Gene and protein signatures in sporadic Parkinson's disease and a novel genetic model of PD

Parkinsonism and Related Disorders

Volumn 13, Issue SUPPL. 3, 2007, Pages

  Mandel, Silvia A ^a   Fishman, Tali ^a   Youdim, Moussa B H ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Biomarkers; Gene expression profiling; Microarray; Neurodegenerative diseases; Neuroprotection; Parkinson's disease

Indexed keywords

BIOLOGICAL MARKER;

ARTICLE; CELL ADHESION; CELL CYCLE; CYTOSKELETON; DISEASE COURSE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DNA FINGERPRINTING; DOPAMINE METABOLISM; GENE EXPRESSION; GENE OVEREXPRESSION; GENE SILENCING; GENETIC ANALYSIS; GENETIC MODEL; HUMAN; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; SYNAPTIC TRANSMISSION;

ANIMALS; DISEASE MODELS, ANIMAL; GENE EXPRESSION REGULATION; GENETIC PREDISPOSITION TO DISEASE; HUMANS; PARKINSON DISEASE; PROTEINS;

EID: 38949125133     PISSN: 13538020     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1353-8020(08)70009-9     Document Type: Article

References (32)

1. Dauer W., and Przedborski S. Parkinson's disease: mechanisms and models. Neuron 39 (2003) 889-909
2. Jellinger K. Recent developments in the pathology of Parkinson's disease. J Neural Transm Suppl 62 (2002) 347-376
3. Bove J., Prou D., Perier C., and Przedborski S. Toxin-induced models of Parkinson's disease. NeuroRx 2 (2005) 484-494
4. Grünblatt E., Mandel S., Jacob-Hirsch J., Zeligson S., Amariglo N., Rechavi G., et al. Gene expression profiling of parkinsonian substantia nigra pars compacta; alterations in ubiquitin-proteasome, heat shock protein, iron and oxidative stress regulated proteins, cell adhesion/cellular matrix and vesicle trafficking genes. J Neural Transm 111 (2004) 1543-1573
5. Tanner C., and Langston J. Do environmental toxins cause Parkinson's disease?. A critical review. Neurology 40 Suppl 3 (1990) 17-30
6. Mandel S., Grünblatt E., Riederer P., Gerlach M., Levites Y., and Youdim M. Neuroprotective strategies in Parkinson's disease: an update on progress. CNS Drugs 17 (2003) 729-762
7. Mandel S., Amit T., Kalfon L., and Youdim M. Applying transcriptomic and proteomic knowledge to Parkinson's disease drug discovery 2 (2007) 1225-1240
8. Van der Schyf C., Geldenhuys W., and Youdim M. Multifunctional drugs with different CNS targets for neuropsychiatric disorders. J Neurochem 99 (2006) 1033-1048
9. Hauser M., Li Y., Xu H., Noureddine M., Shao Y., Gullans S., et al. Expression profiling of substantia nigra in Parkinson disease, progressive supranuclear palsy, and frontotemporal dementia with parkinsonism. Arch Neurol 62 (2005) 917-921
10. Miller R., Kiser G., Kaysser-Kranich T., Lockner R., Palaniappan C., and Federoff H. Robust dysregulation of gene expression in substantia nigra and striatum in Parkinson's disease. Neurobiol Dis 21 (2006) 305-313
11. Moran L., Duke D., Deprez M., Dexter D., Pearce R., and Graeber M. Whole genome expression profiling of the medial and lateral substantia nigra in Parkinson's disease. Neurogenetics 7 (2006) 1-11
12. Zhang Y., James M., Middleton F., and Davis R. Transcriptional analysis of multiple brain regions in Parkinson's disease supports the involvement of specific protein processing, energy metabolism, and signaling pathways, and suggests novel disease mechanisms. Am J Med Genet B Neuropsychiatr Genet 137 (2005) 5-16
13. Murata S., Chiba T., and Tanaka K. CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int J Biochem Cell Biol 35 (2003) 572-578
14. Sherman M., and Goldberg A. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29 (2001) 15-32
15. Stenoien D., Cummings C., Adams H., Mancini M., Patel K., DeMartino G., et al. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 8 (1999) 731-741
16. Epstein A., Gleadle J., McNeill L., Hewitson K., O'Rourke J., Mole D., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107 (2001) 43-54
17. Duke D., Moran L., Kalaitzakis M., Deprez M., Dexter D., Pearce R., et al. Transcriptome analysis reveals link between proteasomal and mitochondrial pathways in Parkinson's disease. Neurogenetics 7 (2006) 139-148
18. McNaught K., and Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci Lett 297 (2001) 191-194
19. Palop J., Chin J., and Mucke L. A network dysfunction perspective on neurodegenerative diseases. Nature 443 (2006) 768-773
20. Farrer M. Genetics of Parkinson disease: paradigm shifts and future prospects. Nat Rev Genet 7 (2006) 306-318
21. Perez F., and Palmiter R. Parkin-deficient mice are not a robust model of parkinsonism. Proc Natl Acad Sci USA 102 (2005) 2174-2179
22. Son J., Chun H., Joh T., Cho S., Conti B., and Lee J. Neuroprotection and neuronal differentiation studies using substantia nigra dopaminergic cells derived from transgenic mouse embryos. J Neurosci 19 (1999) 10-20
23. Zhou H., Falkenburger B., Schulz J., Tieu K., Xu Z., and Xia X. Silencing of the Pink1 gene expression by conditional RNAi does not induce dopaminergic neuron death in mice. Int J Biol Sci 3 (2007) 242-250
24. Bates T., Heales S., Davies S., Boakye P., and Clark J. Effects of 1-methyl-4-phenylpyridinium on isolated rat brain mitochondria: evidence for a primary involvement of energy depletion. J Neurochem 63 (1994) 640-648
25. +) involves binding at the same site as the respiratory inhibitor, rotenone. Biochem Biophys Res Commun 169 (1990) 123-128
26. Feldman R., Correll C., Kaplan K., and Deshaies R. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91 (1997) 221-230
27. Spruck C., and Strohmaier H. Seek and destroy: SCF ubiquitin ligases in mammalian cell cycle control. Cell Cycle 1 (2002) 250-254
28. Zheng N., Schulman B., Song L., Miller J., Jeffrey P., Wang P., et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416 (2002) 703-709
29. Copani A., Uberti D., Sortino M., Bruno V., Nicoletti F., and Memo M. Activation of cell-cycle-associated proteins in neuronal death: a mandatory or dispensable path?. Trends Neurosci 24 (2001) 25-31
30. Hermand D. F-box proteins: more than baits for the SCF?. Cell Div 1 (2006) 30
31. Galan J., Wiederkehr A., Seol J., Haguenauer-Tsapis R., Deshaies R., Riezman H., et al. Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast. Mol Cell Biol 21 (2001) 3105-3117
32. Nelson R., Glenn K., Zhang Y., Wen H., Knutson T., Gouvion C., et al. Selective cochlear degeneration in mice lacking the F-box protein, Fbx2, a glycoprotein-specific ubiquitin ligase subunit. J Neurosci 27 (2007) 5163-5171