Proteome analysis of substantia nigra and striatal tissue in the mouse MPTP model of Parkinson's disease

Proteomics - Clinical Applications

Volumn 1, Issue 12, 2007, Pages 1559-1569

  Zhao, Xin ^a   Li, Quan ^a   Zhao, Lei ^a   Pu, Xiao Ping ^a,b  

^a PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

MPTP; Parkinson's disease; Substantia nigra and striatum

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; HEAT SHOCK PROTEIN; NEUROTOXIN; PROTEOME;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; C57BL 6 MOUSE; CELL DESTRUCTION; CONTROLLED STUDY; CORPUS STRIATUM; DISEASE MODEL; DOPAMINERGIC NERVE CELL; ENERGY METABOLISM; ENZYME ACTIVITY; MITOCHONDRION; MOUSE; NERVE CELL DEGENERATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEOMICS; SUBSTANTIA NIGRA;

MUS;

EID: 38349126342     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200700077     Document Type: Article

References (58)

1. McNaught, K. S., Olanow, C. W., Halliwell, B., Isacson, O., Jenner, P., Failure of the ubiquitin-proteasome system in Parkinson's disease. Nat. Rev. Neurosci. 2001, 2, 589-594.
2. Owen, A. D., Schapira, A. H., Jenner, P., Marsden, C. D., Oxidative stress and Parkinson's disease. Ann. NY Acad. Sci. 1996, 786, 217-223.
3. Langston, J. W., Ballard, P., Tetrud, J. W., Irwin, I., Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 1983, 219, 979-980.
4. Betarbet, R., Sherer, T. B., MacKenzie, G., Garcia-Osuna, M. et al., Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat. Neurosci. 2000, 3, 1301-1306.
5. McNaught, K. S., Perl, D. P., Brownell, A. L., Olanow, C. W., Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann. Neurol. 2004, 56, 149-162.
6. Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E. et al., Mutation in the alpha-synuclein gene identified in families with Parkinson's disease, Science 1997, 276, 2045-2047.
7. Leroy, E., Boyer, R., Auburger, G., Leube, B. et al., The ubiquitin pathway in Parkinson's disease. Nature 1998, 395, 451-452.
8. Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P. et al., Ubiquitination of a new form of alpha-synuclein by parkin from human brain: Implications for Parkinson's disease. Science 2001, 293, 263-269.
9. Alam, Z. I., Daniel, S. E., Lees, A. J., Marsden, D. C. et al., A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem. 1997, 69, 1326-1329.
10. Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M. et al., Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. USA 1996, 93, 2696-2701.
11. Lopiano, L., Fasano, M., Giraudo, S., Digilio, G. et al., Nuclear magnetic relaxation dispersion profiles of substantia nigra pars compacta in Parkinson's disease patients are consistent with protein aggregation. Neurochem. Int. 2000, 37, 331-336.
12. McNaught, K. S., Belizaire, R., Jenner, P., Olanow, C. W., Isacson, O., Selective loss of 20S proteasome alpha-sub-units in the substantia nigra pars compacts in Parkinson's disease. Neurosci. Lett. 2002, 326, 155-158.
13. McNaught, K. S., Belizaire, R., Isacson, O., Jenner, P., Olanow, C. W., Altered proteasomal function in sporadic Parkinson's disease. Exp. Neurol. 2003, 179, 38-46.
14. McNaught, K. S., Jenner, P., Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 2001, 297, 191-194.
15. Beal, M. F., Experimental models of Parkinson's disease. Nat. Rev. Neurosci. 2001, 2, 325-332.
16. Watanabe, Y., Himeda, T., Araki, T., Mechanisms of MPTP toxicity and their implications for therapy of Parkinson's disease. Med. Sci. Monit. 2005, 11, RA17-RA23.
17. Hauser, M. A., Li, Y. J., Takeuchi, S., Walters, R. et al., Genomic convergence: Identifying candidate genes for Parkinson's disease by combining serial analysis of gene expression and genetic linkage. Hum. Mol. Genet. 2003, 12, 671-677.
18. Brown, V. M., Ossadtchi, A., Khan, A. H., Yee, S. et al., Multiplex three-dimensional brain gene expression mapping in a mouse model of Parkinson's disease. Genome Res. 2002, 12, 868-884.
19. Simpson, R. J., Proteins and Proteomics: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York 2003, pp. 6-7.
20. Lopez, M. F., Melov, S., Applied proteomics: Mitochondrial proteins and effect on function. Circ. Res. 2002, 90, 380-389.
21. Benvenuti, S., Cramer, R., Bruce, J., Waterfield, M. D., Jat, P. S., Identification of novel candidates for replicative senescence by functional proteomics. Oncogene 2002, 21, 4403-4413.
22. Gygi, S. P., Corthals, G. L., Zhang, Y., Rochon, Y., Aebersold, R., Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc. Natl. Acad. Sci. USA 2000, 97, 9390-9395.
23. Tatton, N. A., Kish, S. J., In situ detection of apoptotic nuclei in the substantia nigra compacta of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-treated mice using terminal deoxynucleotidyl transferase labelling and acridine orange staining. Neuroscience 1997, 77, 1037-1048.
24. Crocker, S. J., Smith, P. D., Jackson-Lewis, V., Lamba, W. R. et al., Inhibition of calpains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease. J. Neurosci. 2003, 23, 4081-4091.
25. Sedelis, M., Schwarting, R. K., Huston, J. P., Behavioral phenotyping of the MPTP mouse model of Parkinson's disease. Behav. Brain Res. 2001, 125, 109-125.
26. Rozas, G., Lopez-Martin, E., Guerra, M. J., Labandeira-Garcia, J. L., The overall rod performance test in the MPTP-treated-mouse model of Parkinsonism. J. Neurosci. Methods 1998,83, 165-175.
27. Sommer, B., Barbieri, S., Hofele, K., Wiederhold, K. et al., Mouse models of alpha-synucleinopathy and Lewy pathology. Exp. Gerontol. 2000, 35, 1389-1403.
28. Langen, H., Roder, D., Juranville, J. F., Fountoulakis, M., Effect of protein application mode and acrylamide concentration on the resolution of protein spots separated by two-dimensional gel electrophoresis. Electrophoresis 1997, 18, 2085-2090.
29. Fernandez, J., Gharahdaghi, F., Mische, S. M., Routine identification of proteins from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gels or polyvinyl difluoride membranes using matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS). Electrophoresis 1998, 19, 1036-1045.
30. Gharahdaghi, F., Weinberg, C. R., Meagher, D. A., Imai, B. S., Mische, S. M., Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity. Electrophoresis 1999, 20, 601-605.
31. Landrigan, P. J., Sonawane, B., Butler, R. N., Trasande, L. et al., Early environmental origins of neurodegenerative disease in later life. Environ. Health Perspect. 2005, 113, 1230-1233.
32. Kopin, I. J., MPTP: An industrial chemical and contaminant of illicit narcotics stimulates a new era in research on Parkinson's disease. Environ. Health Perspect. 1987, 75, 45-51.
33. Basso, M., Giraudo, S., Corpillo, D., Bergamasco, B. et al., Proteome analysis of human substantia nigra in Parkinson's disease. Proteomics 2004, 4, 3943-3952.
34. Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D. et al., Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 2004, 279, 13256-13264.
35. De luliis, A., Grigoletto, J., Recchia, A., Giusti, P., Arslan, P., A proteomic approach in the study of an animal model of Parkinson's disease. Clin. Chim. Acta 2005, 357, 202-209.
36. Tanaka, K., Proteasomes: Structure and biology. J. Biochem. (Tokyo) 1998, 123, 195-204.
37. DeMartino, G. N., Slaughter, C. A., The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 1999, 274, 22123-22126.
38. Alves-Rodrigues, A., Gregori, L., Figueiredo-Pereira, M. E., Ubiquitin, cellular inclusions and their role in neurodegeneration. Trends Neurosci. 1998, 21, 516-520.
39. Tanaka, K., Suzuki, T., Hattori, N., Mizuno, Y., Ubiquitin, proteasome and Parkin. Biochim. Biophys. Acta 2004, 1695, 235-247.
40. Ross, C. A., Pickart, C. M., The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol. 2004, 14, 703-711.
41. Betarbet, R., Sherer, T. B., Greenamyre, J. T., Ubiquitin-proteasome system and Parkinson's diseases. Exp. Neurol. 2005, 191, S17-S27.
42. Crompton, M., The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 1999, 341, 233-249.
43. Nicklas, W. J., Vyas, I., Heikkila, R. E., Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci. 1985, 36, 2503-2508.
44. Richardson, A., Schwager, F., Landry, S. J., Georgopoulos, C., The importance of a mobile loop in regulating chaperonin/co-chaperonin interaction: Humans versus Escherichia coli. J. Biol. Chem. 2001, 276, 4981-4987.
45. Gupta, R. S., Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 1995, 15, 1-11.
46. Hohfeld, J., Hartl, F. U., Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J. Cell. Biol. 1994, 126, 305-315.
47. Samali, A., Cotter, T. G., Heat shock proteins increase resistance to apoptosis. Exp. Cell Res. 1996, 223, 163-170.
48. Klucken, J., Shin, Y., Hyman, B. T., McLean, P. J., A single amino acid substitution differentiates Hsp70-dependent effects on alpha-synuclein degradation and toxicity. Biochem. Biophys. Res. Commun. 2004, 325, 367-373.
49. Wu, Y. R., Wang, C. K., Chen, C. M., Hsu, Y. et al., Analysis of heat-shock protein 70 gene polymorphisms and the risk of Parkinson's disease. Hum. Genet. 2004, 114, 236-241.
50. Scott, H. S., Chen, H., Rossier, C., Lalioti, M. D., Antonarakis, S. E., Isolation of a human gene (HES1) with homology to an Escherichia coli and a zebrafish protein that maps to chromosome 21q22.3. Hum. Genet. 1997, 99, 616-623.
51. Nagamine, K., Kudoh, J., Minoshima, S., Kawasaki, K. et al., Isolation of cDNA for a novel human protein KNP-I that is homologous to the E. coli SCRP-27A protein from the autoimmune polyglandular disease type I (APECED) region of chromosome 21q22.3. Biochem. Biophys. Res. Commun. 1996, 225, 608-616.
52. Abou-Sleiman, P. M., Muqit, M. M., Wood, N. W., Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 2006, 7, 207-219.
53. Bolt, H. M., Thier, R., Relevance of the deletion polymorphisms of the glutathione S-transferases GSTT1 and GSTM1 in pharmacology and toxicology. Curr. Drug Metab.i 2006, 7, 613-628.
54. Stroombergen, M. C., Waring, R. H., Determination of glutathione S-transferase mu and theta polymorphisms in neurological disease. Hum. Exp. Toxicol. 1999, 18, 141-145.
55. Ahmad, Z., Salim, M., Maines, M. D., Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress. J. Biol. Chem. 2002, 277, 9226-9232.
56. Salim, M., Brown-Kipphut, B. A., Maines, M. D., Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation. J. Biol. Chem. 2001, 276, 10929-10934.
57. Galat, A., Peptidylproline cis-trans-isomerases: Immunophilins. Eur. J. Biochem. 1993, 216, 689-707.
58. Freskgard, P. O., Bergenhem, N., Jonsson, B. H., Svensson, M., Carlsson, U., Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 1992, 258, 466-468.