Overexpression of methionine sulfoxide reductases A and B2 protects MOLT-4 cells against zinc-induced oxidative stress

Antioxidants and Redox Signaling

Volumn 11, Issue 2, 2009, Pages 215-225

  Cabreiro, Filipe ^a   Picot, Cědric R ^a   Perichon, Martine ^a   Friguet, Bertrand ^a,b   Petropoulos, Isabelle ^a,b  

^a UNIVERSITÉ PARIS DESCARTES   (France)

^b SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

METALLOTHIONEIN; METHIONINE SULFOXIDE REDUCTASE A; METHIONINE SULFOXIDE REDUCTASE B; METHIONINE SULFOXIDE REDUCTASE B2; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; ZINC;

ANTIOXIDANT ACTIVITY; ARTICLE; CELL CLONING; CELL DEATH; CELL PROLIFERATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME REGULATION; GENE EXPRESSION; HUMAN; HUMAN CELL; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION;

CELL LINE, TUMOR; CELL SURVIVAL; GENE EXPRESSION; HUMANS; IMMUNOBLOTTING; METALLOTHIONEIN; OXIDATIVE STRESS; OXIDOREDUCTASES; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TRANSCRIPTION FACTORS; ZINC;

EID: 58149100981     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2008.2102     Document Type: Article

References (54)

1. Achilli C, Ciana A, Rossi A, Balduini C, and Minetti G. Neutrophil granulocytes uniquely express, among human blood cells, high levels of methionine-sulfoxide-reductase enzymes. J Leukoc Biol 83: 181-189, 2008.
2. Brot N, Werth J, Koster D, and Weissbach H. Reduction of N-acetyl methionine sulfoxide: a simple assay for peptide methionine sulfoxide reductase. Anal Biochem 122: 291-294, 1982.
3. Butler JS and Loh SN. Zn(2 )-dependent misfolding of the p53 DNA binding domain. Biochemistry 46: 2630-2639, 2007.
4. Cabreiro F, Picot CR, Perichon M, Mary J, Friguet B, and Petropoulos I. Identification of proteins undergoing expression level modifications in WI-38 SV40 fibroblasts overexpressing methionine sulfoxide reductase A. Biochimie 89: 1388-1395, 2007.
5. Cabreiro F, Picot CR, Perichon M, Castel J, Friguet B, and Petropoulos I. Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage. J Biol Chem 283: 16673-16681, 2008.
6. Cabreiro F, Perichon M, Jatje J, Malavolta M, Mocchegiani E, Friguet B, and Petropoulos I. Zinc supplementation in the elderly subjects: Effect on oxidized protein degradation and repair systems in peripheral blood lymphocytes. Exp Gerontol 43: 483-487, 2008.
7. Chimienti F, Jourdan E, Favier A, and Seve M. Zinc resistance impairs sensitivity to oxidative stress in HeLa cells: protection through metallothioneins expression. Free Radic Biol Med 31: 1179-1190, 2001.
8. Chung MJ, Walker PA, Brown RW, and Hogstrand C. Zinc-mediated gene expression offers protection against H2O2-induced cytotoxicity. Toxicol Appl Pharmacol 205: 225-236, 2005.
9. Davies MJ. The oxidative environment and protein damage. Biochim Biophys Acta 1703: 93-109, 2005.
10. Formigari A, Irato P, and Santon A. Zinc, antioxidant systems and metallothionein in metal mediated-apoptosis: biochemical and cytochemical aspects. Comp Biochem Physiol C Toxicol Pharmacol 146: 443-459, 2007.
11. Frazzini V, Rockabrand E, Mocchegiani E, and Sensi SL. Oxidative stress and brain aging: is zinc the link? Biogerontology 7: 307-314, 2006.
12. Gazaryan IG, Krasinskaya IP, Kristal BS, and Brown AM. Zinc irreversibly damages major enzymes of energy production and antioxidant defense prior to mitochondrial permeability transition. J Biol Chem 282: 24373-24380, 2007.
13. Glushchenko AV and Jacobsen DW. Molecular targeting of proteins by L-homocysteine: mechanistic implications for vascular disease. Antioxid Redox Signal 9: 1883-1898, 2007.
14. Grimaud R, Ezraty B, Mitchell JK, Lafitte D, Briand C, Derrick PJ, and Barras F. Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase. J Biol Chem 276: 48915-48920, 2001.
15. Hamatake M, Iguchi K, Hirano K, and Ishida R. Zinc induces mixed types of cell death, necrosis, and apoptosis, in molt-4 cells. J Biochem 128: 933-939, 2000.
16. Hansel A, Kuschel L, Hehl S, Lemke C, Agricola HJ, Hoshi T, and Heinemann SH. Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. FASEB J 16: 911-913, 2002.
17. Hao Q and Maret W. Imbalance between pro-oxidant and pro-antioxidant functions of zinc in disease. J Alzheimers Dis 8: 161-170; discussion 209-115, 2005.
18. Jung S, Hansel A, Kasperczyk H, Hoshi T, and Heinemann SH. Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett 527: 91-94, 2002.
19. Kantorow M, Hawse JR, Cowell TL, Benhamed S, Pizarro GO, Reddy VN, and Hejtmancik JF. Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc Natl Acad Sci USA 101: 9654-9659, 2004.
20. Kim HY and Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 15: 1055-1064, 2004.
21. Kim HY and Gladyshev VN. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 44: 8059-8067, 2005.
22. Kim HY and Gladyshev VN. Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol 7: 11, 2006.
23. Kim HY and Gladyshev VN. Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 407: 321-329, 2007.
24. Kumar RA, Koc A, Cerny RL, and Gladyshev VN. Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J Biol Chem 277: 37527-37535, 2002.
25. Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, and Heinemann SH. Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett 456: 17-21, 1999.
26. Lee JW, Gordiyenko NV, Marchetti M, Tserentsoodol N, Sagher D, Alam S, Weissbach H, Kantorow M, and Rodriguez IR. Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina. Exp Eye Res 82: 816-827, 2006.
27. Lescure A, Gautheret D, Carbon P, and Krol A. Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem 274: 38147-38154, 1999.
28. Levine RL, Mosoni L, Berlett BS, and Stadtman ER. Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci USA 93: 15036-15040, 1996.
29. Marchetti MA, Lee W, Cowell TL, Wells TM, Weissbach H, and Kantorow M. Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells. Exp Eye Res 83: 1281-1286, 2006.
30. Marchetti MA, Pizarro GO, Sagher D, Deamicis C, Brot N, Hejtmancik JF, Weissbach H, and Kantorow M. Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells. Invest Ophthalmol Vis Sci 46: 2107-2112, 2005.
31. Maret W. Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxid Redox Signal 8: 1419-1441, 2006.
32. Maret W. Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc. Exp Gerontol 43: 363-369, 2007.
33. Maret W and Krezel A. Cellular zinc and redox buffering capacity of metallothionein/thionein in health and disease. Mol Med 13: 371-375, 2007.
34. Moskovitz J, Berlett BS, Poston JM, and Stadtman ER. The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94: 9585-9589, 1997.
35. Moskovitz J, Flescher E, Berlett BS, Azare J, Poston JM, and Stadtman ER. 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 USA 95: 14071-14075, 1998.
36. Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, and Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 98: 12920-12925, 2001.
37. Moskovitz J, Rahman MA, Strassman J, Yancey SO, Kushner SR, Brot N, and Weissbach H. Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol 177: 502-507, 1995.
38. Noh KM and Koh JY. Induction and activation by zinc of NADPH oxidase in cultured cortical neurons and astrocytes. J Neurosci 20: RC111, 2000.
39. Petropoulos I, Mary J, Perichon M, and Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 355: 819-825, 2001.
40. Petropoulos I, Conconi M, Wang X, Hoenel B, Bregegere F, Milner Y, and Friguet B. Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol A Biol Sci Med Sci 55: B220-227, 2000.
41. Picot CR, Petropoulos I, Perichon M, Moreau M, Nizard C, and Friguet B. Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. Free Radic Biol Med 39: 1332-1341, 2005.
42. Powell SR. The antioxidant properties of zinc. J Nutr 130: 1447S-1454S, 2000.
43. Robinson KM, Janes MS, Pehar M, Monette JS, Ross MF, Hagen TM, Murphy MP, and Beckman JS. Selective fluorescent imaging of superoxide in vivo using ethidium-based probes. Proc Natl Acad Sci USA 103: 15038-15043, 2006.
44. Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, and Hoshi T. High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 99: 2748-2753, 2002.
45. Stadtman ER, Moskovitz J, and Levine RL. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 5: 577-582, 2003.
46. Thornalley PJ and Vasak M. Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim Biophys Acta 827: 36-44, 1985.
47. Uthus EO and Moskovitz J. Specific activity of methionine sulfoxide reductase in CD-1 mice is significantly affected by dietary selenium but not zinc. Biol Trace Elem Res 115: 265-276, 2007.
48. Viarengo A, Burlando B, Ceratto N, and Panfoli I. Antioxidant role of metallothioneins: a comparative overview. Cell Mol Biol 46: 407-417, 2000.
49. Vougier S, Mary J, and Friguet B. Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem J 373: 531-537, 2003.
50. Weissbach H, Resnick L, and Brot N. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta 1703: 203-212, 2005.
51. Weissbach H, Etienne F, Hoshi T, Heinemann SH, Lowther WT, Matthews B, St John G, Nathan C, and Brot N. Peptide methionine sulfoxide reductase: Structure, mechanism of action, and biological function. Arch Biochem Biophys 397: 172-178, 2002.
52. Yermolaieva O, Xu R, Schinstock C, Brot N, Weissbach H, Heinemann SH, and Hoshi T. Methionine sulfoxide reductase A protects neuronal cells against brief hypoxia/ reoxygenation. Proc Natl Acad Sci USA 101: 1159-1164, 2004.
53. Yoshida M, Saegusa Y, Fukuda A, Akama Y, and Owada S. Measurement of radical-scavenging ability in hepatic metallothionein of rat using in vivo electron spin resonance spectroscopy. Toxicology 213: 74-80, 2005.
54. Zhao H, Kalivendi S, Zhang H, Joseph J, Nithipatikom K, Vasquez-Vivar J, and Kalyanaraman B. Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide. Free Radic Biol Med 34: 1359-1368, 2003.