Accumulation of altered proteins and ageing: Causes and effects

Experimental Gerontology

Volumn 41, Issue 5, 2006, Pages 464-473

  Hipkiss, Alan R ^a  

^a QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Aberrant polypeptides; AGEs; Aggregation; Aldehydes; Cross linking; Deamidation; Errors; Glycation; Lysosomes; Mitochondria; Oxidation; Proteasomes; Proteolysis; ROS

Indexed keywords

ALDEHYDE; AMINO ACID; CARBONYL DERIVATIVE; CYTOPLASM PROTEIN; GLUCOSE; GLYCOSYLATED PROTEIN; NITRIC OXIDE; PROTEASOME; PROTEINASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE;

AGING; ALZHEIMER DISEASE; ARTICLE; ATHEROSCLEROSIS; CATARACTOGENESIS; CROSS LINKING; DEAMINATION; DIABETES MELLITUS; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DNA REPAIR; GLYCATION; HUMAN; ISOMERIZATION; LIPID PEROXIDATION; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN SYNTHESIS; RACEMIZATION; RIBOSOME; STRESS;

AGING; AMINO ACIDS; ANIMALS; HUMANS; LYSOSOMES; OXIDATION-REDUCTION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CARBONYLATION; PROTEIN FOLDING; PROTEINS; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN SPECIES;

EID: 33646793360     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exger.2006.03.004     Document Type: Article

References (97)

1. Abe H. Role of histidine-related compounds as intracellular proton buffer constituents in vertebrate muscle. Biochem. (Moscow) 65 (2000) 757-765
2. Ahmed N., Dobler D., Dean M., and Thornalley P.J. Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J. Biol. Chem. 280 (2005) 5724-5732
3. Alaghband-Zadeh J., Mehdizadeh S., Khan N.S., O'Farrell A., Bitensky L., and Chayen J. The natural substrate for nitric oxide synthase activity. Cell Biochem. Funct. 19 (2001) 277-280
4. Arnold I., and Langer T. Membrane protein degradation by AAA proteases in mitochondria. Biochim. Biophys. Acta 1592 (2002) 89-96
5. Attaix D., Mosoni L., Dardevet D., Combaret L., Mirand P.P., and Grizard J. Altered responses in skeletal muscle turnover during aging in anabolic and catabolic periods. Int. J. Biochem. Cell Biol. 37 (2005) 1962-1973
6. Augustin S., Nolden M., Muller S., Hardt O., Arnold I., and Langer T. Characterization of peptides released from mitochondria. Evidence for constant proteolysis and peptide efflux. J. Biol. Chem. 280 (2005) 2691-2699
7. Basoah A., Matthews P.M., and Morten K.J. Rapid rates of newly synthesized mitochondrial protein degradation are significant affected by the generation of mitochondrial free radicals. FEBS Lett. 579 (2005) 6511-6517
8. Baynes J.W., and Monnier V.M. The maillard reaction in aging, diabetes and nutrition (1989), Alan R. Liss, Inc., New York
9. Baynes J.W., and Thorpe S.R. Glycoxidation and lipoperoxidation in atherogenesis. Free Rad. Biol. Med. 28 (2000) 1708-1716
10. Berlanga J., Cibrian D., Guillen I., Frere F., Alba J.S., Lopez-Saura P., merino N., Aldama A., Quintela A., Triana M., Montequin J.F., Ajamieh H., Urquiza D., Ahmed N., and Thornalley P.J. Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of cutaneous wounds. Clin. Sci. (Lond.) 109 (2005) 83-95
11. Biswas S.K., Newby D.E., Rahman I., and Megson I.L. Depressed glutathione synthesis precedes oxidative stress and atherogenesis in Apo-E(-/-) mice. Biochem. Biophys. Res. Commun. 338 (2005) 1368-1373
12. Bohr V.A., and Opresko P.L. Genomic instability in human premature aging. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 65-77
13. Bota D.A., and Davies K.J.A. Protein degradation in mitochondria: implications for oxidative stress, aging and disease: a novel etiological classification of mitochondrial proteolytic disorders. Mitochondrion 1 (2001) 33-49
14. Bota D.A., and Davies K.J.A. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 4 (2002) 674-680
15. Bota D.A., van Remmen H., and Davies K.J.A. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett. 532 (2002) 103-106
16. Brownlee M. Advanced protein glycation in diabetes and aging. Ann. Rev. Med. 46 (1995) 223-234
17. Brownlee M. Biochemistry and molecular biology of diabetic complications. Nature 414 (2001) 813-820
18. Brunk U.T., and Terman A. The mitochondrian-lysosomal axis theory of aging. accumulation of damaged mitochondria as a result of imperfect autophagocytosis. Eur. J. Biochem. 269 (2002) 1996-2002
19. Calabrese V., Colobrita C., Guagliano E., Sapienza M., Ravagna A., Cardile V., Scapagnini G., Santoro A.M., Mangiameli, Butterfield D.A., Giuffrida Stella A.M., and Rizzarelli E. Protective effects of carnosine during nitrosative stress in astroglial cell cultures. Neurochem. Res. 30 (2005) 797-807
20. Carrard G., and Friguet B. The proteasome in aging. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 213-231
21. Carrard G., Bulteau A.-L., Petropoulos I., and Friguet B. Impairment of proteasome structure and function in aging. Int. J. Biochem. Cell Biol. 34 (2002) 1461-1474
22. Chaplen F.W.R. Incidence and potential implications of the toxic metabolite methylglyoxal in cell culture: a review. Cytotechnology 26 (1998) 173-183
23. Chavous D.A., Jackson F.R., and O'Conner C.M. Extension of drosophila lifespan by overexpression of a protein repair methyltransferase. Proc. Natl Acad. Sci. USA 98 (2001) 14814-14818
24. Chondrogianni N., Gonos, E.S. 2005. Proteasome dysfunction in mammalian aging: Steps and factors involved. Exp Gerontol. 40, 931-938.
25. Ciehanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6 (2005) 79-86
26. Clarke S. Protein carboxyl methyltransferase: two distinct classes of enzymes. Annu. Rev. Biochem. 54 (1985) 479-506
27. de Pril, R., Fischer, D.F., van Leeiwren, F.W. 2006. Conformation diseases: an umbrella for various disorders with an impaired ubiquitin-proteasome system. Neurobiol. Aging. 27, 515-520.
28. Del Roso A., Vittorini S., Cavallini G., Donati A., Gori Z., Masini M., Pollera M., and Bergamini E. Ageing-related changes in the in vivo function of rat liver autophagy and proteolysis. Exp. Gerontol. 38 (2003) 519-527
29. Dukan S., Farewell A., Ballesteros M., Taddei F., Radman M., and Nystrom T. Protein oxidation in response to increased transcriptional or translational errors. Proc. Acad. Sci. USA 97 (2000) 5746-5749
30. Ellgaard L., and Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4 (2003) 181-191
31. Gerez L., de Haan A., Hol E.M., Fischer D.F., van Leeuwen F.W., van Steeg H., and Benne R. Molecular misreading: the frequency of dinucleotide deletions in neuronal mRNAs for β-amyloid precursor protein and ubiquitin B. Neurobiol. Aging 26 (2004) 145-155
32. Grune T., Jung T., Merker K., and Davies K.J.A. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceriod, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36 (2004) 2519-2530
33. Gugliucci A. Alternative antiglycation mechanisms: are spermine and fructosamine-3-kinase part of a carbonyl damage control pathway?. Med. Hypoth. 64 (2005) 770-777
34. Hazelton G.A., and Lang C.A. Glutathione content of tissues in the aging mouse. Biochem. J. 188 (1980) 25-30
35. Hipkiss A.R. Carnosine, a protective anti-ageing peptide?. Int. J. Biochem. Cell Biol. 30 (1998) 863-868
36. Hipkiss A.R. Errors, mitochondrial dysfunction and ageing. Biogerontology 4 (2003) 397-400
37. Hipkiss A.R. Do developmentally-related changes in constitutive proteolysis affect aberrant protein accumulation and generation of the aged phenotype?. Mech. Ageing Dev. 124 (2003) 575-579
38. Hipkiss A.R. Non-oxidative modification of DNA and proteins. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 145-177
39. Hipkiss A.R. Glycation, ageing and carnosine: are carnivorous diets beneficial?. Mech. Ageing Dev. 126 (2005) 1034-1039
40. Hipkiss A.R. Caloric restriction and ageing-is glycolysis the problem?. Mech. Ageing Dev. 127 (2006) 8-15
41. Hipkiss A.R., Michaelis J., and Syrris P. Non-enzymatic glycosylation of the dipeptide l-carnosine, a potential anti-protein-cross-linking agent. FEBS Lett. 371 (1995) 81-85
42. Hirokawa K., Gomi K., and Kajiyama N. Molecular cloning and expression of novel fructosyl peptide oxidases and their application for the measurement of glycated protein. Biochem. Biophys. Res. Commun. 311 (2003) 104-111
43. Hsu A.L., Murphy C.T., and Kenyon C. Regulation of aging and ag-related disease by DAF-16 and heat shock factor. Science 300 (2003) 1142-1145
44. Husom A.D., Peters E.A., Kolling E.A., Fugere N.A., Thompson L.V., and Ferrington D.A. Altered proteasome function and subunit composition in aged muscle. Arch. Biochem. Biophys. 421 (2004) 67-76
45. Jay, D., Hitomi, H., Griendling, K.K. 2006. Oxidative stress and diabetic cardiovascular complications. Free Rad. Biol. Med. 40, 183-192.
46. Kim E., Lowenson J.D., MacLaren D.C., Clarke S., and Young S.G. Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth and fatal seizures in mice. Proc. Natl Acad. Sci. USA 94 (1997) 6132-6137
47. Kotamraju, S., Matalon, S., Matsunaga, T., Shang, T., Hickman-Davis, J.M., Kalyanaraman, B. 2006. Upregulation of immunoproteasomes by nitric oxide: potential antioxidative mechanism in endothelail cells. Free Radic. Biol. Med. 40, 1034-1044.
48. Lambert A.J., Wang B., and Merry B.J. Exogenous insulin can reverse the effects of caloric restriction on mitochondria. Biochem. Biophys. Res. Commun. 316 (2004) 1196-1201
49. Lee Y., Hsu C., Lin M., Liu K., and Yin M. Histidine and carnosine delay diabetic deterioration in mice and protect human low density lipoprotein against oxidation and glycation. Eur. J. Pharmacol. 512 (2005) 145-150
50. Levine R.L. Carbonyl modified proteins in cellular regulation, aging and disease. Free Radic. Biol. Med. 32 (2002) 790-796
51. Lindahl T. Instability and decay of the primary structure of DNA. Nature 363 (1993) 709-715
52. Lindner H., and Helliger W. Age-dependent deamidation of asparagine residues in proteins. Exp. Gerontol. 36 (2001) 1551-1563
53. Martinez-Vincente, M., Sovak, G., Cuervo, A.M. 2005. Protein degradation and aging. Exp. Gerontol. 40, 622-633.
54. Masternak M.M., Al-Regaiey K.A., Bonkowski M.S., Panici J.A., and Bartke A. Effect of every other day feeding diet on gene expression in normal and in long-lived Ames dwarf mice. Exp. Gerontol. 40 (2005) 491-497
55. Mattson M.P., and Wan R. Beneficial effects of intermittent feeding and caloric restriction on the cardiovascular and cerebrovascular systems. Nutr. Biochem. 16 (2005) 129-137
56. Moskovitz J., Bar-Noy S., Williams W.M., Requena J., Berlett B.S., and Stadtman E.R. Methionine sulphide reductase (MsrA) is a regulator of anti-oxidant defense and lifespan in animals. Proc. Natl Acad. Sci. 98 (2001) 12920-12925
57. Niijima A., Okui T., Matsumura Y., Yamano T., Tsuruoka N., Kiso Y., and Nagai K. Effects of l-carnosine on renal sympathetic nerve activity and DOCA-salt hypertension in rats. Auton. Neurosci. Basic Clin. 97 (2002) 99-102
58. Pamplone R., and Barja G. Aging rate, mitochondrial free-radical production, and constitutive sensitivity to lipid peroxidation: insights from comparative studies. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 47-64
59. Powell, S.R., Wang, P., Divald, A., Teichberg, S., Haridas, V., McCloskey, T.W., Davies, K.J.A., Katzeff, H. 2005. Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins. Free Radic. Biol. Med. 38, 1093-1101.
60. Proctor C.J., Soti C., Boys R.J., Gillespie C.S., Shanley D.P., Wilkinson D.J., and Kirkwood T.B.L. Modelling the actions of chaperones and their role in ageing. Mech. Ageing Dev. 126 (2005) 119-131
61. Radak Z., Sasari M., Nyakas C., Taylor A.W., Ohno H., Nakamoto H., and Goto S. Regular training modulates the accumulation of reactive carbonyl derivatives in mitochondrial and cytosolic fractions of rat skeletal muscle. Arch. Biochem. Biophys. 383 (2000) 114-118
62. Rapoport S., Dubiel W., and Muller M. Proteolysis of mitochondria in reticulocytes during maturation is ubiquitin-dependent and is accompanied by a high rate of ATP hydrolysis. FEBS Lett. 180 (1985) 249-252
63. Rattan S.J.H., Derventzi A., and Clark B.F.C. Protein synthesis, posttranslational modifications, and aging. Ann. NY Acad. Sci. 663 (1992) 48-60
64. Ririe D.G., Roberts P.R., Shouse M.N., and Zaloga G.P. Vasodilatory actions of the dipeptide carnosine. Nutrition 16 (2000) 168-172
65. Ritz-Timme S., and Collins M.J. Racemization of aspartic acid in human proteins. Ageing Res. Rev. 1 (2002) 43-59
66. Robinson N.E. Protein deamidation. Proc. Natl Acad. Sci. USA 99 (2002) 5283-5288
67. Rosenberger R.F. Senescence and the accumulation of abnormal proteins. Mutat. Res. 256 (1991) 255-262
68. - cells. FEMS Lett. 68 (1990) 19-25
69. Schmidt A.M., Hori O., Brett J., Yan S.D., Wautier J.L., and Stern D. Cellular receptors for advanced glycation end products. Implications for induction of oxidative stress and cellular dysfunction in pathologies of vascular lesions. Arterioscler. Thromb. 14 (1994) 1521-1528
70. Seeberg E. Oxidative DNA damage and repair-implications for aging. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 11-25
71. Seidler N.W., and Yeargans G.S. Effects of thermal denaturation on protein glycation. Life Sci. 70 (2002) 1789-1799
72. Shibamoto T. Genotoxicity testing of Maillard reaction products. In: Baynes J.W., and Monnier V.M. (Eds). The Maillard Reaction in Aging, Diabetes and Nutrition (1989), A.R.Liss, Inc., New York 359-376
73. Shimuzu K., Kiuchi Y., Ando K., Hayakawa M., and Kikugawa K. Coordination of oxidized protein hydrolase and the proteasome in the clearance of cytotoxic proteins. Biochem. Biophys. Res. Commun. 424 (2004) 140-146
74. Sitte N. Oxidative damage to proteins. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 27-45
75. Sitte N., and von Zglinicki T. Free radical production and anti-oxidant defense: a primer. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 1-10
76. Soti C., and Csermely P. Aging and molecular chaperones. Exp. Gerontol. 38 (2003) 1037-1040
77. Stadman E.R. Importance of individuality in oxidative stress and aging. Free Radic. Biol. Med. 33 (2002) 597-604
78. Stadtman E.R. Protein oxidation and aging. Science 257 (1992) 1220-1224
79. Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25
80. Stolzing, A., Widmer, R., Jung, T., Voss, P., Grune, T. 2006. Degradation of glycated serum albumin in microglial cells. Free Rad Biol. Med. 40, 1017-1027.
81. Sullivan P.G., Dragicevic N.B., Deng J.-H., Bai Y., Dimayuga E., Ding Q., Chen Q., Bruce-Keller A.J., and Keller J.N. Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J. Biol. Chem. 279 (2004) 20699-20707
82. Szweda P.A., Camouse M., Lundberg K.C., Oberly T.D., and Szweda L.I. Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems. Ageing Res. Rev. 2 (2003) 383-405
83. Szwergold B.S. Intrinsic toxicity of glucose, due to non-enzymatic glycation, is controlled in vivo by deglycating systems including: FN3K-mediated deglycation of fructosamines and transglycation of aldomines. Med. Hypoth. 65 (2005) 337-348
84. Szwergold B.L., Howell S.K., and Beisswenger P.J. Transglycation-a potential new mechanism for deglycation of Schiff's bases. Ann. NY Acad. Sci. 1043 (2005) 845-864
85. Terman A. Garbage catastrophe theory of aging: imperfect removal of oxidative damage?. Redox Rep. 6 (2001) 15-26
86. Terman A., and Brunk U.T. Aging and lysosomal degradation of cellular constituents. In: von Zglinicki T. (Ed). Aging at the Molecular Level (2003), Kluwer, The Netherlands 233-242
87. Thomas J.A., and Mallis R.J. Aging and oxidation of reactive protein sulfhydryls. Exp. Gerontol. 36 (2001) 1519-1526
88. Tomonaga, S., Tachibana, T., Takahashi, H., Sato, M., Denbow, D.M., Furuse, M. 2005. Nitric oxide involves in carnosine-induced hyperactivity in chicks. Eur. J. Pharamacol. 524, 84-88.
89. Tsirigotis M., Zhang M., Chiu R., and Wouters B.G. Sensivity of mammalian cells expressing mutant ubiquitin to protein-damaging agents. J. Biol. Chem. 276 (2001) 46073-46078
90. Verbeke P., Fonager J., Clark B.F.V., and Rattan S.I.S. Heat shock response and ageing: mechanisms and applications. Cell Biol. Int. 25 (2001) 845-857
91. Williams S., Cusco J., Roddy M., Johnston M., and Creager M. Impaired nitric oxide-mediated vasodilation in patients with non-insulin-dependent diabetes mellitus. J. Am. Coll. Cardiol. 27 (1996) 567-574
92. Wu X., and Monnier V.M. Enzymatic deglycation of proteins. Arch. Biochem. Biophys. 419 (2003) 16-24
93. Yan L.-J., and Sohal R.S. Prevention of flight activity prolongs the lifespan of the housefly, musca domestica, and attenuates the age-associated damage to specific proteins. Free Radic. Biol. Med. 29 (2003) 1143-1150
94. Yarian C.S., Rebrin I., and Sohal R.S. Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. Biochem. Biophys. Res. Commun. 330 (2005) 151-156
95. Yarian, C.S., Toroser, D., Sohal, R.S. 2006. Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria in mice. Mech. Ageing Dev. 127, 79-84.
96. Yokoyama K., Fukumoto K., Murakami T., Harada S., Hosono R., Wadha R., Mitsui Y., and Ohkuma S. Extended longevity of Caenorhabtilis elegans by knocking in extra copies of hsp70F, a homolou of mot-2 (mortalin)/mthsp70/Grp75. FEBS Lett. 516 (2002) 53-57
97. Zhu Y., Wang M., Lin H., Huang C., Shi X., and Luo J. Epidermal growth factor up-regulates the transcription of mouse Lon homologue ATP-dependent protease through extracellular signal-regulated protein kinase- and phosphatidylinositol-3-kinase-dependent pathways. Exp. Cell Res. 280 (2002) 97-106