Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome

Bioscience Reports

Volumn 29, Issue 5, 2009, Pages 329-338

  Sunde, Roger A ^a   Raines, Anna M ^a   Barnes, Kimberly M ^a,b   Evenson, Jacqueline K ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

Glutathione peroxidase 1 (Gpx1); Mouse; Nonsense mediated decay (NMD); Se deficiency; Selenoprotein H (Selh); Selenoprotein W (Sepw1)

Indexed keywords

BIOLOGICAL MARKER; DEIODINASE IODOTHYRONINE TYPE 1; GLUTATHIONE PEROXIDASE 1; GLUTATHIONE PEROXIDASE 3; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PROTEIN; PROTEOME; SELENIUM; SELENOPROTEIN; SELENOPROTEIN H; SELENOPROTEIN K; SELENOPROTEIN M; SELENOPROTEIN S; SELENOPROTEIN T; SELENOPROTEIN W; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 2; THYRONINE DERIVATIVE; UNCLASSIFIED DRUG; GLUTATHIONE PEROXIDASE; THIOREDOXIN REDUCTASE;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CODON; CONTROLLED STUDY; DIETARY INTAKE; DNA BASE COMPOSITION; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; HEALTH STATUS; KIDNEY; LIVER; MALE; MOUSE; NONHUMAN; NONSENSE MEDIATED MRNA DECAY; PREDICTION; PROTEIN FUNCTION; PROTEIN MICROARRAY; QUANTITATIVE ANALYSIS; REAL TIME POLYMERASE CHAIN REACTION; SELENIUM DEFICIENCY; TISSUE LEVEL; ANIMAL; C57BL MOUSE; DIET; ENZYMOLOGY; GENETICS; METABOLISM; TIME;

MUS;

ANIMALS; DIET; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE PEROXIDASE; KIDNEY; LIVER; MALE; MICE; MICE, INBRED C57BL; PROTEOME; RNA, MESSENGER; SELENIUM; SELENOPROTEINS; THIOREDOXIN-DISULFIDE REDUCTASE; TIME FACTORS;

EID: 67650855496     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSR20080146     Document Type: Article

References (47)

1. 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
2. Turner, D. C. and Stadtman, T. C. (1973) Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein. Arch. Biochem. Biophys. 154, 366-381
3. Forstrom, J. W., Zakowski, J. J. and Tappel, A. L. (1978) Identification of the catalytic site of rat liver GSH-Px as selenocysteine. Biochemistry 17, 2639-2644
4. Jones, J. B., Dilworth, G. L. and Stadtman, T. C. (1979) Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii. Arch. Biochem. Biophys. 195, 255-260
5. Hatfield, D. L. (2001) Selenium: Its Molecular Biology and Role in Human Health, Kluwer Academic Publishers. Norwood, MA.
6. Sunde, R. A. (2001) Selenium. Present Knowledge in Nutrition (Bowman, B. A. and Russell, R. M., eds), pp. 352-365, ILSI Press, Washington, D.C.
7. Chambers, I., Frampton, J., Goldfarb, P. S., Affara, N., McBain, W. and Harrison, P. R. (1986) The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J. 5, 1221-1227
8. Berry, M. J., Banu, L., Harney, J. W. and Larsen, P. R. (1993) Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons. EMBO J. 12, 3315-3322
9. Walczak, R., Westhof, E., Carbon, P. and Krol, A. (1996) A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs. RNA 2, 367-379
10. Sunde, R. A. and Evenson, J. K. (1987) Serine incorporation into the selenocysteine moiety of glutathione peroxidase. J. Biol. Chem. 262, 933-937
11. Hatfield, D. L., Berry, M. J. and Gladyshev, V. N. (2006) Selenium. Its Molecular Biology and Role in Human Health, Springer, New York, NY
12. Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigo, R. and Gladyshev, V. N. (2003) Characterization of mammalian selenoproteins. Science 300, 1439-1443
13. Sunde, R. A. (2006) Regulation of glutathione peroxidase-1 expression. In Selenium: Its Molecular Biology and Role in Human Health (Hatfield, D. L., Berry, M. J. and Gladyshev, V. N., eds), pp. 149-160, Springer, New York, NY
14. Lei, X. G., Evenson, J. K., Thompson, K. M. and Sunde, R. A. (1995) Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium. J. Nutr. 125, 1438-1446
15. Saedi, M. S., Smith, C. G., Frampton, J., Chambers, I., Harrison, P. R. and Sunde, R. A. (1988) Effect of selenium status on mRNA levels for glutathione peroxidase in rat liver. Biochem. Biophys. Res. Commun. 153, 855-861
16. Sunde, R. A., Evenson, J. K., Thompson, K. M. and Sachdev, S. W. (2005) Dietary selenium requirements based on glutathione peroxidase-1 activity and mRNA levels and other selenium parameters are not increased by pregnancy and lactation in rats. J. Nutr. 135, 2144-2150
17. Hadley, K. B. and Sunde, R. A. (2001) Selenium regulation of thioredoxin reductase activity and mRNA levels in rat liver. J. Nutr. Biochem. 12, 693-702
18. Weiss, S. L. and Sunde, R. A. (1998) Cis-acting elements are required for selenium regulation of glutathione peroxidase-1 mRNA levels. RNA 4, 816-827
19. Moriarty, P. M., Reddy, C. C. and Maquat, L. E. (1998) Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likely to be nonsense codon-mediated decay of cytoplasmic mRNA. Mol. Cell. Biol. 18, 2932-2939
20. Low, S. C. and Berry, M. J. (1996) Knowing when not to stop: selenocysteine incorporation in eukaryotes. Trends Biochem. Sci. 21, 203-208
21. Nagy, E. and Maquat, L. E. (1998) A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem. Sci. 23, 198-199
22. Maquat, L. E. (2005) Nonsense-mediated mRNA decay in mammals. J. Cell Sci. 118, 1773-1776
23. Weiss Sachdev, S. and Sunde, R. A. (2001) Selenium regulation of transcript abundance and relative translational efficiency of glutathione peroxidase 1 and 4 in rat liver. Biochem. J. 357, 851-858
24. Sun, X., Li, X., Moriarty, P. M., Henics, T., LaDuca, J. P. and Maquat, L. E. (2001) Nonsense-mediated decay of mRNA for the selenoprotein phospholipid hydroperoxide glutathione peroxidase is detectable in cultured cells but masked or inhibited in rat tissues. Mol. Biol. Cell 12, 1009-1017
25. Muller, C., Wingler, K. and Brigelius-Flohé, R. (2003) 3′UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency. Biol. Chem. 384, 11-18
26. Carlson, B. A., Xu, X. M., Gladyshev, V. N. and Hatfield, D. L. (2005) Selective rescue of selenoprotein expression in mice lacking a highly specialized methyl group in selenocysteine tRNA. J. Biol. Chem. 280, 5542-5548
27. Squires, J. E., Stoytchev, I., Forry, E. P. and Berry, M. J. (2007) SBP2 binding affinity is a major determinant in differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay. Mol. Cell Biol. 27, 7848-7855
28. Bubenik, J. L. and Driscoll, D. M. (2007) Altered RNA binding activity underlies abnormal thyroid hormone metabolism linked to a mutation in selenocysteine insertion sequence-binding protein 2. J. Biol. Chem. 282, 34653-34662
29. National Research Council (1995) Nutrient Requirements of Laboratory Animals, National Academy Press, Washington, DC
30. McKown, D. M. and Morris, J. S. (1978) Rapid measurement of selenium in biological samples using instrumental neutron activation analysis. J. Radioanal. Nucl. Chem. 43, 411-420
31. Lawrence, R. A., Sunde, R. A., Schwartz, G. L. and Hoekstra, W. G. (1974) Glutathione peroxidase activity in rat lens and other tissues in relation to dietary selenium intake. Exp. Eye Res. 18, 563-569
32. Hill, K. E., McCollum, G. W. and Burk, R. F. (1997) Determination of thioredoxin reductase activity in rat liver supernatant. Anal. Biochem. 253, 123-125
33. Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275
34. Gubler, U. and Hoffman, B. J. (1983) A simple and very efficient method for generating cDNA libraries. Gene 25, 263-269
35. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (1989) Current Protocols in Molecular Biology. Wiley and Sons, New York, NY
36. Eisen, M. B., Spellman, P. T., Brown, P. O. and Botstein, D. (1998) Cluster analysis and display of genome-wide expression patterns. Proc. Natl. Acad. Sci. U.S.A. 95, 14863-14868
37. Peirson, S. N., Butler, J. N. and Foster, R. G. (2003) Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res. 31, e73
38. Pfaffl, M. W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45
39. Weiss, S. L., Evenson, J. K., Thompson, K. M. and Sunde, R. A. (1996) The selenium requirement for glutathione peroxidase mRNA level is half of the selenium requirement for glutathione peroxidase activity in female rats. J. Nutr. 126, 2260-2267
40. Zhang, L., Maiorino, M., Roveri, A. and Ursini, F. (1989) Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim. Biophys. Acta 1006, 140-143
41. Hooven, L. A., Butler, J., Ream, L. W. and Whanger, P. D. (2006) Microarray analysis of selenium-depleted and selenium-supplemented mice. Biol. Trace Elem. Res. 109, 173-179
42. Vendeland, S. C., Beilstein, M. A., Yeh, J. Y., Ream, W. and Whanger, P. D. (1995) Rat skeletal muscle selenoprotein W: cDNA clone and mRNA modulation by dietary selenium. Proc. Natl. Acad. Sci. U.S.A. 92, 8749-8753
43. Wen, W., Weiss, S. L. and Sunde, R. A. (1998) UGA codon position affects the efficiency of selenocysteine incorporation into glutathione peroxidase-1. J. Biol. Chem. 273, 28533-28541
44. Wingler, K., Bocher, M., Flohé, L., Kollmus, H. and Brigelius-Flohé, R. (1999) mRNA stability and selenocysteine insertion sequence efficiency rank gastrointestinal glutathione peroxidase high in the hierarchy of selenoproteins. Eur. J. Biochem. 259, 149-157
45. Chittum, H. S., Hill, K. E., Carlson, B. A., Lee, B. J., Burk, R. F. and Hatfield, D. L. (1997) Replenishment of selenium deficient rats with selenium results in redistribution of the selenocysteine tRNA population in a tissue specific manner. Biochim. Biophys. Acta 1359, 25-34
46. Howard, M. T., Aggarwal, G., Anderson, C. B., Khatri, S., Flanigan, K. M. and Atkins, J. F. (2005) Recoding elements located adjacent to a subset of eukaryal selenocysteine-specifying UGA codons. EMBO J. 24, 1596-1607
47. Barnes, K. M., Evenson, J. K., Raines, A. M. and Sunde, R. A. (2009) Transcript analysis of the selenoproteome indicates that dietary selenium requirements based on selenium-regulated selenoprotein mRNAs are uniformly less than requirements based on glutathione peroxidase activity in rats. J. Nutr. 139, 199-206