomyocytes, J. Mol. Cell. Cardiol., 24, 423, 1992.
81. Jornot, L. and Junod, A.F., Differential regulation of glutathione peroxidase by selenomethionine and hyperoxia in endothelial cells, Biochem. J., 306, 581, 1995.
82. Forman, H.J. and Dickinson, D.A., Oxidative signaling and glutathione synthesis, Biofactors, 17, 1, 2003.
83. Finley, J.W., Davis, C.D., and Feng, Y., Selenium from high selenium broccoli protects rats from colon cancer, J. Nutr., 130, 2384, 2000.
84. Davis, C.D., Zeng, H., and Finley, J.W., Selenium-enriched broccoli decreases intestinal tumorigenesis in multiple intestinal neoplasia mice, J. Nutr., 132, 307, 2002.
85. Finley, J.W., Ip, C., Lisk, D.J., Davis, C.D., Hintze, K.J., and Whanger, P.D., Cancerprotective properties of high-selenium broccoli, J. Agric. Food Chem., 49, 2679, 2001.
86. Keck, A.S. and Finley, J.W., Aqueous extracts of selenium-fertilized broccoli increase selenoprotein activity and inhibit DNA single-strand breaks, but decrease the activity of quinone reductase in Hepa 1c1c7 cells, Food Chem. Toxicol., 44, 695, 2006.
87. Robbins, R.J., Keck, A.S., Banuelos, G., and Finley, J.W., Cultivation conditions and selenium fertilization alter the phenolic profile, glucosinolate, and sulforaphane content of broccoli, J. Med. Food, 8, 204, 2005.
88. Chu, F.F., Esworthy, R.S., Lee, L., and Wilczynski, S., Retinoic acid induces Gpx2 gene expression in MCF-7 human breast cancer cells, J. Nutr., 129, 1846, 1999.
89. Morbitzer, M. and Herget, T., Expression of gastrointestinal glutathione peroxidase is inversely correlated to the presence of hepatitis C virus subgenomic RNA in human liver cells, J. Biol. Chem., 280, 8831, 2005.
90. Jakobs, T.C., Schmutzler, C., Meissner, J., and Köhrle, J., The promoter of the human type I 5′-deiodinase gene-mapping of the transcription start site and identification of a DR+4 thyroid-hormone-responsive element, Eur. J. Biochem., 247, 288, 1997.
91. Schütze, N., Bachthaler, M., Lechner, A., Köhrle, J., and Jakob, F., Identification by differential display PCR of the selenoprotein thioredoxin reductase as a 1 alpha, 25(OH)2-vitamin D3-responsive gene in human osteoblasts-regulation by selenite, Biofactors, 7, 299, 1998.
92. Brigelius-Flohé, R., Lötzer, K., Maurer, S., Schultz, M., and Leist, M., Utilization of selenium from different chemical entities for selenoprotein biosynthesis by mammalian cell lines, Biofactors, 5, 125, 1995.
93. Leist, M., Raab, B., Maurer, S., Rosick, U., and Brigelius-Flohé, R., Conventional cell culture media do not adequately supply cells with antioxidants and thus facilitate peroxide-induced genotoxicity, Free Radic. Biol. Med., 21, 297, 1996.
94. Schütze, N., Fritsche, J., Ebert-Dumig, R., Schneider, D., Köohrle, J., Andreesen, R., Kreutz, M., and Jakob, F., The selenoprotein thioredoxin reductase is expressed in peripheral blood monocytes and THP1 human myeloid leukemia cells: regulation by 1,25-dihydroxyvitamin D3 and selenite, Biofactors, 10, 329, 1999.
95. Hintze, K.J., Wald, K., and Finley, J.W., Phytochemicals in broccoli transcriptionally induce thioredoxin reductase, J. Agric. Food Chem., 53, 5535, 2005.
96. Pinto, R.E. and Bartley, W., The nature of the sex-linked differences in glutathione peroxidase activity and aerobic oxidation of glutathione in male and female rat liver, Biochem. J., 115, 449, 1969.
97. Vina, J., Borras, C., Gomez-Cabrera, M.C., and Orr, W.C., Part of the series: from dietary antioxidants to regulators in cellular signalling and gene expression. Role of reactive oxygen species and (phyto)oestrogens in the modulation of adaptive response to stress, Free Radic. Res., 40, 111, 2006.
98. Suzuki, K., Koike, H., Matsui, H., Ono, Y., Hasumi, M., Nakazato, H., Okugi, H., Sekine, Y., Oki, K., Ito, K., Yamamoto, T., Fukabori, Y., Kurokawa, K., and Yamanaka, H., Genistein, a soy isoflavone, induces glutathione peroxidase in the human prostate cancer cell lines LNCaP and PC-3, Int. J. Cancer, 99, 846, 2002.
99. Migliaccio, A., Di Domenico, M., Castoria, G., de Falco, A., Bontempo, P., Nola, E., and Auricchio, F., Tyrosine kinase/p21ras/MAP-kinase pathway activation by estradiol- receptor complex in MCF-7 cells, EMBO J., 15, 1292, 1996.
100. Gao, Y., Walder, K., Sunderland, T., Kantham, L., Feng, H.C., Quick, M., Bishara, N., de Silva, A., Augert, G., Tenne-Brown, J., and Collier, G.R., Elevation in Tanis expression alters glucose metabolism and insulin sensitivity in H4IIE cells, Diabetes, 52, 929, 2003.
101. Karlsson, H.K., Tsuchida, H., Lake, S., Koistinen, H.A., and Krook, A., Relationship between serum amyloid A level and Tanis/SelS mRNA expression in skeletal muscle and adipose tissue from healthy and type 2 diabetic subjects, Diabetes, 53, 1424, 2004.
102. Gao, Y., Feng, H.C., Walder, K., Bolton, K., Sunderland, T., Bishara, N., Quick, M., Kantham, L., and Collier, G.R., Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress: SelS is a novel glucose-regulated protein, FEBS Lett., 563, 185, 2004.
103. Vendeland, S.C., Beilstein, M.A., Chen, C.L., Jensen, O.N., Barofsky, E., and Whanger, P.D., Purification and properties of selenoprotein W from rat muscle, J. Biol. Chem., 268, 17103, 1993.
104. Amantana, A., Vorachek, W.R., Butler, J.A., Costa, N.D., and Whanger, P.D., Effect of copper, zinc and cadmium on the promoter of selenoprotein W in glial and myoblast cells, J. Inorg. Biochem., 91, 356, 2002.
105. Sakurai, A., Nishimoto, M., Himeno, S., Imura, N., Tsujimoto, M., Kunimoto, M., and Hara, S., Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: role of NF-E2-related factor-2, J. Cell. Physiol., 203, 529, 2005.
106. Alam, J., Stewart, D., Touchard, C., Boinapally, S., Choi, A.M., and Cook, J.L., Nrf2, a Cap ʼn' Collar transcription factor, regulates induction of the heme oxygenase-1 gene, J. Biol. Chem., 274, 26071, 1999.
107. Rederstorff, M., Krol, A., and Lescure, A., Understanding the importance of selenium and selenoproteins in muscle function, Cell. Mol. Life Sci., 63, 52, 2006.
108. Hsieh, H.S. and Ganther, H.E., Acid-volatile selenium formation catalyzed by glutathione reductase, Biochemistry, 14, 1632, 1975.
109. Ganther, H.E., Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase, Biochemistry, 10, 4089, 1971.
110. Bjornstedt, M., Kumar, S., and Holmgren, A., Selenite and selenodiglutathione: reactions with thioredoxin systems, Methods Enzymol., 252, 209, 1995.
111. Esaki, N., Nakamura, T., Tanaka, H., and Soda, K., Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme, J. Biol. Chem., 257, 4386, 1982.
112. Soda, K., Oikawa, T., and Esaki, N., Vitamin B6 enzymes participating in selenium amino acid metabolism, Biofactors, 10, 257, 1999.
113. Commandeur, J.N., Andreadou, I., Rooseboom, M., Out, M., de Leur, L.J., Groot, E., and Vermeulen, N.P., Bioactivation of selenocysteine Se-conjugates by a highly purified rat renal cysteine conjugate beta-lyase/glutamine transaminase K, J. Pharmacol. Exp. Ther., 294, 753, 2000.
114. Balogun, E., Hoque, M., Gong, P., Killeen, E., Green, C.J., Foresti, R., Alam, J., and Motterlini, R., Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element, Biochem. J., 371, 887, 2003.
115. Ben-Dor, A., Steiner, M., Gheber, L., Danilenko, M., Dubi, N., Linnewiel, K., Zick, A., Sharoni, Y., and Levy, J., Carotenoids activate the antioxidant response element transcription system, Mol. Cancer Ther., 4, 177, 2005.
116. Chen, C., Yu, R., Owuor, E.D., and Kong, A.N., Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death, Arch. Pharm. Res., 23, 605, 2000.
117. Chen, C., Pung, D., Leong, V., Hebbar, V., Shen, G., Nair, S., Li, W., and Kong, A.N., Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: effect of chemical structure and stress signals, Free Radic. Biol. Med., 37, 1578, 2004.
118. Dietz, B.M., Kang, Y.H., Liu, G., Eggler, A.L., Yao, P., Chadwick, L.R., Pauli, G.F., Farnsworth, N.R., Mesecar, A.D., van Breemen, R.B., and Bolton, J.L., Xanthohumol isolated from Humulus lupulus inhibits menadione-induced DNA damage through induction of quinone reductase, Chem. Res. Toxicol., 18, 1296, 2005.
119. Feng, R., Lu, Y., Bowman, L.L., Qian, Y., Castranova, V., and Ding, M., Inhibition of activator protein-1, NF-kappaB, and MAPKs and induction of phase 2 detoxifying enzyme activity by chlorogenic acid, J. Biol. Chem., 280, 27888, 2005.
120. Ogborne, R.M., Rushworth, S.A., and O’Connell, M.A., Alpha-lipoic acid-induced heme oxygenase-1 expression is mediated by nuclear factor erythroid 2-related factor 2 and p38 mitogen-activated protein kinase in human monocytic cells, Arterioscler. Thromb. Vasc. Biol., 25, 2100, 2005.