The role of ER stress-induced apoptosis in neurodegeneration

Current Alzheimer Research

Volumn 9, Issue 3, 2012, Pages 373-387

  Stefani, Ioanna C ^a   Wright, Daniel ^a   Polizzi, Karen M ^a   Kontoravdi, Cleo ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Apoptosis; Calcium dyshomeostasis; Endoplasmic reticulum stress; Neurodegeneration; Oxidative stress; Reactive oxygen species

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; APOPTOSIS SIGNAL REGULATING KINASE 1; CALCIUM ION; CASPASE 12; CASPASE 3; CASPASE 9; CYTOCHROME C; DOPAMINE; GLUCOSE REGULATED PROTEIN 94; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; LEUCINE RICH REPEAT KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P53; REACTIVE OXYGEN METABOLITE; RYANODINE RECEPTOR; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UBIQUITIN; UNINDEXED DRUG; X BOX BINDING PROTEIN 1;

ALZHEIMER DISEASE; APOPTOSIS; ARTICLE; DISEASE ASSOCIATION; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; GENE MUTATION; HUMAN; HUNTINGTON CHOREA; MITOCHONDRION; NERVE CELL; NERVE DEGENERATION; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALS; APOPTOSIS; CALCIUM SIGNALING; ENDOPLASMIC RETICULUM STRESS; HUMANS; MITOCHONDRIAL DISEASES; NEURODEGENERATIVE DISEASES; NEURONS; OXIDATIVE STRESS;

EID: 84859435142     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/156720512800107618     Document Type: Article

References (132)

1. th December 2010).
2. Desai AK, Grossberg GT. Diagnosis and treatment of Alzheimer's disease. Neurology 64: S34-9 (2005).
3. Mattson MP. Pathways towards and away from Alzheimer's disease. Nature 430: 631-9 (2004).
4. Zhu X, Raina AK, Perry G, Smith MA. Alzheimer's disease: the two-hit hypothesis. Lancet Neurol 3: 219-26 (2004).
5. Hoozemans JJM, Veerhuis R, Van Haastert ES, Rozemuller JM, Baas F, Eikelenboom P, et al. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathologica 110: 165-172 (2005).
6. Wang XL, Su B, Perry G, Smith MA, Zhu XW. Insights into amyloid-beta-induced mitochondrial dysfunction in Alzheimer disease. Free Radical Biology and Medicine 43:1569-1573 (2007).
7. Reddy PH. Amyloid precursor protein-mediated free radicals and oxidative damage: Implications for the development and progression of Alzheimer's disease. J Neurochem 96: 1-13. (2006).
8. Wagner SL, Munoz B. Modulation of amyloid beta protein precursor processing as a means of retarding progression of Alzheimer's disease. J Clin Investig 104: 1329-1332. (1999).
9. Wirths O, Multhaup G, Czech C, Blanchard V, Moussaoui S, Tremp G, et al. Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci Lett 306: 116-20 (2001).
10. Bayer TA, Wirths O, Majtenyi K, Hartmann T, Multhaup G, Beyreuther K, et al. Key factors in Alzheimer's disease: betaamyloid precursor protein processing, metabolism and intraneuronal transport. Brain Pathology 11: 1-11. (2001).
11. Rogaeva E, Meng Y, Lee JH, Gu Y, Kawarai T, Zou F, et al. The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease. Nature Genetics 39: 168-177 (2007).
12. Cook DG, Forman MS, Sung JC, Leight S, Kolson DL, Iwatsubo T, et al. Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Medicine 3:1021-1023 (1997).
13. Skovronsky DM, Doms RW, Lee VMY. Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J Cell Biol 141:1031-1039 (1998).
14. WildBode C, Yamazaki T, Capell A, Leimer U, Steiner H, Ihara Y, et al. Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42. J Biol Chem 272: 16085-16088 (1997).
15. Hartmann T, Bieger SC, Bruhl B, Tienari PJ, Ida N, Allsop D, et al. Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nature Medicine 3: 1016-20 (1997).
16. Kloskowska E. Amyloid precursor protein with the Alzheimer's disease 670/671 mutation. PhD Thesis, Karolinska Institutet pp:1-48 (2008).
17. Almeida CG, Takahashi RH, Gouras GK. Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 26: 4277-88 (2006).
18. Farrer MJ. Genetics of Parkinson disease: paradigm shifts and future prospects. Nature Reviews Genetics 7: 306-318 (2006).
19. Betarbet R, Sherer TB, MacKenzie G, Garcia-Osuna M, Panov AV, Greenamyre JT. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nature Neuroscience 3: 1301-1306 (2000).
20. Irizarry MC, Growdon W, Gomez-Isla T, Newell K, George JM, Clayton DF, et al. Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J Neuropathol Exp Neurol 57: 334-7 (1998).
21. Wakabayashi K, Hayashi S, Kakita A, Yamada M, Toyoshima Y, Yoshimoto M, et al. Accumulation of alpha-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy. Acta Neuropathologica 96: 445-452 (1998).
22. Maguire-Zeiss KA, Federoff HJ. Convergent pathobiologic model of Parkinson's disease. Ann NY Acad Sci 991:152-66 (2003).
23. Kumar P, Kalonia H, Kumar A. Huntington's disease: pathogenesis to animal models. Pharmacol Rep 62:1-14 (2010).
24. Kehoe P, Krawczak M, Harper PS, Owen MJ, Jones AL. Age of onset in Huntington disease: sex specific influence of apolipoprotein E genotype and normal CAG repeat length. Journal of Medical Genetics 36: 108-111 (1999).
25. Trottier Y, Devys D, Imbert G, Saudou F, An I, Lutz Y, et al. Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form. Nature Genetics 10:104-10 (1995).
26. Kremer B, Goldberg P, Andrew SE, Theilmann J, Telenius H, Zeisler J, et al. A worldwide study of the Huntington's disease mutation. The sensitivity and specificity of measuring CAG repeats. N Engl J Med 330: 1401-6 (1994).
27. Andrew SE, Goldberg YP, Kremer B, Telenius H, Theilmann J, Adam S, et al. The Relationship between Trinucleotide (Cag) Repeat Length and Clinical-Features of Huntington Disease. American Journal of Human Genetics 53: 1118-1118 (1993).
28. Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. The Presence of Malfolded Proteins in the Endoplasmic-Reticulum Signals the Induction of Glucose-Regulated Proteins. Nature 332: 462-464 (1988).
29. Lee AS. Mammalian stress response: induction of the glucoseregulated protein family. Curr Opin Cell Biol 4: 267-73 (1992).
30. Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529 (2007).
31. Kadowaki H, Nishitoh, HIchijo H. Survival and apoptosis signals in ER stress: the role of protein kinases. Journal of Chemical Neuroanatomy 28: 93-100 (2004).
32. Breckenridge DG, Germain M, Mathai JP, Nguyen M, Shore GC. Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene 22: 8608-8618 (2003).
33. Zhang KZ, Kaufman RJ. The unfolded protein response-A stress signaling pathway critical for health and disease. Neurology 66: S102-S109 (2006).
34. Kim I, Xu WJ, Reed JC. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nature Reviews Drug Discovery 7: 1013-1030 (2008).
35. Trusina A, Papa FR, Tang C. Rationalizing translation attenuation in the network architecture of the unfolded protein response. Proc Natl Acad Sci USA 105: 20280-5(2008).
36. Mengesdorf T, Jensen PH, Mies G, Aufenberg C, Paschen W. Down-regulation of parkin protein in transient focal cerebral ischemia: A link between stroke and degenerative disease? Proc Natl Acad Sci USA 99: 15042-15047(2002).
37. Van Anken E, Braakman I. Endoplasmic reticulum stress and the making of a professional secretory cell. Crit Rev Biochem Mol Biol 40: 269-283(2005).
38. Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403: 98-103 (2000).
39. Urano F, Wang XZ, Bertolotti A, Zhang YH, Chung P, Harding HP, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666 (2000).
40. Srivastava SP, Kumar KU, Kaufman RJ. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J Biol Chem 273: 2416-2423(1998).
41. Barone MV, Crozat A, Tabaee A, Philipson L, Ron D. Chop (Gadd153) and Its Oncogenic Variant, Tls-Chop, Have Opposing Effects on the Induction of G(1)/S Arrest. Genes & Development 8: 453-464 (1994).
42. Althausen S, Mengesdorf T, Mies G, Olah L, Nairn AC, Proud CG, et al. Changes in the phosphorylation of initiation factor eIF-2 alpha, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice. J Neurochem 78:779-787 (2001).
43. DeGracia DJ, Kumar R, Owen CR, Krause GS, White BC. Molecular pathways of protein synthesis inhibition during brain reperfusion: Implications for neuronal survival or death. J Cereb Blood Flow Metab 22: 127-14 (2002).
44. Hu BR, Martone ME, Jones YZ, Liu CL. Protein aggregation after transient cerebral ischemia. J Neurosci 20: 3191-3199 (2000).
45. Nowak TS, Fried RL, Lust WD, Passonneau JV. Changes in Brain Energy-Metabolism and Protein-Synthesis Following Transient Bilateral Ischemia in the Gerbil. Journal of Neurochemistry 44: 487-494 (1985).
46. Paschen W, Frandsen A. Endoplasmic reticulum dysfunction-a common denominator for cell injury in acute and degenerative diseases of the brain? J Neurochem 79: 719-725 (2001).
47. Chafekar SM, Zwart R, Veerhuis R, Vanderstichele H, Baas F, Scheper W. Increased A beta(1-42) Production Sensitizes Neuroblastoma Cells for ER Stress Toxicity. Curr Alzheimer Res 5: 469-474. (2008).
48. Colombo A, Bastone A, Ploia C, Sclip A, Salmona M, Forloni G, et al. JNK regulates APP cleavage and degradation in a model of Alzheimer's disease. Neurobiol Dis 33: 518-525 (2009).
49. Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CMF. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiology of Disease 23: 669-678. (2006).
50. Oh S, Hong HS, Hwang E, Sim HJ, Lee W, Shin SJ, et al. Amyloid peptide attenuates the proteasome activity in neuronal cells. Mech Ageing Dev 126: 1292-1299 (2005).
51. Copanaki E, Schurmann T, Eckert A, Leuner K, Muller WE, Prehn JH, et al. The amyloid precursor protein potentiates CHOP induction and cell death in response to ER Ca2+ depletion. Biochim Biophys Acta 1773: 157-65 (2007).
52. Sakono M, Zako T. Amyloid oligomers: formation and toxicity of Abeta oligomers. Febs Journal 277: 1348-58 (2010).
53. Valincius G, Heinrich F, Budvytyte R, Vanderah DJ, McGillivray DJ, Sokolov Y, et al. Soluble amyloid betaoligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity. Biophysical J 95: 4845-61 (2008).
54. Lin H, Bhatia R, Lal R. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB Jl 15:2433-2444 (2001).
55. Glabe CG, Kayed R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 66:S74-S78 (2006).
56. Lai AY, McLaurin J. Mechanisms of amyloid-Beta Peptide uptake by neurons: the role of lipid rafts and lipid raft-associated proteins. Int J Alzheimers Dis 2011: 548380 (2010).
57. Chafekar SM, Baas F, Scheper W. Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake. Biochim Biophys Acta 1782: 523-31 (2008).
58. Rushworth JV, Hooper NM. Lipid Rafts: Linking Alzheimer's Amyloid-beta Production, Aggregation, and Toxicity at Neuronal Membranes. Int J Alzheimers Dis 2011:603052 (2010).
59. Chafekar SM, Hoozemans JJ, Zwart R, Baas F, Scheper W. Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antioxid Redox Signal 9: 2245-54 (2007).
60. Lee JN, Ye J. Proteolytic activation of sterol regulatory elementbinding protein induced by cellular stress through depletion of Insig-1. J Biol Chem 279: 45257-45265 (2004).
61. Paschen W, Mengesdorf T. Cellular abnormalities linked to endoplasmic reticulum dysfunction in cerebrovascular disease-therapeutic potential. Pharmacol Ther 108: 362-375 (2005).
62. Katayama T, Imaizumi K, Manabe T, Hitomi J, Kudo T, Tohyama M. Induction of neuronal death by ER stress in Alzheimer's disease. J Chem Neuroanat 28: 67-78 (2004).
63. Yoshida H, Oku M, Suzuki M, Mori K. pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J Cell Biol 172: 565-575. (2006).
64. Kudo T, Kanemoto S, Hara H, Morimoto N, Morihara T, Kimura R, et al. A molecular chaperone inducer protects neurons from ER stress. Cell Death and Differentiation 15: 364-375 (2008).
65. Lindholm D, Wootz H, Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ 13: 385-392 (2006).
66. Chung KKK, Dawson VL, Dawson TM. The role of the ubiquitinproteasomal pathway in Parkinson's disease and other neurodegenerative disorders. Trends in Neurosciences 24: S7-S14 (2001).
67. Rao RV, Bredesen DE. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol 16: 653-662 (2004).
68. Smith WW, Jiang HB, Pei Z, Tanaka Y, Morita H, Sawa A, et al. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Human Molecular Genetics 14: 3801-3811 (2005).
69. Wang HQ, Takahashi R. Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease. Antioxid Redox Signal 9: 553-61 (2007).
70. Chan CS, Gertler TS, Surmeier DJ. Calcium homeostasis, selective vulnerability and Parkinson's disease. Trends Neurosci 32: 249-56 (2009).
71. Levy OA, Malagelada C, Greene LA. Cell death pathways in Parkinson's disease: proximal triggers, distal effectors, and final steps. Apoptosis 14: 478-500 (2009).
72. Hoozemans JJ, van Haastert ES, Eikelenboom P, de Vos RA, Rozemuller JM, Scheper W. Activation of the unfolded protein response in Parkinson's disease. Biochem Biophys Res Commun 354:707-11. (2007).
73. Tan YY, Zhou HY, Wang ZQ, Chen SD. Endoplasmic reticulum stress contributes to the cell death induced by UCH-L1 inhibitor. Mol Cell Biochem 318: 109-15 (2008).
74. Hayashi T, Saito A, Okuno S, Ferrand-Drake M, Dodd RL, Nishi T, et al. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal cell death. J Cereb Blood Flow Metab 23:1117-28. (2003).
75. Scorrano L, Oakes SA, Opferman JT, Cheng EH, Sorcinelli MD, Pozzan T, et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science 300:135-139(2003).
76. Haynes CM, Titus EA, Cooper AA. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Molecular Cell 15: 767-776 (2004).
77. Kouroku Y, Fujita E, Jimbo A, Kikuchi T, Yamagata T, Momoi MY, et al. Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation. Human Molecular Genetics 11: 1505-15 (2002).
78. Duennwald ML, Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes & Development 22: 3308-3319 (2008).
79. Carnemolla A, Fossale E, Agostoni E, Michelazzi S, Calligaris R, De Maso L, et al. Rrs1 Is Involved in Endoplasmic Reticulum Stress Response in Huntington Disease. J Biol Chem 284:18167-18173 (2009).
80. Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, et al. ASK1 is essential for endoplasmic reticulum stressinduced neuronal cell death triggered by expanded polyglutamine repeats. Genes & Development 16: 1345-1355 (2002).
81. Reijonen S, Kukkonen JP, Hyrskyluoto A, Kivinen J, Kairisalo M, Takei N, et al. Downregulation of NF-kappaB signaling by mutant huntingtin proteins induces oxidative stress and cell death. Cell Mol Life Sci 67: 1929-41(2010).
82. Kouroku Y, Fujita E, Tanida I, Ueno T, Isoai A, Kumagai H, et al. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death and Differentiation 14: 230-9(2007).
83. Nakayama H, Hamada M, Fujikake N, Nagai Y, Zhao J, Hatano O, et al. ER stress is the initial response to polyglutamine toxicity in PC12 cells. Biochem Biophys Res Commun 377: 550-555 (2008).
84. Atwal RS, Xia J, Pinchev D, Taylor J, Epand RM, Truant, R. Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Human Molecular Genetics 16: 2600-2615 (2007).
85. Rockabrand E, Slepko N, Pantalone A, Nukala VN, Kazantsev A, Marsh JL, et al. The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Human Molecular Genetics 16: 61-77 (2007).
86. Omi K, Hachiya NS, Tokunaga K, Kaneko K. siRNA-mediated inhibition of endogenous Huntington disease gene expression induces an aberrant configuration of the ER network in vitro. Biochem Biophys Res Commun 338: 1229-1235(2005).
87. Atwal RS, Truant R. A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 4: 91-93 (2008).
88. Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 26: 9220-31 (2006).
89. Jana NR, Zemskov EA, Wang GH, Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Human Molecular Genetics 10:1049-1059 (2001).
90. Waelter S, Boeddrich A, Lurz R, Scherzinger E, Lueder G, Lehrach H, et al. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Molecular Biology of the Cell 12: 1393-1407 (2001).
91. Yang H, Liu C, Zhong YW, Luo SQ, Monteiro MJ, Fang SY. Huntingtin Interacts with the Cue Domain of gp78 and Inhibits gp78 Binding to Ubiquitin and p97/VCP. Plos One 5: (2010).
92. Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitinproteasome system by protein aggregation. Science 292:1552-5 (2001).
93. Naidoo N. ER and aging-Protein folding and the ER stress response. Ageing Res Rev 8: 150-9 (2009).
94. Bueler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Experimental Neurology 218: 235-246 (2009).
95. Bueler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp Neurol 218: 235-46 (2009).
96. Banerjee R, Starkov AA, Beal MF, Thomas B. Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis. Biochim Biophys Acta 1792: 651-63 (2009).
97. Fiskum G, Starkov A, Polster BM, Chinopoulos C. Mitochondrial mechanisms of neural cell death and neuroprotective interventions in Parkinson's disease. Ann NY Acad Sci 991: 111-9 (2003).
98. Van Laar VS, Berman SB. Mitochondrial dynamics in Parkinson's disease. Exp Neurol 218: 247-56 (2009).
99. Greenamyre JT, Hastings TG. Parkinson's-Divergent causes, convergent mechanisms. Science 304: 1120-1122 (2004).
100. Meredith GE, Sonsalla PK, Chesselet MF. Animal models of Parkinson's disease progression. Acta Neuropathologica 115: 385-98 (2008).
101. LaFerla FM, Green KN, Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8: 499-509 (2007).
102. Panov AV, Gutekunst CA, Leavitt BR, Hayden MR, Burke JR, Strittmatter WJ, et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 5: 731-6 (2002).
103. Yu ZX, Li SH, Evans J, Pillarisetti A, Li HL, Li XJ. Mutant huntingtin causes context-dependent neurodegeneration in mice with Huntington's disease. J Neurosci 23:2193-202. (2003).
104. th Edition. New York: Garland Science, Taylor & Francis Group (2002).
105. Chakroborty S, Goussakov I, Miller MB, Stutzmann GE. Deviant ryanodine receptor-mediated calcium release resets synaptic homeostasis in presymptomatic 3xTg-AD mice. J Neurosci 29: 9458-70 (2009).
106. Cheng EHY, Sheiko TV, Fisher JK, Craigen WJ, Korsmeyer SJ. VDAC2 inhibits BAK activation and mitochondrial apoptosis. Science 301: 513-517 (2003).
107. Wei MC, Zong WX, Cheng EHY, Lindsten T, Panoutsakopoulou V, Ross AJ, et al. Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 292: 727-730 (2001).
108. Li, P, Nijhawan, D, Budihardjo, I, Srinivasula, SM, Ahmad, M, Alnemri, ES, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489 (1997).
109. Wang JF, Young LT. Regulation of molecular chaperone GRP78 by mood stabilizing drugs. Clinical Neuroscience Research 4: 281-288 (2004).
110. Shao L, Sun XJ, Xu L, Young LT, Wang JF. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sciences 78:1317-1323 (2006).
111. Bown CD, Wang, JF, Chen B, Young, LT. Regulation of ER stress proteins by valproate: therapeutic implications. Bipolar Disord 4: 145-51 (2002).
112. Kim AJ, Shi YY, Austin RC, Werstuck GH. Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3. J Cell Sci 118: 89-99. (2005).
113. Suzuki S, Okuse Y, Kawase M, Takiguchi M, Fukuyama Y, Takahashi H, et al. A norbergenin derivative inhibits neuronal cell damage induced by tunicamycin. Biol Pharm Bull 29: 1335-1338 (2006).
114. Qi X, Hosoi T, Okuma Y, Kaneko MN, Omura Y. Sodium 4-phenylbutyrate protects against cerebral ischemic injury. Molecular Pharmacology 66: 899-908 (2004).
115. Ozcan U, Yilmaz E, Ozcan L, Furuhashi M, Vaillancourt E, Smith RO, et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313: 1137-1140. (2006).
116. Woltjer RL, McMahan W, Milatovic D, Kjerulf JD, Shie FS, Rung LG, et al. Effects of chemical chaperones on oxidative stress and detergent-insoluble species formation following conditional expression of amyloid precursor protein carboxy-terminal fragment. Neurobiol Disease 25: 427-437 (2007).
117. Wiley JC, Meabon, JS, Frankowski H, Smith EA, Schecterson LC, Bothwell M, et al. Phenylbutyric Acid Rescues Endoplasmic Reticulum Stress-Induced Suppression of APP Proteolysis and Prevents Apoptosis in Neuronal Cells. Plos One 5: (2010).
118. Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, et al. A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307: 935-9 (2005).
119. Hosoi T, Ozawa K. Endoplasmic reticulum stress in disease: mechanisms and therapeutic opportunities. Clinical Science 118: 19-29 (2010).
120. Reijonen S, Putkonen N, Norremolle A, Lindholm D, Korhonen L. Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp Cell Res 314: 950-960 (2008).
121. Lee DY, Lee KS, Lee HJ, Kim DH, Noh YH, Yu K, et al. Activation of PERK Signaling Attenuates A beta-Mediated ER Stress. Plos One 5: (2010).
122. Tabata Y, Takano K, Ito T, Iinuma M, Yoshimoto T, Miura H, et al. Vaticanol B, a resveratrol tetramer, regulates endoplasmic reticulum stress and inflammation. Am J Physiol 293: C411-C418 (2007).
123. Takano K, Tabata Y, Kitao Y, Murakami R, Suzuki H, Yamada M, et al. Methoxyflavones protect cells against endoplasmic reticulum stress and neurotoxin. Am J Physiol-Cell Physiology 292: C353-C361 (2007).
124. Takano K, Kitao Y, Tabata Y, Miura H, Sato K, Takuma K, et al. A dibenzoylmethane derivative protects dopaminergic neurons against both oxidative stress and endoplasmic reticulum stress. Am J Physiol Cell Physiol 293: C1884-C1894 (2007).
125. Park YJ, Jang YMK, Won YH. Isoflavones Prevent Endoplasmic Reticulum Stress-Mediated Neuronal Degeneration by Inhibiting Tau Hyperphosphorylation in SH-SY5Y Cells. J Med Food12: 528-535 (2009).
126. Choi AY, Choi JH, Lee JY, Yoon KS, Choe W, Ha J, et al. Apigenin protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis. Neurochemistry International 57: 143-152. (2010).
127. Hosoi T, Sasaki M, Baba SOzawa K. Effect of pranoprofen on endoplasmic reticulum stress in the primary cultured glial cells. Neurochemistry International 54: 1-6 (2009).
128. Sanz E, Quintana A, Hidalgo J, Marco JL, Unzeta M. PF9601N [N-(2-propynyl)-2-(5-benzyloxy-indolyl) methylamine] confers MAO-B independent neuroprotection in ER stress-induced cell death. Mol Cell Neurosci 41:19-31 (2009).
129. Bouchecareilh M, Caruso ME, Roby P, Parent S, Rouleau N, Taouji S, et al. AlphaScreen (R)-Based Characterization of the Bifunctional Kinase/RNase IRE1 alpha: A Novel and Atypical Drug Target. J Biomol Screen 15: 406-417 (2010).
130. Wang H, Blais J, Ron D, Cardozo, T. Structural Determinants of PERK Inhibitor Potency and Selectivity. Chem Biol Drug Des 76: 480-495 (2010).
131. Ashall L, Horton CA, Nelson DE, Paszek P, Harper CV, Sillitoe K, et al. Pulsatile stimulation determines timing and specificity of NFkappaB-dependent transcription. Science 324: 242-6 (2009).
132. Toettcher JE, Loewer A, Ostheimer GJ, Yaffe MB, Tidor B, Lahav G. Distinct mechanisms act in concert to mediate cell cycle arrest. Proc Natl Acad Sci USA 106: 785-90 (2009).