Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system

Current Pharmaceutical Design

Volumn 17, Issue 36, 2011, Pages 4007-4022

  Kästle, Marc ^a   Grune, Tilman ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Age dependent diseases; Aging; Proteasome; Protein aggregation; Protein oxidation; Ubiquitin

Indexed keywords

ADVANCED GLYCATION END PRODUCT; LIPOFUSCIN; POLYUBIQUITIN; PROTEASOME; SULFUR; UBIQUITIN;

AGING; ALZHEIMER DISEASE; ARTICLE; ATHEROSCLEROSIS; CUTANEOUS PARAMETERS; DISEASES; EYE; HUMAN; HUNTINGTON CHOREA; MEDICAL LITERATURE; NONHUMAN; OXIDATION; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CARBONYLATION; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN MODIFICATION; UBIQUITIN PROTEASOMAL SYSTEM;

EID: 84855217371     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161211798764898     Document Type: Article

References (242)

1. Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 1956; 11(3): 298-300.
2. Harman D. Aging: overview. Ann N Y Acad Sci 2001; 928: 1-21.
3. Wong E, Cuervo AM. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2010; 2(12): a006734.
4. Jung T, Catalgol B, Grune T. The proteasomal system. Mol As-pects Med 2009; 30(4): 191-296.
5. [5]Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem 1996; 271(26): 15504-9.
6. [6]Sitte N, Merker K, Grune T. Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts. FEBS Lett 1998; 440(3): 399-402.
7. [7]Schmitz A, Herzog V. Endoplasmic reticulum-associated degradation: exceptions to the rule. Eur J Cell Biol 2004; 83(10): 501-9.
8. Hampton RY. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 2002; 14(4): 476-82.
9. [9]Takeuchi J, Toh-e A. [Regulation of cell cycle by proteasome in yeast]. Tanpakushitsu Kakusan Koso 1997; 42(14 Suppl): 2247-54.
10. Moriishi K, Mochizuki R, Moriya K, et al. Critical role of PA28gamma in hepatitis C virus-associated steatogenesis and he-patocarcinogenesis. Proc Natl Acad Sci U S A 2007; 104(5): 1661-6.
11. Scheffner M, Whitaker NJ. Human papillomavirus-induced car-cinogenesis and the ubiquitin-proteasome system. Semin Cancer Biol 2003; 13(1): 59-67.
12. Cabrera R, Sha Z, Vadakkan TJ, et al. Proteasome nuclear import mediated by Arc3 can influence efficient DNA damage repair and mitosis in Schizosaccharomyces pombe. Mol Biol Cell 2010; 21(18): 3125-36.
13. Daulny A, Tansey WP. Damage control: DNA repair, transcription, and the ubiquitin-proteasome system. DNA Repair (Amst) 2009; 8(4): 444-8.
14. Catalgol B, Ziaja I, Breusing N, et al. The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression. J Biol Chem 2009; 284(44): 30076-86.
15. Zimmermann J, Lamerant N, Grossenbacher R, Furst P. Protea-some- and p38-dependent regulation of ERK3 expression. J Biol Chem 2001; 276(14): 10759-66.
16. Bregegere F, Milner Y, Friguet B. The ubiquitin-proteasome system at the crossroads of stress-response and aging pathways: a handle for skin care? Aging Res Rev 2006; 5(1): 60-90.
17. Pirlich M, Muller C, Sandig G, et al. Increased proteolysis after single-dose exposure with hepatotoxins in HepG2 cells. Free Radic Biol Med 2002; 33(2): 283-91.
18. Seifert U, Kruger E. Remodelling of the ubiquitin-proteasome system in response to interferons. Biochem Soc Trans 2008; 36(Pt 5): 879-84.
19. Borissenko L, Groll M. Diversity of proteasomal missions: fine tuning of the immune response. Biol Chem 2007; 388(9): 947-55.
20. [20] Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S protea-some complex during oxidative stress. Sci Signal 2010; 3(151): ra88.
21. Strosova M, Voss P, Engels M, Horakova L, Grune T. Limited degradation of oxidized calmodulin by proteasome: formation of peptides. Arch Biochem Biophys 2008; 475(1): 50-4.
22. Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997; 386(6624): 463-71.
23. Unno M, Mizushima T, Morimoto Y, et al. Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution. J Biochem 2002; 131(2): 171-3.
24. Ruschak AM, Religa TL, Breuer S, Witt S, Kay LE. The protea-some antechamber maintains substrates in an unfolded state. Nature 2010; 467(7317): 868-71.
25. Baldovino S, Piccinini M, Anselmino A, et al. Structural and functional properties of proteasomes purified from the human kidney. J Nephrol 2006; 19(6): 710-16.
26. Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996; 65: 801-47.
27. Ustrell V, Hoffman L, Pratt G, Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J 2002; 21(13): 3516-25.
28. Ustrell V, Pratt G, Gorbea C, Rechsteiner M. Purification and assay of proteasome activator PA200. Methods Enzymol 2005; 398: 321-9.
29. Kisselev AF, Akopian TN, Castillo V, Goldberg AL. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell 1999; 4(3): 395-402.
30. Jager S, Groll M, Huber R, Wolf DH, Heinemeyer W. Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J Mol Biol 1999; 291(4): 997-1013.
31. Shringarpure R, Grune T, Davies KJ. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001; 58(10): 1442-50.
32. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79(1): 13-21.
33. Kohler A, Cascio P, Leggett DS, Woo KM, Goldberg AL, Finley D. The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol Cell 2001; 7(6): 1143-1152.
34. Kohler A, Bajorek M, Groll M, et al. The substrate translocation channel of the proteasome. Biochimie 2001; 83(3-4): 325-332.
35. Tanaka K. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci 2009; 85(1): 12-36.
36. Eytan E, Ganoth D, Armon T, Hershko A. ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proc Natl Acad Sci U S A 1989; 86(20): 7751-5.
37. Orino E, Tanaka K, Tamura T, Sone S, Ogura T, Ichihara A. ATP-dependent reversible association of proteasomes with multiple protein components to form 26S complexes that degrade ubiquitinated proteins in human HL-60 cells. FEBS Lett 1991; 284(2): 206-10.
38. Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 2000; 275(19): 14336-45.
39. Brooks P, Fuertes G, Murray RZ, et al. Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem J 2000; 346 Pt 1: 155-61.
40. Burroughs AM, Balaji S, Iyer LM, Aravind L. Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold. Biol Direct 2007; 2: 18.
41. Pickart CM, Eddins MJ. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 2004; 1695(1-3): 55-72.
42. Barriere H, Nemes C, Du K, Lukacs GL. Plasticity of polyubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery. Mol Biol Cell 2007; 18(10): 3952-65.
43. Mosesson Y, Shtiegman K, Katz M, et al. Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquity-lation. J Biol Chem 2003; 278(24): 21323-6.
44. Sun L, Chen ZJ. The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 2004; 16(2): 119-26.
45. Wilkinson KD, Urban MK, Haas AL. Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J Biol Chem 1980; 255(16): 7529-32.
46. Hochstrasser M. Lingering mysteries of ubiquitin-chain assembly. Cell 2006; 124(1): 27-34.
47. Reiss Y, Heller H, Hershko A. Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein. J Biol Chem 1989; 264(18): 10378-83.
48. Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999; 96(5): 635-44.
49. Kuhlbrodt K, Mouysset J, Hoppe T. Orchestra for assembly and fate of polyubiquitin chains. Essays Biochem 2005; 41: 1-14.
50. Verdecia MA, Joazeiro CA, Wells NJ, et al. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol Cell 2003; 11(1): 249-59.
51. Korolchuk VI, Menzies FM, Rubinsztein DC. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 2010; 584(7): 1393-8.
52. Pankiv S, Clausen TH, Lamark T, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282(33): 24131-45.
53. Clague MJ, Urbe S. Ubiquitin: same molecule, different degradation pathways. Cell 2010; 143(5): 682-5.
54. Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002; 419(6903): 135-41.
55. Thomson TM, Guerra-Rebollo M. Ubiquitin and SUMO signalling in DNA repair. Biochem Soc Trans 2010; 38(Pt 1): 116-31.
56. Garcia-Higuera I, Taniguchi T, Ganesan S, et al. Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. Mol Cell 2001; 7(2): 249-62.
57. Angers S, Li T, Yi X, MacCoss MJ, Moon RT, Zheng N. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 2006; 443(7111): 590-3.
58. Sugasawa K, Okuda Y, Saijo M, et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 2005; 121(3): 387-400.
59. Wang H, Zhai L, Xu J, et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 2006; 22(3): 383-94.
60. Huen MS, Grant R, Manke I, et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007; 131(5): 901-14.
61. Doil C, Mailand N, Bekker-Jensen S, et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 2009; 136(3): 435-46.
62. Golden TR, Hinerfeld DA, Melov S. Oxidative stress and aging: beyond correlation. Aging Cell 2002; 1(2): 117-23.
63. Girotti AW. Lipid hydroperoxide generation, turnover, and effector action in biological systems. J Lipid Res 1998; 39(8): 1529-42.
64. van LB, Markkanen E, Hubscher U. Oxygen as a friend and enemy: How to combat the mutational potential of 8-oxo-guanine. DNA Repair (Amst) 2010; 9(6): 604-16.
65. Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272(33): 20313-16.
66. Stadtman ER, Levine RL. Protein oxidation. Ann N Y Acad Sci 2000; 899: 191-208.
67. Kido K, Kassell B. Oxidation of methionine residues of porcine and bovine pepsins. Biochemistry 1975; 14(3): 631-5.
68. Pryor WA, Jin X, Squadrito GL. One- and two-electron oxidations of methionine by peroxynitrite. Proc Natl Acad Sci USA 1994; 91(23): 11173-7.
69. Moreno JJ, Pryor WA. Inactivation of alpha 1-proteinase inhibitor by peroxynitrite. Chem Res Toxicol 1992; 5(3): 425-31.
70. Zhao F, Yang J, Schoneich C. Effects of polyaminocarboxylate metal chelators on iron-thiolate induced oxidation of methionine-and histidine-containing peptides. Pharm Res 1996; 13(6): 931-38.
71. Mudd JB, Leavitt R, Ongun A, McManus TT. Reaction of ozone with amino acids and proteins. Atmos Environ 1969; 3(6): 669-2.
72. Picot CR, Moreau M, Juan M, et al. Impairment of methionine sulfoxide reductase during UV irradiation and photoaging. Exp Gerontol 2007; 42(9): 859-63.
73. Friguet B. Protein repair and degradation during aging. Scientific-WorldJournal 2002; 2: 248-54.
74. 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(23): 12920-5.
75. Petropoulos I, Mary J, Perichon M, Friguet B. Rat peptide me-thionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 2001; 355(Pt 3): 819-25.
76. Le HT, Chaffotte AF, mey-Thomas E, Vinh J, Friguet B, Mary J. Impact of hydrogen peroxide on the activity, structure, and con-formational stability of the oxidized protein repair enzyme me-thionine sulfoxide reductase A. J Mol Biol 2009; 393(1): 58-66.
77. Jung T, Engels M, Kaiser B, Poppek D, Grune T. Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress. Free Radic Biol Med 2006; 40(8): 1303-12.
78. Catalgol B, Wendt B, Grimm S, Breusing N, Ozer NK, Grune T. Chromatin repair after oxidative stress: role of PARP-mediated proteasome activation. Free Radic Biol Med 2010; 48(5): 673-80.
79. Powell SR, Wang P, Katzeff H, et al. Oxidized and ubiquitinated proteins may predict recovery of postischemic cardiac function: essential role of the proteasome. Antioxid Redox Signal 2005; 7(5-6): 538-46.
80. 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(2): 229-38.
81. Petropoulos I, Conconi M, Wang X, et al. 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(5): B220-B7.
82. Moskovitz J, Oien DB. Protein carbonyl and the methionine sulfox-ide reductase system. Antioxid Redox Signal 2010; 12(3): 405-15.
83. Amici A, Levine RL, Tsai L, Stadtman ER. Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J Biol Chem 1989; 264(6): 3341-6.
84. Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272(33): 20313-16.
85. Bar-Shai M, Carmeli E, Ljubuncic P, Reznick AZ. Exercise and immobilization in aging animals: the involvement of oxidative stress and NF-kappaB activation. Free Radic Biol Med 2008; 44(2): 202-14.
86. Ishii N. Oxidative stress and aging in Caenorhabditis elegans. Free Radic Res 2000; 33(6): 857-64.
87. Goto S, Nakamura A, Radak Z, et al. Carbonylated proteins in aging and exercise: immunoblot approaches. Mech Aging Dev 1999; 107(3): 245-53.
88. Smith CD, Carney JM, Starke-Reed PE, et al. Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA 1991; 88(23): 10540-3.
89. Garland D, Russell P, Zigler JS, Jr. The oxidative modification of lens proteins. Basic Life Sci 1988; 49: 347-52.
90. Oliver CN, Ahn BW, Moerman EJ, Goldstein S, Stadtman ER. Age-related changes in oxidized proteins. J Biol Chem 1987; 262(12): 5488-91.
91. Tyedmers J, Mogk A, Bukau B. Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 2010; 11(11): 777-88.
92. Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 2005; 24(7): 1311-7.
93. [93] Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10 Suppl: S10-S7.
94. Tsuji S. Genetics of neurodegenerative diseases: insights from high-throughput resequencing. Hum Mol Genet 2010; 19(R1): R65-R70.
95. Laskowska E, Matuszewska E, Kuczynska-Wisnik D. Small heat shock proteins and protein-misfolding diseases. Curr Pharm Bio-technol 2010; 11(2): 146-57.
96. McHaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. Biochemistry 2009; 48(18): 3828-37.
97. Drummond DA, Wilke CO. The evolutionary consequences of erroneous protein synthesis. Nat Rev Genet 2009; 10(10): 715-24.
98. Drummond DA, Wilke CO. Mistranslation-induced protein mis-folding as a dominant constraint on coding-sequence evolution. Cell 2008; 134(2): 341-52.
99. Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggre-gation mediated by heat-shock protein Hsp104. Nature 1994; 372(6505): 475-8.
100. Bosl B, Grimminger V, Walter S. The molecular chaperone Hsp104--a molecular machine for protein disaggregation. J Struct Biol 2006; 156(1): 139-48.
101. Jung T, Bader N, Grune T. Oxidized proteins: intracellular distribution and recognition by the proteasome. Arch Biochem Biophys 2007; 462(2): 231-37.
102. Pacifici RE, Kono Y, Davies KJ. Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. J Biol Chem 1993; 268(21): 15405-11.
103. Buchberger A, Bukau B, Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 2010; 40(2): 238-52.
104. Rudiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 2001; 20(5): 1042-50.
105. Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005; 62(6): 670-84.
106. Broadley SA, Hartl FU. The role of molecular chaperones in human misfolding diseases. FEBS Lett 2009; 583(16): 2647-53.
107. Breusing N, Grune T. Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol Chem 2008; 389(3): 203-9.
108. Giulivi C, Pacifici RE, Davies KJ. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Arch Biochem Biophys 1994; 311(2): 329-41.
109. Ferrington DA, Sun H, Murray KK, et al. Selective degradation of oxidized calmodulin by the 20 S proteasome. J Biol Chem 2001; 276(2): 937-3.
110. Davies KJ. Degradation of oxidized proteins by the 20S protea-some. Biochimie 2001; 83(3-4): 301-10.
111. Squier TC. Oxidative stress and protein aggregation during biological aging. Exp Gerontol 2001; 36(9): 1539-50.
112. Terman A, Brunk UT. Oxidative stress, accumulation of biological 'garbage', and aging. Antioxid Redox Signal 2006; 8(1-2): 197-204.
113. Terman A, Brunk UT. Lipofuscin: mechanisms of formation and increase with age. APMIS 1998; 106(2): 265-76.
114. Merker K, Grune T. Proteolysis of oxidised proteins and cellular senescence. Exp Gerontol 2000; 35(6-7): 779-86.
115. Sitte N, Merker K, Grune T, von ZT. Lipofuscin accumulation in proliferating fibroblasts in vitro: an indicator of oxidative stress. Exp Gerontol 2001; 36(3): 475-86.
116. Stroikin Y, Dalen H, Brunk UT, Terman A. Testing the garbage accumulation theory of aging: mitotic activity protects cells from death induced by inhibition of autophagy. Biogerontology 2005; 6(1): 39-47.
117. Hohn A, Jung T, Grimm S, Grune T. Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells. Free Radic Biol Med 2010; 48(8): 1100-08.
118. Jung T, Bader N, Grune T. Lipofuscin: formation, distribution, and metabolic consequences. Ann N Y Acad Sci 2007; 1119: 97-111.
119. Terman A, Gustafsson B, Brunk UT. Autophagy, organelles and aging. J Pathol 2007; 211(2): 134-43.
120. Brunk UT, Terman A. The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis. Eur J Biochem 2002; 269(8): 1996-2002.
121. Friguet B, Szweda LI. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett 1997; 405(1): 21-5.
122. Sitte N, Merker K, von ZT, Grune T. Protein oxidation and degradation during proliferative senescence of human MRC-5 fibro-blasts. Free Radic Biol Med 2000; 28(5): 701-8.
123. Sitte N, Huber M, Grune T, et al. Proteasome inhibition by lipofus-cin/ceroid during postmitotic aging of fibroblasts. FASEB J 2000; 14(11): 1490-8.
124. Sayre LM, Moreira PI, Smith MA, Perry G. Metal ions and oxida-tive protein modification in neurological disease. Ann Ist Super Sanita 2005; 41(2): 143-64.
125. Hohn A, Jung T, Grimm S, Catalgol B, Weber D, Grune T. Lipo-fuscin inhibits the proteasome by binding to surface motifs. Free Radic Biol Med 2010.
126. Szweda PA, Camouse M, Lundberg KC, Oberley TD, Szweda LI. Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems. Aging Res Rev 2003; 2(4): 383-405.
127. Sohal RS, Dubey A. Mitochondrial oxidative damage, hydrogen peroxide release, and aging. Free Radic Biol Med 1994; 16(5): 621-6.
128. Elleder M, Sokolova J, Hrebicek M. Follow-up study of subunit c of mitochondrial ATP synthase (SCMAS) in Batten disease and in unrelated lysosomal disorders. Acta Neuropathol 1997; 93(4): 379-90.
129. 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(12): 2519-30.
130. Chondrogianni N, Gonos ES. Proteasome inhibition induces a senescence-like phenotype in primary human fibroblasts cultures. Biogerontology 2004; 5(1): 55-61.
131. Bulteau AL, Szweda LI, Friguet B. Mitochondrial protein oxidation and degradation in response to oxidative stress and aging. Exp Gerontol 2006; 41(7): 653-7.
132. Xu H, Chen M, Manivannan A, Lois N, Forrester JV. Age-dependent accumulation of lipofuscin in perivascular and subretinal microglia in experimental mice. Aging Cell 2008; 7(1): 58-68.
133. Terman A, Abrahamsson N, Brunk UT. Ceroid/lipofuscin-loaded human fibroblasts show increased susceptibility to oxidative stress. Exp Gerontol 1999; 34(6): 755-70.
134. Merker K, Ullrich O, Schmidt H, Sitte N, Grune T. Stability of the nuclear protein turnover during cellular senescence of human fi-broblasts. FASEB J 2003; 17(13): 1963-5.
135. Singh R, Barden A, Mori T, Beilin L. Advanced glycation end-products: a review. Diabetologia 2001; 44(2): 129-46.
136. Desai KM, Chang T, Wang H, et al. Oxidative stress and aging: is methylglyoxal the hidden enemy? Can J Physiol Pharmacol 2010; 88(3): 273-84.
137. Vlassara H. Advanced glycation end-products and atherosclerosis. Ann Med 1996; 28(5): 419-26.
138. Boel E, Selmer J, Flodgaard HJ, Jensen T. Diabetic late complications: will aldose reductase inhibitors or inhibitors of advanced glycosylation endproduct formation hold promise? J Diabetes Complications 1995; 9(2): 104-29.
139. Farouque HM, O'Brien RC, Meredith IT. Diabetes mellitus and coronary heart disease--from prevention to intervention: Part I. Aust N Z J Med 2000; 30(3): 351-9.
140. Miranda HV, Outeiro TF. The sour side of neurodegenerative disorders: the effects of protein glycation. J Pathol 2010; 221: 13-25.
141. Kueper T, Grune T, Prahl S, et al. Vimentin is the specific target in skin glycation. Structural prerequisites, functional consequences, and role in skin aging. J Biol Chem 2007; 282(32): 23427-36.
142. Monnier VM, Glomb M, Elgawish A, Sell DR. The mechanism of collagen cross-linking in diabetes: a puzzle nearing resolution. Diabetes 1996; 45 Suppl 3: S67-72.
143. Couppe C, Hansen P, Kongsgaard M, et al. Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. J Appl Physiol 2009; 107(3): 880-6.
144. Paul RG, Bailey AJ. The effect of advanced glycation end-product formation upon cell-matrix interactions. Int J Biochem Cell Biol 1999; 31(6): 653-60.
145. Nozynski J, Zakliczynski M, Konecka-Mrowka D, et al. Advanced glycation end-products in myocardium-supported vessels: Effects of heart failure and diabetes mellitus. J Heart Lung Transplant 2011.
146. Yan SF, Ramasamy R, Schmidt AM. Mechanisms of disease: advanced glycation end-products and their receptor in inflammation and diabetes complications. Nat Clin Pract Endocrinol Metab 2008; 4(5): 285-93.
147. Grimm S, Hoehn A, Davies KJ, Grune T. Protein oxidative modifications in the aging brain: Consequence for the onset of neurode-generative disease. Free Radic Res 2011; 45(1): 73-88.
148. Terman A, Kurz T, Gustafsson B, Brunk UT. The involvement of lysosomes in myocardial aging and disease. Curr Cardiol Rev 2008; 4(2): 107-15.
149. Nagaraj RH, Linetsky M, Stitt AW. The pathogenic role of Mail-lard reaction in the aging eye. Amino Acids 2010.
150. Combaret L, Dardevet D, Bechet D, Taillandier D, Mosoni L, Attaix D. Skeletal muscle proteolysis in aging. Curr Opin Clin Nutr Metab Care 2009; 12(1): 37-41.
151. Lindner AB, Madden R, Demarez A, Stewart EJ, Taddei F. Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation. Proc Natl Acad Sci USA 2008; 105(8): 3076-81.
152. Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003; 299(5613): 1751-3.
153. Rujano MA, Bosveld F, Salomons FA, et al. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol 2006; 4(12): e417.
154. Davies KJ, Shringarpure R. Preferential degradation of oxidized proteins by the 20S proteasome may be inhibited in aging and in inflammatory neuromuscular diseases. Neurology 2006; 66(2 Suppl 1): S93-6.
155. Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Bio-chem Biophys Res Commun 2003; 305(3): 709-18.
156. 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(1): 311-8.
157. Farout L, Friguet B. Proteasome function in aging and oxidative stress: implications in protein maintenance failure. Antioxid Redox Signal 2006; 8(1-2): 205-16.
158. 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(12): 11840-50.
159. [159] 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 phe-notype upon its inhibition and resistance to stress upon its activation. J Biol Chem 2003; 278(30): 28026-37.
160. Shang F, Taylor A. Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and prote-olytic activities in bovine lens epithelial cells. Biochem J 1995; 307 (Pt 1): 297-303.
161. Shang F, Gong X, Taylor A. Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated. J Biol Chem 1997; 272(37): 23086-93.
162. Medicherla B, Goldberg AL. Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins. J Cell Biol 2008; 182(4): 663-73.
163. Dudek EJ, Shang F, Valverde P, Liu Q, Hobbs M, Taylor A. Selectivity of the ubiquitin pathway for oxidatively modified proteins: relevance to protein precipitation diseases. FASEB J 2005; 19(12): 1707-9.
164. Dantuma NP, Lindsten K. Stressing the ubiquitin-proteasome system. Cardiovasc Res 2010; 85(2): 263-71.
165. Reinheckel T, Ullrich O, Sitte N, Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000; 377(1): 65-8.
166. Kurepa J, Wang S, Li Y, Smalle J. Proteasome regulation, plant growth and stress tolerance. Plant Signal Behav 2009; 4(10): 924-7.
167. Louie JL, Kapphahn RJ, Ferrington DA. Proteasome function and protein oxidation in the aged retina. Exp Eye Res 2002; 75(3): 271-84.
168. Keller JN, Hanni KB, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem 2000; 75(1): 436-9.
169. Keller JN, Hanni KB, Markesbery WR. Possible involvement of proteasome inhibition in aging: implications for oxidative stress. Mech Aging Dev 2000; 113(1): 61-70.
170. 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(2): 197-203.
171. Bulteau AL, Szweda LI, Friguet B. Age-dependent declines in proteasome activity in the heart. Arch Biochem Biophys 2002; 397(2): 298-304.
172. Carrard G, Dieu M, Raes M, Toussaint O, Friguet B. Impact of aging on proteasome structure and function in human lymphocytes. Int J Biochem Cell Biol 2003; 35(5): 728-39.
173. Hayashi T, Goto S. Age-related changes in the 20S and 26S protea-some activities in the liver of male F344 rats. Mech Aging Dev 1998; 102(1): 55-66.
174. Kapphahn RJ, Bigelow EJ, Ferrington DA. Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina. Exp Eye Res 2007; 84(4): 646-54.
175. Demasi M, Silva GM, Netto LE. 20 S proteasome from Saccharo-myces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 2003; 278(1): 679-85.
176. Andersson M, Sjostrand J, Karlsson JO. Differential inhibition of three peptidase activities of the proteasome in human lens epithelium by heat and oxidation. Exp Eye Res 1999; 69(1): 129-38.
177. Ferrington DA, Kapphahn RJ. Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal. FEBS Lett 2004; 578(3): 217-23.
178. Conley KE, Marcinek DJ, Villarin J. Mitochondrial dysfunction and age. Curr Opin Clin Nutr Metab Care 2007; 10(6): 688-92.
179. Lee CK, Klopp RG, Weindruch R, Prolla TA. Gene expression profile of aging and its retardation by caloric restriction. Science 1999; 285(5432): 1390-3.
180. [180] Gray DA, Tsirigotis M, Woulfe J. Ubiquitin, proteasomes, and the aging brain. Sci Aging Knowledge Environ 2003; 2003(34): RE6.
181. Mura CV, Gong X, Taylor A, Villalobos-Molina R, Scrofano MM. Effects of calorie restriction and aging on the expression of anti-oxidant enzymes and ubiquitin in the liver of Emory mice. Mech Aging Dev 1996; 91(2): 115-29.
182. Scrofano MM, Shang F, Nowell TR, Jr., et al. Aging, calorie restriction and ubiquitin-dependent proteolysis in the livers of Emory mice. Mech Aging Dev 1998; 101(3): 277-96.
183. Coelho SG, Hearing VJ. UVA tanning is involved in the increased incidence of skin cancers in fair-skinned young women. Pigment Cell Melanoma Res 2010; 23(1): 57-63.
184. de Gruijl FR, van Kranen HJ, Mullenders LH. UV-induced DNA damage, repair, mutations and oncogenic pathways in skin cancer. J Photochem Photobiol B 2001; 63(1-3): 19-27.
185. Bulteau AL, Moreau M, Nizard C, Friguet B. Impairment of pro-teasome function upon UVA- and UVB-irradiation of human keratinocytes. Free Radic Biol Med 2002; 32(11): 1157-70.
186. Koziel R, Greussing R, Maier AB, Declercq L, Jansen-Durr P. Functional Interplay between Mitochondrial and Proteasome Activity in Skin Aging. J Invest Dermatol 2010.
187. Torres CA, Perez VI. Proteasome modulates mitochondrial function during cellular senescence. Free Radic Biol Med 2008; 44(3): 403-14.
188. Terman A, Sandberg S. Proteasome inhibition enhances lipofuscin formation. Ann N Y Acad Sci 2002; 973: 309-12.
189. Alexiades-Armenakas MR, Dover JS, Arndt KA. The spectrum of laser skin resurfacing: nonablative, fractional, and ablative laser resurfacing. J Am Acad Dermatol 2008; 58(5): 719-37.
190. Graw J. Genetics of crystallins: cataract and beyond. Exp Eye Res 2009; 88(2): 173-89.
191. Hoehenwarter W, Klose J, Jungblut PR. Eye lens proteomics. Amino Acids 2006; 30(4): 369-89.
192. Talla V, Srinivasan N, Balasubramanian D. Visualization of in situ intracellular aggregation of two cataract-associated human gamma-crystallin mutants: lose a tail, lose transparency. Invest Ophthalmol Vis Sci 2008; 49(8): 3483-90.
193. Stiuso P, Libondi T, Facchiano AM, et al. Alteration in the ubiq-uitin structure and function in the human lens: a possible mechanism of senile cataractogenesis. FEBS Lett 2002; 531(2): 162-7.
194. Hooper P, Jutai JW, Strong G, Russell-Minda E. Age-related macular degeneration and low-vision rehabilitation: a systematic review. Can J Ophthalmol 2008; 43(2): 180-7.
195. Fletcher AE. Free radicals, antioxidants and eye diseases: evidence from epidemiological studies on cataract and age-related macular degeneration. Ophthalmic Res 2010; 44(3): 191-8.
196. Joussen AM, Bornfeld N. The treatment of wet age-related macular degeneration. Dtsch Arztebl Int 2009; 106(18): 312-7.
197. Anderson DH, Mullins RF, Hageman GS, Johnson LV. A role for local inflammation in the formation of drusen in the aging eye. Am J Ophthalmol 2002; 134(3): 411-31.
198. Khandhadia S, Lotery A. Oxidation and age-related macular degeneration: insights from molecular biology. Expert Rev Mol Med 2010; 12: e34.
199. Lamb LE, Zareba M, Plakoudas SN, Sarna T, Simon JD. Retinyl palmitate and the blue-light-induced phototoxicity of human ocular lipofuscin. Arch Biochem Biophys 2001; 393(2): 316-20.
200. Li Y, Wang YS, Shen XF, et al. Alterations of activity and intracel-lular distribution of the 20S proteasome in aging retinal pigment epithelial cells. Exp Gerontol 2008; 43(12): 1114-22.
201. Ethen CM, Hussong SA, Reilly C, Feng X, Olsen TW, Ferrington DA. Transformation of the proteasome with age-related macular degeneration. FEBS Lett 2007; 581(5): 885-90.
202. World Health Organization. World Health Organization Fact Sheet. The top 10 causes of death. Geneva, Switzerland 2008.
203. Yoshida H, Kisugi R. Mechanisms of LDL oxidation. Clin Chim Acta 2010; 411(23-24): 1875-82.
204. Heinecke JW. Oxidants and antioxidants in the pathogenesis of atherosclerosis: implications for the oxidized low density lipopro-tein hypothesis. Atherosclerosis 1998; 141(1): 1-15.
205. Galkina E, Ley K. Immune and inflammatory mechanisms of atherosclerosis (*). Annu Rev Immunol 2009; 27: 165-97.
206. Naghavi M, Libby P, Falk E, et al. From vulnerable plaque to vulnerable patient: a call for new definitions and risk assessment strategies: Part I. Circulation 2003; 108(14): 1664-72.
207. Naghavi M, Libby P, Falk E, et al. From vulnerable plaque to vulnerable patient: a call for new definitions and risk assessment strategies: Part II. Circulation 2003; 108(15): 1772-8.
208. Hermann J, Gulati R, Napoli C, et al. Oxidative stress-related increase in ubiquitination in early coronary atherogenesis. FASEB J 2003; 17(12): 1730-2.
209. Herrmann J, Soares SM, Lerman LO, Lerman A. Potential role of the ubiquitin-proteasome system in atherosclerosis: aspects of a protein quality disease. J Am Coll Cardiol 2008; 51(21): 2003-10.
210. Herrmann J, Saguner AM, Versari D, et al. Chronic proteasome inhibition contributes to coronary atherosclerosis. Circ Res 2007; 101(9): 865-74.
211. Rocken C, Tautenhahn J, Buhling F, et al. Prevalence and pathology of amyloid in atherosclerotic arteries. Arterioscler Thromb Vasc Biol 2006; 26(3): 676-677.
212. Medeiros LA, Khan T, El Khoury JB, et al. Fibrillar amyloid protein present in atheroma activates CD36 signal transduction. J Biol Chem 2004; 279(11): 10643-8.
213. Beckmann N, Schuler A, Mueggler T, et al. Age-dependent cere-brovascular abnormalities and blood flow disturbances in APP23 mice modeling Alzheimer's disease. J Neurosci 2003; 23(24): 8453-9.
214. Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta-and gamma-secretases. FEBS Lett 2000; 483(1): 6-10.
215. Gregori L, Hainfeld JF, Simon MN, Goldgaber D. Binding of amyloid beta protein to the 20 S proteasome. J Biol Chem 1997; 272(1): 58-62.
216. Tseng BP, Green KN, Chan JL, Blurton-Jones M, LaFerla FM. Abeta inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiol Aging 2008; 29(11): 1607-18.
217. Park HM, Kim JA, Kwak MK. Protection against amyloid beta cytotoxicity by sulforaphane: role of the proteasome. Arch Pharm Res 2009; 32(1): 109-15.
218. Zhao X, Yang J. Amyloid-beta peptide is a substrate of the human 20S proteasome. ACS Chem Neurosci 2010; 1(10): 655-60.
219. Shringarpure R, Grune T, Sitte N, Davies KJ. 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell Mol Life Sci 2000; 57(12): 1802-9.
220. Lehman NL. The ubiquitin proteasome system in neuropathology. Acta Neuropathol 2009; 118(3): 329-47.
221. Poppek D, Keck S, Ermak G, et al. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J 2006; 400(3): 511-20.
222. Keck S, Nitsch R, Grune T, Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 2003; 85(1): 115-22.
223. Lee VM, Goedert M, Trojanowski JQ. Neurodegenerative tauopathies. Annu Rev Neurosci 2001; 24: 1121-59.
224. Waldemar G, Dubois B, Emre M, et al. Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline. Eur J Neurol 2007; 14(1): e1-26.
225. Ramesh BJ, Lamar SM, Peng J, et al. Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegen-eration. J Neurochem 2008; 106(1): 107-20.
226. [226] Tan JM, Wong ES, Dawson VL, Dawson TM, Lim KL. Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy. Autophagy 2007; 4(2).
227. Finkbeiner S, Mitra S. The ubiquitin-proteasome pathway in Huntington's disease. ScientificWorldJournal 2008; 8: 421-33.
228. Feng Z, Jin S, Zupnick A, et al. p53 tumor suppressor protein regulates the levels of huntingtin gene expression. Oncogene 2006; 25(1): 1-7.
229. Diaz-Hernandez M, Valera AG, Moran MA, et al. Inhibition of 26S proteasome activity by huntingtin filaments but not inclusion bodies isolated from mouse and human brain. J Neurochem 2006; 98(5): 1585-96.
230. Walker FO. Huntington's disease. Lancet 2007; 369(9557): 218-28.
231. Ragland M, Hutter C, Zabetian C, Edwards K. Association between the ubiquitin carboxyl-terminal esterase L1 gene (UCHL1) S18Y variant and Parkinson's Disease: a HuGE review and meta-analysis. Am J Epidemiol 2009; 170(11): 1344-57.
232. Ruiperez V, Darios F, Davletov B. Alpha-synuclein, lipids and Parkinson's disease. Prog Lipid Res 2010; 49(4): 420-8.
233. Kawahara K, Hashimoto M, Bar-On P, et al. alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease. J Biol Chem 2008; 283(11): 6979-87.
234. Setsuie R, Wada K. The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem Int 2007; 51(2-4): 105-11.
235. Setsuie R, Wang YL, Mochizuki H, et al. Dopaminergic neuronal loss in transgenic mice expressing the Parkinson's disease-associated UCH-L1 I93M mutant. Neurochem Int 2007; 50(1): 119-29.
236. Giasson BI, Duda JE, Murray IV, et al. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synu-cleinopathy lesions. Science 2000; 290(5493): 985-9.
237. Bedford L, Lowe J, Dick LR, Mayer RJ, Brownell JE. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov 2011; 10(1): 29-46.
238. Chondrogianni N, Petropoulos I, Franceschi C, Friguet B, Gonos ES. Fibroblast cultures from healthy centenarians have an active proteasome. Exp Gerontol 2000; 35(6-7): 721-8.
239. Huang Q, Figueiredo-Pereira ME. Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications. Apop-tosis 2010; 15(11): 1292-311.
240. Shin Y, Klucken J, Patterson C, Hyman BT, McLean PJ. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteaso-mal and lysosomal pathways. J Biol Chem 2005; 280(25): 23727-34.
241. Yasuda T, Miyachi S, Kitagawa R, et al. Neuronal specificity of alpha-synuclein toxicity and effect of Parkin co-expression in primates. Neuroscience 2007; 144(2): 743-53.
242. 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(1-2): 136-43.