Rat peptide methionine sulphoxide reductase: Cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging

Biochemical Journal

Volumn 355, Issue 3, 2001, Pages 819-825

  Petropoulos, Isabelle ^a   Mary, Jean ^a   Perichon, Martine ^a   Friguet, Bertrand ^a  

^a UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Post translational modification; Protein oxidation; Protein repair

Indexed keywords

BIOLOGICAL ORGANS; CATALYST ACTIVITY; CLONING; DNA; GENES; PROTEINS;

RAT PEPTIDE;

ENZYMES;

COMPLEMENTARY DNA; GENE PRODUCT; MESSENGER RNA; METHIONINE SULFOXIDE; OXIDOREDUCTASE; PHOSPHORUS 32; RECOMBINANT PROTEIN;

AGED; AGING; ANIMAL TISSUE; ARTICLE; BRAIN; CATALYSIS; DOWN REGULATION; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; KIDNEY; LIVER; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT;

ANIMALIA;

EID: 0035339675     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3550819     Document Type: Article

References (36)

1. 1 Berlett, B. S. and Stadtman, E. R. (1997) Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272, 20313-20316
2. 2 Beckman, K. B. and Ames, B. N. (1998) The free radical theory of aging matures. Physiol. Rev. 78, 547-581
3. 3 Rivett, A. J. (1985) Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase. J. Biol. Chem. 260, 12600-12606
4. 4 Pacifici, R. E., Salo, D. C. and Davies, K. J. (1989) Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radical Biol. Med. 7, 521-536
5. 5 Grune, T., Reinheckel, T. and Davies, K. J. (1997) Degradation of oxidized proteins in mammalian cells. FASEB J. 11, 526-534
6. 6 Brot, N. and Weissbach, H. (1983) Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch. Biochem. Biophys. 223, 271-281
7. 7 Holmgren, A. (1989) Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-13966
8. 8 Brot, N. and Weissbach, H. (1991) Biochemistry of methionine sulfoxide residues in proteins. Biofactors 3, 91-96
9. 9 Garner, M. H. and Spector, A. (1980) Selective oxidation of cysteine and methionine in normal and senile cataractous lenses. Proc. Natl. Acad. Sci. U.S.A. 77, 1274-1277
10. 10 Abrams, W. R., Weinbaum, G., Weissbach, L., Weissbach, H. and Brot, N. (1981) Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity. Proc. Natl, Acad. Sci. U.S.A. 78, 7483-7486
11. 11 Gabbita, S. P., Aksenov, M. Y., Lovell, M. A. and Markesbery, W. R. (1999) Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 73, 1660-1666
12. 12 Mushegian, A. R. and Koonin, E. V. (1996) A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl. Acad. Sci. U.S.A. 93, 10268-10273
13. 13 Moskovitz, J., Jenkins, N. A., Gilbert, D. J. Copeland, N. G., Jursky, F., Weissbach, H. and Brot, N. (1996) Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues. Proc. Natl. Acad. Sci, U.S.A. 93, 3205-3208
14. 14 Kuschel, L., Hansel, A., Schonherr, R., Weissbach, H., Brot, N., Hoshi, T. and Heinemann, S. H. (1999) Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett. 456, 17-21
15. 15 Moskovitz, J., Berlett, B. S., Poston, J. M. and Stadtman, E. R. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc. Natl. Acad. Sci. U.S.A. 94, 9585-9589
16. 16 Moskovitz, J., Rahman, M. A., Strassman, J., Yancey, S. O., Kushner, S. R., Brot, N. and Weissbach, H. (1995) Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J. Bacteriol. 177, 502-507
17. 17 Moskovitz, J., Flescher, E., Berlett, B. S., Azare, J., Poston, J. M. and Stadtman, E. R. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 95, 14071-14075
18. 18 Levine, R. L., Mosoni, L., Berlett, B. S. and Stadtman; E. R. (1996) Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 15036-15040
19. 19 Levine, R. L., Berlett, B. S., Moskovitz, J., Mosoni, L., and Stadtman, E. R. (1999) Methionine residues may protect proteins from critical oxidative damage. Mech. Ageing Dev. 107, 323-332
20. 20 Minetti, G., Balduini, C. and Brovelli, A. (1994) Reduction of DABS-L-methionine-DL-sulfoxide by protein methionine sulfoxide reductase from polymorphonuclear leukocytes; stereospecificity towards the L-sulfoxide. Ital. J. Biochem. 43, 273-283
21. 21 Moskovitz, J., Weissbach, H. and Brot, N. (1996) Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 2095-2099
22. 22 Cohn, E. J. and Edsall, J. T. (1943) Density and apparent specific volume of proteins. In Proteins, Aminoacids and Peptides as Ions and Dipolar Ions (Nostrand-Reinhold, V., ed.), pp. 370-381, Princeton University Press, Princeton
23. 23 Kozak, M. and Shatkin, A. J. (1979) Characterization of translational initiation regions from eukaryotic messenger RNAs. Methods Enzymol. 60, 360-375
24. 24 Lowther, W. T., Brot, N., Weissbach, H., Honek, J. F. and Matthews, B. W. (2000) Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc. Natl. Acad. Sci. U.S.A. 97, 6463-6468
25. 25 Moskovitz, J., Poston, J. M., Berlett, B. S., Nosworthy, N. J., Szczepanowski, R. and Stadtman, E. R. (2000) Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275, 14167-14172
26. 26 Boschi-Muller, S., Azza, S., Sangller-Clanferani, S., Talfournier, F., Van Dorsselear, A. and Branlant, G. (2000) A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J. Biol. Chem. 275, 35908-35913
27. 27 Lowther, W. T., Brat, N., Weissbach, H. and Matthews, B. W. (2000) Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry 39, 13307-13312
28. 28 Tete-Favier, F., Cobessi, D., Boschi-Muller, S., Azza, S., Branlant, G. and Aubry, A. (2000) Crystal structure of the Escherihia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Struct. Fold. Des. 8, 1167-1178
29. 29 Moskovitz, J., Berlett, B. S., Poston, J. M. and Stadtman, E. R. (1999) Methionine sulfoxide reductase in antioxidant defense. Methods Enzymol. 300, 239-244
30. 30 Vogt, W. (1995) Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radical Biol. Med. 18, 93-105
31. 31 Ciorba, M. A., Heinemann, S. H., Weissbach, H., Brot, N. and Hoshi, T. (1997) Modulation of potassium channel function by methionine oxidation and reduction. Proc. Natl. Acad. Sci. U.S.A. 94, 9932-9937
32. 32 Friguet, B., Bulteau, A. L., Chondrogianni, N., Conconi, M. and Petropoulos, I. (2000) Protein degradation by the proteasome and its implications in aging. Ann. N.Y. Acad. Sci. 908, 143-154
33. 33 Sun, H., Gao, J., Ferrington, D. A., Biesiada, H., Williams, T. D. and Squier, T. C. (1999) Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase, Biochemistry 38, 105-112
34. 34 Lee, C. K., Klopp, R. G., Weindruch, R. and Prolla, T. A. (1999) Gene expression profile of aging and its retardation by caloric restriction. Science 285, 1390-1393
35. 35 Lee, C. K., Weindruch, R. and Prolla, T. A. (2000) Gene-expression profile of the ageing brain in mice. Nat. Genet. 25, 294-297
36. 36 Ly, D. H., Lockhart, D. J., Lerner, R. A. and Schultz, P. G. (2000) Mitotic misregulation and human aging. Science 287, 2486-2492