Maintenance of proteins and aging: The role of oxidized protein repair

References

• Beckman KB, Ames BN. The free radical theory of aging matures. Physiol Rev 1998; 78: 547–581
   PubMed Web of Science ®Google Scholar
• Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272: 20313–20316
   PubMed Web of Science ®Google Scholar
• Friguet B, Bulteau AL, Chondrogianni N, Conconi M, Petropoulos I. Protein degradation by the proteasome and its implications in aging. Ann N Y Acad Sci 2000; 908: 143–154
   PubMedGoogle Scholar
• Petropoulos I, Friguet B. Protein maintenance in aging and replicative senescence: A role for the peptide methionine sulfoxide reductases. Biochim Biophys Acta 2005; 1703: 261–266
   PubMedGoogle Scholar
• Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003; 305: 709–718
   PubMed Web of Science ®Google Scholar
• Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002; 4: 674–680
   PubMed Web of Science ®Google Scholar
• Brot N, Weissbach H. Peptide methionine sulfoxide reductase: Biochemistry and physiological role. Biopolymers 2000; 55: 288–296
   PubMed Web of Science ®Google Scholar
• Holmgren A, Johansson C, Berndt C, Lonn ME, Hudemann C, Lillig CH. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans 2005; 33: 1375–1377
   PubMed Web of Science ®Google Scholar
• Friguet B. Oxidized protein degradation and repair in ageing and oxidative stress. FEBS Lett 2006; 580: 2910–2916
   PubMed Web of Science ®Google Scholar
• Levine RL, Williams JA, Stadtman ER, Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 1994; 233: 346–357
   PubMed Web of Science ®Google Scholar
• Shringarpure R, Grune T, Mehlhase J, Davies KJ. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003; 278: 311–318
   PubMed Web of Science ®Google Scholar
• Shang F, Nowell TR, Jr, Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp Eye Res 2001; 73: 229–238
   PubMedGoogle Scholar
• Kiffin R, Christian C, Knecht E, Cuervo AM. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 2004; 15: 4829–4840
   PubMed Web of Science ®Google Scholar
• Klionsky DJ. The molecular machinery of autophagy: Unanswered questions. J Cell Sci 2005; 118: 7–18
   PubMed Web of Science ®Google Scholar
• Bota DA, Van Remmen H, Davies KJ. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett 2002; 532: 103–106
   PubMed Web of Science ®Google Scholar
• Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996; 65: 801–847
   PubMed Web of Science ®Google Scholar
• Voges D, Zwickl P, Baumeister W. The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015–1068
   PubMed Web of Science ®Google Scholar
• Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997; 386: 463–471
   PubMed Web of Science ®Google Scholar
• Gaczynska M, Rock KL, Goldberg AL. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 1993; 365: 264–267
   PubMed Web of Science ®Google Scholar
• Rivett AJ, Hearn AR. Proteasome function in antigen presentation: Immunoproteasome complexes, peptide production, and interactions with viral proteins. Curr Protein Pept Sci 2004; 5: 153–161
   PubMed Web of Science ®Google Scholar
• Grune T, Jung T, Merker K, Davies KJ. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and “aggresomes” during oxidative stress, aging, and disease. Int J Biochem Cell Biol 2004; 36: 2519–2530
   PubMed Web of Science ®Google Scholar
• Friguet B, Stadtman ER, Szweda LI. Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease. J Biol Chem 1994; 269: 21639–21643
   PubMed Web of Science ®Google Scholar
• Friguet B, Szweda LI. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett 1997; 405: 21–25
   PubMed Web of Science ®Google Scholar
• Conconi M, Szweda LI, Levine RL, Stadtman ER, Friguet B. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Arch Biochem Biophys 1996; 331: 232–240
   PubMedGoogle Scholar
• Shibatani T, Nazir M, Ward WF. Alteration of rat liver 20S proteasome activities by age and food restriction. J Gerontol A Biol Sci Med Sci 1996; 51: B316–B322
   PubMedGoogle Scholar
• Anselmi B, Conconi M, Veyrat-Durebex C, Turlin E, Biville F, Alliot J, Friguet B. Dietary self-selection can compensate an age-related decrease of rat liver 20 S proteasome activity observed with standard diet. J Gerontol A Biol Sci Med Sci 1998; 53: B173–B179
   PubMedGoogle Scholar
• Bulteau AL, Petropoulos I, Friguet B. Age-related alterations of proteasome structure and function in aging epidermis. Exp Gerontol 2000; 35: 767–777
   PubMedGoogle Scholar
• Bulteau AL, Szweda LI, Friguet B. Age-dependent declines in proteasome activity in the heart. Arch Biochem Biophys 2002; 397: 298–304
   PubMed Web of Science ®Google Scholar
• Diaz-Hernandez M, Hernandez F, Martin-Aparicio E, Gomez-Ramos P, Moran MA, Castano JG, Ferrer I, Avila J, Lucas JJ. Neuronal induction of the immunoproteasome in Huntington's disease. J Neurosci 2003; 23: 11653–11661
   PubMed Web of Science ®Google Scholar
• Carrard G, Dieu M, Raes M, Toussaint O, Friguet B. Impact of ageing on proteasome structure and function in human lymphocytes. Int J Biochem Cell Biol 2003; 35: 728–739
   PubMedGoogle Scholar
• Viteri G, Carrard G, Birlouez-Aragon I, Silva E, Friguet B. Age-dependent protein modifications and declining proteasome activity in the human lens. Arch Biochem Biophys 2004; 427: 197–203
   PubMed Web of Science ®Google Scholar
• Bulteau AL, Verbeke P, Petropoulos I, Chaffotte AF, Friguet B. Proteasome inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20 S proteasome degradation in vitro. J Biol Chem 2001; 276: 45662–45668
   PubMed Web of Science ®Google Scholar
• Farout L, Mary J, Vinh J, Szweda LI, Friguet B. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes. Arch Biochem Biophys 2006
   PubMedGoogle Scholar
• Chondrogianni N, Stratford FL, Trougakos IP, Friguet B, Rivett AJ, Gonos ES. Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J Biol Chem 2003; 278: 28026–28037
   PubMed Web of Science ®Google Scholar
• Keller JN, Huang FF, Markesbery WR. Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 2000; 98: 149–156
   PubMedGoogle Scholar
• Petropoulos I, Conconi M, Wang X, Hoenel B, Bregegere F, Milner Y, 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 2000; 55: B220–B227
   PubMedGoogle Scholar
• Lee CK, Klopp RG, Weindruch R, Prolla TA. Gene expression profile of aging and its retardation by caloric restriction. Science 1999; 285: 1390–1393
   PubMed Web of Science ®Google Scholar
• Ly DH, Lockhart DJ, Lerner RA, Schultz PG. Mitotic misregulation and human aging. Science 2000; 287: 2486–2492
   PubMed Web of Science ®Google Scholar
• Chondrogianni N, Petropoulos I, Franceschi C, Friguet B, Gonos ES. Fibroblast cultures from healthy centenarians have an active proteasome. Exp Gerontol 2000; 35: 721–728
   PubMed Web of Science ®Google Scholar
• Chondrogianni N, Tzavelas C, Pemberton AJ, Nezis IP, Rivett AJ, Gonos ES. Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates. J Biol Chem 2005; 280: 11840–11850
   PubMed Web of Science ®Google Scholar
• Sitte N, Huber M, Grune T, Ladhoff A, Doecke WD, Von Zglinicki T, Davies KJ. Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. Faseb J 2000; 14: 1490–1498
   PubMed Web of Science ®Google Scholar
• Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc Natl Acad Sci USA 1993; 90: 11247–11251
   PubMedGoogle Scholar
• Bakala H, Delaval E, Hamelin M, Bismuth J, Borot-Laloi C, Corman B, Friguet B. Changes in rat liver mitochondria with aging. Lon protease-like reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix. Eur J Biochem 2003; 270: 2295–2302
   PubMedGoogle Scholar
• Delaval E, Perichon M, Friguet B. Age-related impairment of mitochondrial matrix aconitase and ATP-stimulated protease in rat liver and heart. Eur J Biochem 2004; 271: 4559–4564
   PubMedGoogle Scholar
• Ferrington DA, Sun H, Murray KK, Costa J, Williams TD, Bigelow DJ, Squier TC. Selective degradation of oxidized calmodulin by the 20 S proteasome. J Biol Chem 2001; 276: 937–943
   PubMed Web of Science ®Google Scholar
• Holmgren A. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid Redox Signal 2000; 2: 811–820
   PubMed Web of Science ®Google Scholar
• Biteau B, Labarre J, Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 2003; 425: 980–984
   PubMed Web of Science ®Google Scholar
• Budanov AV, Sablina AA, Feinstein E, Koonin EV, Chumakov PM. Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 2004; 304: 596–600
   PubMed Web of Science ®Google Scholar
• Johnson D, Travis J. Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor. J Biol Chem 1978; 253: 7142–7144
   PubMed Web of Science ®Google Scholar
• Bartlett RK, Bieber Urbauer RJ, Anbanandam A, Smallwood HS, Urbauer JL, Squier TC. Oxidation of Met144 and Met145 in calmodulin blocks calmodulin dependent activation of the plasma membrane Ca-ATPase. Biochemistry 2003; 42: 3231–3238
   PubMedGoogle Scholar
• Vougier S, Mary J, Dautin N, Vinh J, Friguet B, Ladant D. Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases. J Biol Chem 2004; 279: 30210–30218
   PubMedGoogle Scholar
• Davis DA, Newcomb FM, Moskovitz J, Wingfield PT, Stahl SJ, Kaufman J, Fales HM, Levine RL, Yarchoan R. HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase. Biochem J 2000; 346(2)305–311
   PubMedGoogle Scholar
• Garner B, Witting PK, Waldeck AR, Christison JK, Raftery M, Stocker R. Oxidation of high density lipoproteins. I. Formation of methionine sulfoxide in apolipoproteins AI and AII is an early event that accompanies lipid peroxidation and can be enhanced by alpha-tocopherol. J Biol Chem 1998; 273: 6080–6087
   PubMed Web of Science ®Google Scholar
• Ezraty B, Grimaud R, El Hassouni M, Moinier D, Barras F. Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli. Embo J 2004; 23: 1868–1877
   PubMedGoogle Scholar
• Mary J, Vougier S, Picot CR, Perichon M, Petropoulos I, Friguet B. Enzymatic reactions involved in the repair of oxidized proteins. Exp Gerontol 2004; 39: 1117–1123
   PubMed Web of Science ®Google Scholar
• Moskovitz J. Roles of methionine sulfoxide reductases in antioxidant defense, protein regulation and survival. Curr Pharm Des 2005; 11: 1451–1457
   PubMed Web of Science ®Google Scholar
• Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat Struct Biol 2002; 9: 348–352
   PubMedGoogle Scholar
• Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Structure 2000; 8: 1167–1178
   PubMedGoogle Scholar
• Hansel A, Kuschel L, Hehl S, Lemke C, Agricola HJ, Hoshi T, Heinemann SH. Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. Faseb J 2002; 16: 911–913
   PubMedGoogle Scholar
• Vougier S, Mary J, Friguet B. Subcellular localization of methionine sulphoxide reductase A (MsrA): Evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem J 2003; 373: 531–537
   PubMed Web of Science ®Google Scholar
• Kim HY, Gladyshev VN. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 2005; 44: 8059–8067
   PubMed Web of Science ®Google Scholar
• Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM. Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun 2006; 342: 145–152
   PubMed Web of Science ®Google Scholar
• Kim HY, Gladyshev VN. Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol 2006; 7: 11
   PubMedGoogle Scholar
• Hansel A, Heinemann SH, Hoshi T. Heterogeneity and function of mammalian MSRs: Enzymes for repair, protection and regulation. Biochim Biophys Acta 2005; 1703: 239–247
   PubMed Web of Science ®Google Scholar
• Kryukov GV, Kumar RA, Koc A, Sun Z, Gladyshev VN. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002; 99: 4245–4250
   PubMed Web of Science ®Google Scholar
• Boschi-Muller S, Olry A, Antoine M, Branlant G. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim Biophys Acta 2005; 1703: 231–238
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 2001; 98: 12920–12925
   PubMed Web of Science ®Google Scholar
• Hanbauer I, Moskovitz J. The yeast cytosolic thioredoxins are involved in the regulation of methionine sulfoxide reductase A. Free Radic Biol Med 2006; 40: 1391–1396
   PubMedGoogle Scholar
• Sigalov AB, Stern LJ. Dihydrolipoic acid as an effective cofactor for peptide methionine sulfoxide reductase in enzymatic repair of oxidative damage to both lipid-free and lipid-bound apolipoprotein a-I. Antioxid Redox Signal 2002; 4: 553–557
   PubMedGoogle Scholar
• Sagher D, Brunell D, Hejtmancik JF, Kantorow M, Brot N, Weissbach H. Thionein can serve as a reducing agent for the methionine sulfoxide reductases. Proc Natl Acad Sci USA 2006; 103: 8656–8661
   PubMedGoogle Scholar
• Harman D. Aging: A theory based on free radical and radiation chemistry. J Gerontol 1956; 11: 298–300
   PubMedGoogle Scholar
• Petropoulos I, Mary J, Perichon M, Friguet B. Rat peptide methionine sulphoxide reductase: Cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 2001; 355: 819–825
   PubMedGoogle Scholar
• Picot CR, Perichon M, Cintrat JC, Friguet B, Petropoulos I. The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts. FEBS Lett 2004; 558: 74–78
   PubMed Web of Science ®Google Scholar
• Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T. High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2002; 99: 2748–2753
   PubMed Web of Science ®Google Scholar
• Koc A, Gasch AP, Rutherford JC, Kim HY, Gladyshev VN. Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci USA 2004; 101: 7999–8004
   PubMed Web of Science ®Google Scholar
• Levine RL, Mosoni L, Berlett BS, Stadtman ER. Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci USA 1996; 93: 15036–15040
   PubMed Web of Science ®Google Scholar
• Picot CR, Petropoulos I, Perichon M, Moreau M, Nizard C, Friguet B. Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. Free Radic Biol Med 2005; 39: 1332–1341
   PubMed Web of Science ®Google Scholar
• Yermolaieva O, Xu R, Schinstock C, Brot N, Weissbach H, Heinemann SH, Hoshi T. Methionine sulfoxide reductase A protects neuronal cells against brief hypoxia/reoxygenation. Proc Natl Acad Sci USA 2004; 101: 1159–1164
   PubMed Web of Science ®Google Scholar
• Kantorow M, Hawse JR, Cowell TL, Benhamed S, Pizarro GO, Reddy VN, Hejtmancik JF. Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc Natl Acad Sci USA 2004; 101: 9654–9659
   PubMed Web of Science ®Google Scholar
• Sreekumar PG, Kannan R, Yaung J, Spee CK, Ryan SJ, Hinton DR. Protection from oxidative stress by methionine sulfoxide reductases in RPE cells. Biochem Biophys Res Commun 2005; 334: 245–253
   PubMed Web of Science ®Google Scholar
• Picot CR, Perichon M, Lundberg KC, Friguet B, Szweda LI, Petropoulos I. Alterations in mitochondrial and cytosolic methionine sulfoxide reductase activity during cardiac ischemia and reperfusion. Exp Gerontol 2006, in press
   PubMedGoogle Scholar
• Bulteau AL, Moreau M, Saunois A, Nizard C, Friguet B. Algae extract-mediated stimulation and protection of proteasome activity within human keratinocytes exposed to UVA and UVB irradiation. Antioxid Redox Signal 2006; 8: 136–143
   PubMed Web of Science ®Google Scholar