Proteomic insights into the protective mechanisms of an in vitro oxidative stress model of early stage Parkinson's disease

Neuroscience Letters

Volumn 488, Issue 1, 2011, Pages 11-16

  Bauereis, Brian ^a   Haskins, William E ^a,b   LeBaron, Richard G ^a   Renthal, Robert ^a,b  

^a UNIVERSITY OF TEXAS AT SAN ANTONIO   (United States)

^b University of Texas Health Science Center   (United States)

Author keywords

Oxidative stress; Parkinson's disease; Proteomics; Rotenone; Unfolded protein response

Indexed keywords

BINDING IMMUNOGLOBULIN PROTEIN; BINDING PROTEIN; CASPASE 3; CELL ENZYME; FOLDASE; HEAT SHOCK PROTEIN; PROTEASOME; PROTEOME; REACTIVE OXYGEN METABOLITE; ROTENONE; UNCLASSIFIED DRUG;

ARTICLE; CELL VIABILITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOSOL; DOPAMINERGIC SYSTEM; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HOMEOSTASIS; HUMAN; HUMAN CELL; IN VITRO STUDY; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEOMICS; UPREGULATION;

ANALYSIS OF VARIANCE; APOPTOSIS; CASPASE 3; CELL LINE, TUMOR; CELL SURVIVAL; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPLASMIC RETICULUM; ENZYME-LINKED IMMUNOSORBENT ASSAY; HEAT-SHOCK PROTEINS; HUMANS; INSECTICIDES; NEUROBLASTOMA; OXIDATIVE STRESS; PROTEOME; PROTEOMICS; ROTENONE; SIGNAL TRANSDUCTION; UP-REGULATION;

EID: 78650510736     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2010.10.071     Document Type: Article

References (37)

1. Berg D. Redox imbalance. Oxidative Stress and Neurodegenerative Diseases 2005, 183-191. Elsevier. G. Qureshi, S. Parvez (Eds.).
2. Cannon J., Tapias V., Na H., Honick A., Drolet R., Greenamyre J.T. A highly reproducible rotenone model of Parkinson's disease. Neurobiol. Dis. 2009, 34:279-290.
3. Chen S., Smith D. Hop as an adaptor in the heat shock protein 70 (HSP70) and HSP90 chaperone machinery. J. Biol. Chem. 1998, 273:35194-35200.
4. Cheng S., Brown I. Neuronal expression of constitutive heat shock proteins: implications for neurodegenerative disorders. Cell Stress Chaperones 2007, 12:51-58.
5. Csermely P., Schainder T., Söti C., Prohászka Z., Nardai G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 1998, 79:129-168.
6. Douglas K.T. Mechanisms of action of glutathione-dependent enzymes. Adv. Enzymol. 1987, 59:103-167.
7. Frickel E.M., Frei P., Bouvier M., Stafford W., Helenius A., Clockshuber R., Ellgaard L. ERp57 is a multifunctional thiol-disulfide oxioreductase. J. Biol. Chem. 2004, 279:18277-18287.
8. Geisler S., Holmstrom K.M., Skujat D., Fiesel F.C., Rothfuss O.C., Kahle P.J., Springer W. PINK1/PARKIN-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 2009, 12:119-131.
9. Graves J., Metukuri M., Scott D., Rothermund K., Prochownik E. Regulation of reactive oxygen species homeostasis by peroxiredoxin and c-Myc. J. Biol. Chem. 2009, 284:6520-6529.
10. Greenamyer J.T., Betarbet R., Sherer T.B. The rotenone model of Parkinson's disease: genes, environment and mitochondria. Parkinsonism Relat. Disord. 2003, 9:59-64.
11. 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.
12. Holtz W.A., Turetzky J.M., Jong Y.I., O'Malley K.L. Oxidative stress-triggered unfolded protein response is upstream of intrinsic cell death evoked by Parkinsonian mimetics. J. Neurochem. 2006, 99:54-69.
13. Hoozemans J.J.M., van Haastert E.S., Eikelenboom P., de Vas R.A.I., Rozemuller J.M., Sheper W. Activation of the unfolded protein response in Parkinson's disease. B.B.R.C. 2007, 354:707-711.
14. Imai J., Maruya M., Yashiroda H., Yahara I., Tanaka K. The molecular chaperone HSP90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 2003, 22:3557-3567.
15. Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Emperical statistical model to estimate the accuracy of peptide identification made by MS/MS and database search. Anal. Chem. 2002, 74:5383-5392.
16. Kersey P.J., Duarte J., Williams A., Karavidopoulou Y., Birney E., Apweiler R. The international protein index: an integrated database for proteomics experiments. Proteomics 2004, 4:1985-1988.
17. Koll H., Guiard B., Rassow J., Ostermann J., Horwich A., Neupert W., Hartl F.U. Antifolding activity of HSP60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 1992, 68:1163-1175.
18. Lin C.Y., Kaufman R.J. The unfolded protein response. J. Cell Sci. 2003, 116:1861-1862.
19. Maes T., Barcelo A., Buesa C. Neuron navigator: a human gene family with homology to unc-53, a cell guidance gene from Caenorhabditis elegans. Genomics 2002, 80:21-30.
20. Manning-Krieg U.C, Scherer P.E., Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 1991, 10:3273-3280.
21. Mashima T., Naito M., Kataoka S., Kawai H., Tsuruo T. Aspartate-based inhibitor of interleukin-1 beta-converting enzyme prevents antitumor agent-induced apoptosis in human myeloid leukemia U937 cell. B.B.R.C. 1995, 209:907-915.
22. McClung J.K., Jupe E.R., Liu X.T., Dell'Orco R.T. Prohibitin: potential role in senescence, development, and tumor suppression. Exp. Gerontol. 1995, 30:99-124.
23. McNaught K.S.P, Olanow C.W. Proteolytic stress: a unifying concept for the etiopathogenesis of Parkinson's disease. Ann. Neurol. 2003, 53:73-86.
24. Mehlen P., Hickey E., Weber L.A., Arrigo A.P. Large unphosphorylated aggregates as the active form of HSP27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells. Biochem. Biophys. Res. Commun. 1997, 241:187-192.
25. Morano K. New tricks for an old dog. The evolving world of HSP70. Ann. NY Acad. Sci. 2007, 1113:1-14.
26. Nesvizhskii A.I., Keller A., Kolker E., Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 2003, 75:4646-4685.
27. Ozon S., El Mestikawy S., Sobel A. Differential, regional, and cellular expression of the Stathmin family transcripts in the adult rat brain. J. Neurosci. Res. 1999, 56:553-564.
28. Parcellier A., Schmitt E., Gurbuxani S., Seigneurin-Berny D., Pance A., Chantome A., Plenchette S., Khochbin S., Solary E., Garrido C. HSP27 is a ubiquitin-binding protein involved in I-κBα proteasomal degradation. Mol. Cell. Biol. 2003, 23:5790-5802.
29. Ross J., Nagy Z., Kirken R. The PHB1/2 phosphocomplex is required for mitochondrial homeostasis and survival of human T cells. J. Biol. Chem. 2008, 283:4699-4713.
30. Ryu E.J., Harding H.P., Angelastro J.M., Vitolo O.V., Ron D., Greene L.A. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J. Neurosci. 2002, 22:10690-10698.
31. Schröder M., Kaufman R. The mammalian unfolded protein response. Annu. Rev. Biochem. 2005, 74:739-789.
32. Sherer T., Betarbet R., Stout A., Lund S., Baptista M., Panov A., Cookson M., Greenmyre T. An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered α-synuclein metabolism and oxidative damage. J. Neurosci. 2002, 22:7006-7015.
33. Taira T., Saito Y., Niki T., Iguchi-Ariga S.M.M., Takahashi K., Ariga H. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep. 2004, 5:213-218.
34. M.M.M. Wilhelmus, R. Verhaar, G. Andringa, J.G.J.M. Bol, P. Cras, L. Shan, J.J.M. Hoozemans, B. Drukarch, Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain, Brain Path. (). doi:10.1111/j.1750-3639.2010.00429.x.
35. Wilkinson B., Gilbert H. Protein disulfide isomerase. Biochim. Biophys. Acta 2004, 1699:35-44.
36. Wang N., Xu M., Wang P., Li L. Development of mass spectrometry-based shotgun method for proteome analysis of 500-5000 cancer cells. Anal. Chem. 2010, 82:2262-2271.
37. Yaffe M., Farr G.W., Miklos D., Horwich A.L., Sternlicht M.L., Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 1992, 358:245-248.