The impact of specific oxidized amino acids on protein turnover in J774 cells

Biochemical Journal

Volumn 410, Issue 1, 2008, Pages 131-140

  Dunlop, Rachael A ^a   Dean, Roger T ^b   Rodgers, Kenneth J ^a  

^a HEART RESEARCH INSTITUTE   (Australia)

^b UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

Author keywords

Aging; Cathepsin B; Dopa; Lysosome; Oxidized protein; Proteasome

Indexed keywords

BIOSYNTHESIS; DEPOSITION; OXIDATION; PROTEINS;

AETIOLOGY; PROTEIN CATABOLISM;

AMINO ACIDS;

CATHEPSIN; LEVODOPA; PROTEASOME; TYROSINE;

AGING; ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; ATHEROSCLEROSIS; AUTOFLUORESCENCE; CONTROLLED STUDY; ENZYME ACTIVITY; IN VITRO STUDY; LYSOSOME; NONHUMAN; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN SYNTHESIS;

AMINO ACIDS; ANIMALS; BASE SEQUENCE; CELL LINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROLYSIS; MICE; OXIDATION-REDUCTION; PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION;

EID: 39749176956     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070161     Document Type: Article

References (45)

1. Halliwell, B. (2006) Oxidative stress and neurodegeneration: where are we now? J. Neurochem. 97, 1634-1658
2. Liu, S. X., Hou, F. F., Guo, Z. J., Nagai, R., Zhang, W. R., Liu, Z. Q., Zhou, Z. M., Zhou, M., Xie, D., Wang, G. B. and Zhang, X. (2006) Advanced oxidation protein products accelerate atherosclerosis through promoting oxidative stress and inflammation. Arterioscler. Thromb. Vasc. Biol. 26, 1156-1162
3. Woods, A. A., Linton, S. M. and Davies, M. J. (2003) Detection of HOCl-mediated protein oxidation products in the extracellular matrix of human atherosclerotic plaques. Biochem. J. 370, 729-735
4. Fu, S., Davies, M. J., Stocker, R. and Dean, R. T. (1998) Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plague. Biochem. J. 333, 519-525
5. Molnar, G. A., Nemes, V., Biro, Z., Ludany, A., Wagner, Z. and Wittmann, I. (2005) Accumulation of the hydroxyl free radical markers meta-, ortho-tyrosine and DOPA in cataractous lenses is accompanied by a lower protein and phenylalanine content of the water-soluble phase. Free Radical Res. 39, 1359-1366
6. Fu, S., Dean, R., Southan, M. and Truscott, R. (1998) The hydroxyl radical in lens nuclear cataractogenesis. J. Biol. Chem. 273, 28603-28609
7. Schmitz-Valckenberg, S., Bindewald-Wittich, A., Dolar-Szczasny, J., Dreyhaupt, J., Wolf, S., Scholl, H. P. and Holz, F. G. (2006) Correlation between the area of increased autofluorescence surrounding geographic atrophy and disease progression in patients with AMD. Invest. Ophthalmol. Visual Sci. 47, 2648-2654
8. Furukawa, Y., Fu, R., Deng, H. X., Siddique, T. and O'Halloran, T. V. (2006) Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu,Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc. Natl. Acad. Sci. U.S.A. 103, 7148-7153
9. Deng, H. X., Shi, Y., Furukawa, Y., Zhai, H., Fu, R., Liu, E., Gorrie, G. H., Khan, M. S., Hung, W. Y., Bigio, E. H. et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 103, 7142-7147
10. Baskol, G., Demir, H., Baskol, M., Kilic, E., Ates, F., Karakukcu, C. and Ustdal, M. (2006) Investigation of protein oxidation and lipid peroxidation in patients with rheumatoid arthritis. Cell Biochem. Funct. 24, 307-311
11. Rodgers, K. J., Hume, P. M., Dunlop, R. A. and Dean, R. T. (2004) Biosynthesis and turnover of DOPA-containing proteins by human cells. Free Radical Biol. Med. 37, 1756-1764
12. Rodgers, K. J., Wang, H., Fu, S. and Dean, R. T. (2002) Biosynthetic incorporation of oxidized amino acids into proteins and their cellular proteolysis. Free Radical Biol. Med. 32, 766-775
13. Gurer-Orhan, H., Ercal, N., Mare, S., Pennathur, S., Orhan, H. and Heinecke, J. W. (2006) Misincorporation of free m-tyrosine into cellular proteins: a potential cytotoxic mechanism for oxidized amino acids. Biochem. J. 395, 277-284
14. Grune, T., Reinheckel, T. and Davies, K. J. (1996) Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem. 271, 15504-15509
15. Sitte, N., Merker, K. and Grune, T. (1998) Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts. FEBS Lett. 440, 399-402
16. Pattison, D. I., Dean, R. T. and Davies, M. J. (2002) Oxidation of DNA, proteins and lipids by DOPA, protein-bound DOPA and related catechol(amine)s. Toxicology 177, 23-37
17. Stadtman, E. R. (2001) Protein oxidation in aging and age-related diseases. Ann. N.Y. Acad. Sci. 928, 22-38
18. Garrison, W. M. (1987) Reaction mechanisms in the radiolysis of peptides, polypeptides and proteins. Chem. Rev. 87, 381-398
19. Akagawa, M., Ishii, Y., Ishii, T., Shibata, T., Yotsu-Yamashita, M., Suyama, K. and Uchida, K. (2006) Metal-catalyzed oxidation of protein-bound dopamine. Biochemistry 45, 15120-15128
20. Rodgers, K. J. and Dean, R. T. (2000) Metabolism of protein bound DOPA in mammals. Int. J. Biochem. Cell Biol. 32, 945-955
21. Gieseg, S. P., Simpson, J. A., Charlton, T. S., Duncan, M. W. and Dean, R. T. (1993) Protein-bound 3,4-dihydroxypbenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 32, 4780-4786
22. Sun, J. Z., Kaur, H., Halliwell, B., Li, X. Y. and Bolli, R. (1993) Use of aromatic hydroxylation of phenylalanine to measure production of hydroxyl radicals after myocardial ischemia in vivo: direct evidence for a pathogenetic role of the hydroxyl radical in myocardial stunning. Circ. Res. 73, 534-549
23. O'Neill, C. A., Fu, L. W., Halliwell, B. and Longhurst, J. C. (1996) Hydroxyl radical production during myocardial ischemia and reperfusion in cats. Am. J. Physiol. 271, H660-H667
24. Rodgers, K. J., Hume, P. M., Morris, J. G. and Dean, R. T. (2006) Evidence for L-dopa incorporation into cell proteins in patients treated with levodopa. J. Neurochem. 98, 1061-1067
25. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
26. Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354
27. Paz, M. A., Fluckiger, R., Boak, A., Kagan, H. M. and Gallop, P. M. (1991) Specific detection of quinoproteins by redox-cycling staining. J. Biol. Chem. 266, 689-692
28. ΔΔCT method. Methods 25, 402-408
29. Kisselev, A. F. and Goldberg, A. L. (2005) Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol. 398, 364-378
30. Orange, R. P. and Moore, E. G. (1976) Functional characterization of rat mast cell arylsulfatase activity. J. Immunol. 117, 2191-2196
31. Ciechanover, A. (2006) Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Exp. Biol. Med. 231, 1197-1211
32. Stadtman, E. R. (2004) Role of oxidant species in aging. Curr. Med. Chem. 11, 1105-1112
33. Dean, R. T., Dunlop, R., Hume, P. and Rodgers, K. J. (2003) Proteolytic 'defences' and the accumulation of oxidized polypeptides in cataractogenesis and atherogenesis. Biochem. Soc. Symp. 70, 135-146
34. Fu, S., Fu, M., Baynes, J. W., Thorpe, S. R. and Dean, R. T. (1998) Presence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs): amino acid oxidation products as a possible source of oxidative stress induced by AGE proteins. Biochem. J. 330, 233-239
35. Giulivi, C., Pacifici, R. E. and Davies, K. J. (1994) Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Arch. Biochem. Biophys. 311, 329-341
36. Pacifici, R. E., Kono, Y. and Davies, K. J. (1993) Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. J. Biol. Chem. 268, 15405-15411
37. Ozawa, K., Headlam, M. J., Mouradov, D., Watt, S. J., Beck, J. L., Rodgers, K. J., Dean, R. T., Huber, T., Otting, G. and Dixon, N. E. (2005) Translational incorporation of L-3,4-dihydroxyphenylalanine into proteins. FEBS J. 272, 3162-3171
38. Ii, K., Ito, H., Kominami, E. and Hirano, A. (1993) Abnormal distribution of cathepsin proteinases and endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam, and senile dementia and in the aged. Virchows Arch. A Pathol. Anat. Histopathol. 423, 185-194
39. Cataldo, A. M., Hamilton, D. J. and Nixon, R. A. (1994) Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease. Brain Res. 640, 68-80
40. Kikuchi, H., Yamada, T., Furuya, H., Doh-ura, K., Ohyagi, Y., Iwaki, T. and Kira, J. (2003) Involvement of cathepsin B in the motor neuron degeneration of amyotrophic lateral sclerosis. Acta Neuropathol. 105, 462-468
41. Ferrario, J. E., Taravini, I. R., Mourlevat, S., Stefano, A., Delfino, M. A., Raisman-Vozari, R., Murer, M. G., Ruberg, M. and Gershanik, O. (2004) Differential gene expression induced by chronic levodopa treatment in the striatum of rats with lesions of the nigrostriatal system. J. Neurochem. 90, 1348-1358
42. Seehafer, S. S. and Pearce, D. A. (2006) You say lipofuscin, we say ceroid: defining autofluorescent storage material. Neurobiol. Aging 27, 576-588
43. Jones, A. F. and Lunec, J. (1987) Protein fluorescence and its relationship to free radical activity. Br. J. Cancer Suppl. 8, 60-65
44. Nilsson, E. and Yin, D. (1997) Preparation of artificial ceroid/lipofuscin by UV-oxidation of subcellular organelles. Mech. Ageing Dev. 99, 61-78
45. Brunk, U. T. and Terman, A. (2002) Lipofuscin: mechanisms of age-related accumulation and influence on cell function. Free Radical Biol. Med. 33, 611-619