Gene expression profiling in ataxin-3 expressing cell lines reveals distinct effects of normal and mutant ataxin-3

Journal of Neuropathology and Experimental Neurology

Volumn 62, Issue 10, 2003, Pages 1006-1018

  Evert, Bernd O ^a   Vogt, Ina R ^a   Vieira Saecker, Ana M ^a   Ozimek, Lucia ^a   De Vos, Rob A I ^b   Brunt, Ewout R P ^c   Klockgether, Thomas ^a   Wüllner, Ullrich ^a  

^a UNIVERSITY OF BONN   (Germany)

^b Laboratorium Pathologie Oost Nederland   (Netherlands)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Ataxin 3; Differential gene expression; Extracellular matrix; Inflammation; Oligonucleotide microarray; SCA3; Transcriptional regulation

Indexed keywords

ATAXIN 3; GENE PRODUCT; POLYGLUTAMINE; UNCLASSIFIED DRUG;

ADULT; ARTICLE; AUTOPSY; BRAIN TISSUE; CASE REPORT; CONTROLLED STUDY; DNA MICROARRAY; EXTRACELLULAR MATRIX; FEMALE; GENE EXPRESSION PROFILING; GENE MUTATION; GENE OVEREXPRESSION; GENETIC CODE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MALE; NERVE CELL; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PONS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SPINOCEREBELLAR DEGENERATION; TRANSCRIPTION REGULATION; UPREGULATION;

EID: 0141891166     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnen/62.10.1006     Document Type: Article

References (65)

1. Kawaguchi Y, Okamoto T, Taniwaki M, et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat Genet 1994;8:221-28
2. Schmidt T, Landwehrmeyer GB, Schmitt I, et al. An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain Pathol 1998;8:669-79
3. Paulson HL. Toward an understanding of polyglutamine neurodegeneration. Brain Pathol 2000;10:293-99
4. Zoghbi HY, Orr HT. Glutamine repeats and neurodegeneration. Annu Rev Neurosci 2000;23:217-47
5. Margolis RL, Ross CA. Expansion explosion: New clues to the pathogenesis of repeat expansion neurodegenerative diseases. Trends Mol Med 2001;7:479-82
6. Luthi-Carter R, Strand AD, Hanson SA, et al. Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum Mol Genet 2002;11:1927-37
7. Kazantsev A, Preisinger E, Dranovsky A, Goldgaber D, Housman D. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc Natl Acad Sci USA 1999;96:11404-9
8. Steffan JS, Kazantsev A, Spasic-Boskovic O, et al. The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci USA 2000;97:6763-68
9. McCampbell A, Taylor JP, Taye AA, et al. CREB-binding protein sequestration by expanded polyglutamine. Hum Mol Genet 2000;9:2197-2202
10. Nucifora FC, Jr, Sasaki M, Peters MF, et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 2001;291:2423-28
11. Chai Y, Wu L, Griffin JD, Paulson HL. The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease. J Biol Chem 2001;276:44889-97
12. Chai Y, Shao J, Miller VM, Williams A, Paulson HL. Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc Natl Acad Sci USA 2002;99:9310-15
13. Shimohata T, Nakajima T, Yamada M, et al. Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription. Nat Genet 2000;26:29-36
14. Luthi-Carter R, Strand A, Peters NL, et al. Decreased expression of striatal signaling genes in a mouse model of Huntington's disease. Hum Mol Genet 2000;9:1259-71
15. Wyttenbach A, Swartz J, Kita H, et al. Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum Mol Genet 2001;10:1829-45
16. Sipione S, Rigamonti D, Valenza M, et al. Early transcriptional profiles in huntingtin-inducible striatal cells by microarray analyses. Hum Mol Genet 2002;11:1953-65
17. Lin X, Antalffy B, Kang D, Orr HT, Zoghbi HY. Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1. Nat Neurosci 2000;3:157-63
18. Yue S, Serra HG, Zoghbi HY, Orr HT. The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract. Hum Mol Genet 2001;10:25-30
19. Lieberman AP, Harmison G, Strand AD, Olson JM, Fischbeck KH. Altered transcriptional regulation in cells expressing the expanded polyglutamine androgen receptor. Hum Mol Genet 2002;11:1967-76
20. Evert BO, Vogt IR, Kindermann C, et al. Inflammatory genes are upregulated in expanded ataxin-3-expressing cell lines and spinocerebellar ataxia type 3 brains. J Neurosci 2001;21:5389-96
21. Perez MK, Paulson HL, Pendse SJ, Saionz SJ, Bonini NM, Pittman RN. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 1998;143:1457-70
22. Li F, Macfarlan T, Pittman RN, Chakravarti D. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J Biol Chem 2002;277:45004-12
23. Evert BO, Wullner U, Schulz JB, et al. High level expression of expanded full-length ataxin-3 in vitro causes cell death and formation of intranuclear inclusions in neuronal cells. Hum Mol Genet 1999;8:1169-76
24. Lipshutz RJ, Fodor SP, Gingeras TR, Lockhart DJ. High density synthetic oligonucleotide arrays. Nat Genet 1999;21:20-24
25. Wullner U, Kornhuber J, Weller M, et al. Cell death and apoptosis regulating proteins in Parkinson's disease - A cautionary note. Acta Neuropathol 1999;97:408-12
26. Lorenzet R, Napoleone E, Celi A, Pellegrini G, Di Santo A. Cell-cell interaction and tissue factor expression. Blood Coagul Fibrinolysis 1998;9:49-59
27. Matilla A, Koshy BT, Cummings CJ, Isobe T, Orr HT, Zoghbi HY. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature 1997;389:974-78
28. Zuccato C, Ciammola A, Rigamonti D, et al. Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science 2001;293:493-98
29. Roy-Chowdhury J, Huang TJ, Kesari K, Lederstein M, Arias IM, Roy-Chowdhury N. Molecular basis for the lack of bilirubin-specific and 3-methylcholanthrene-inducible UDP-glucuronosyltransferase activities in Gunn rats. The two isoforms are encoded by distinct mRNA species that share an identical single base deletion. J Biol Chem 1991;266:18294-98
30. Paulson HL, Perez MK, Trottier Y, et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 1997;19:333-44
31. Yamada M, Sato T, Shimohata T, et al. Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases. Am J Pathol 2001;159:1785-95
32. Campbell IL, Abraham CR, Masliah E, et al. Neurologic disease induced in transgenic mice by cerebral overexpression of interleukin 6. Proc Natl Acad Sci USA 1993;90:10061-65
33. Huell M, Strauss S, Volk B, Berger M, Bauer J. Interleukin-6 is present in early stages of plaque formation and is restricted to the brains of Alzheimer's disease patients. Acta Neuropathol 1995;89:544-51
34. Gadient RA, Patterson PH. Leukemia inhibitory factor, Interleukin 6, and other cytokines using the GP130 transducing receptor: Roles in inflammation and injury. Stem Cells 1999;17:127-37
35. Tenen DG, Hromas R, Licht JD, Zhang DE. Transcription factors, normal myeloid development, and leukemia. Blood 1997;90:489-519
36. Lekstrom-Himes J, Xanthopoulos KG. Biological role of the CCAAT/enhancer-binding protein family of transcription factors. J Biol Chem 1998;273:28545-48
37. Jordan M, Otterness IG, Ng R, Gessner A, Rollinghoff M, Beuscher HU. Neutralization of endogenous IL-6 suppresses induction of IL-1 receptor antagonist. J Immunol 1995;154:4081-90
38. Mesri M, Altieri DC. Leukocyte microparticles stimulate endothelial cell cytokine release and tissue factor induction in a JNK1 signaling pathway. J Biol Chem 1999;274:23111-18
39. Matsuoka K, Taoka M, Satozawa N, et al. A nuclear factor containing the leucine-rich repeats expressed in murine cerebellar neurons. Proc Natl Acad Sci USA 1994;91:9670-74
40. Murer MG, Yan Q, Raisman-Vozari R. Brain-derived neurotrophic factor in the control human brain, and in Alzheimer's disease and Parkinson's disease. Prog Neurobiol 2001;63:71-124
41. Takiyama Y, Oyanagi S, Kawashima S, et al. A clinical and pathologic study of a large Japanese family with Machado-Joseph disease tightly linked to the DNA markers on chromosome 14q. Neurology 1994;44:1302-8
42. Cemal CK, Carroll CJ, Lawrence L, et al. YAC transgenic mice carrying pathological alleles of the MJD1 locus exhibit a mild and slowly progressive cerebellar deficit. Hum Mol Genet 2002;11:1075-94
43. West AE, Chen WG, Dalva MB, et al. Calcium regulation of neuronal gene expression. Proc Natl Acad Sci USA 2001;98:11024-31
44. Shieh PB, Ghosh A. Molecular mechanisms underlying activity-dependent regulation of BDNF expression. J Neurobiol 1999;41:127-34
45. Shieh PB, Hu SC, Bobb K, Timmusk T, Ghosh A. Identification of a signaling pathway involved in calcium regulation of BDNF expression. Neuron 1998;20:727-40
46. Tao X, Finkbeiner S, Arnold DB, Shaywitz AJ, Greenberg ME. Ca2+ influx regulates BDNF transcription by a CREB family transcription factor-dependent mechanism. Neuron 1998;20:709-26
47. Rogalla T, Ehrnsperger M, Preville X, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 1999;274:18947-56
48. Song X, Mott JD, von Kampen J, et al. A model for the quaternary structure of the proteasome activator PA28. J Biol Chem 1996;271:26410-17
49. Minami Y, Kawasaki H, Minami M, Tanahashi N, Tanaka K, Yahara I. A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding. J Biol Chem 2000;275:9055-61
50. Cowan KJ, Diamond MI, Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum Mol Genet 2003;12:1377-91
51. Chai Y, Koppenhafer SL, Bonini NM, Paulson HL. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 1999;19:10338-47
52. Schmidt T, Lindenberg KS, Krebs A, et al. Protein surveillance machinery in brains with spinocerebellar ataxia type 3: Redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Ann Neurol 2002;51:302-10
53. Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 1998;19:148-54
54. Cummings CJ, Sun Y, Opal P, et al. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum Mol Genet 2001;10:1511-18
55. Stenoien DL, Cummings CJ, Adams HP, 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 1999;8:731-41
56. Jana NR, Tanaka M, Wang G, Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 2000;9:2009-18
57. Kobayashi Y, Kume A, Li M, et al. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J Biol Chem 2000;275:8772-78
58. Zhou H, Li SH, Li XJ. Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J Biol Chem 2001;276:48417-24
59. Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999;23:425-28
60. Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP, Rubinsztein DC. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 2002;11:1137-51
61. Wyttenbach A, Carmichael J, Swartz J, et al. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc Natl Acad Sci USA 2000;97:2898-2903
62. Woessner JF, Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 1991;5:2145-54
63. Nagase H, Woessner JF, Jr. Matrix metalloproteinases. J Biol Chem 1999;274:21491-94
64. Frisch SM, Morisaki JH. Positive and negative transcriptional elements of the human type IV collagenase gene. Mol Cell Biol 1990;10:6524-32
65. Somasundaram K, Jayaraman G, Williams T, Moran E, Frisch S, Thimmapaya B. Repression of a matrix metalloprotease gene by E1A correlates with its ability to bind to cell type-specific transcription factor AP-2. Proc Natl Acad Sci USA 1996;93:3088-93