The endoplasmic reticulum and neurological diseases

Experimental Neurology

Volumn 219, Issue 2, 2009, Pages 376-381

  Yang, Wei ^a   Paschen, Wulf ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; POLYGLUTAMIC ACID; PRESENILIN 1; PRESENILIN 2;

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; APOPTOSIS; ARTICLE; AUTOPHOSPHORYLATION; BRAIN BLOOD FLOW; BRAIN INJURY; BRAIN ISCHEMIA; CALCIUM HOMEOSTASIS; CELL DAMAGE; CELL LOSS; CEREBROVASCULAR ACCIDENT; DIFFUSE LEWY BODY DISEASE; DISEASE COURSE; ENDOPLASMIC RETICULUM STRESS; FAMILIAL DISEASE; GENE MUTATION; HUMAN; HUNTINGTON CHOREA; MOTOR NEURON DISEASE; NERVE CELL NECROSIS; NERVE DEGENERATION; NEUROLOGIC DISEASE; NONHUMAN; PARKINSON DISEASE; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; SPINOCEREBELLAR DEGENERATION; SUBSTANTIA NIGRA;

EID: 69749109092     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2009.07.009     Document Type: Note

References (112)

1. Atkin J.D., Farg M.A., Walker A.K., McLean C., Tomas D., and Horne M.K. Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol. Dis. 30 (2008) 400-407
2. Bando Y., Katayama T., Kasai K., Taniguchi M., Tamatani M., and Toyama M. GRP94 (94 kDa glucose-regulated protein) suppresses ischemic neuronal death against ischemia/reperfusion injury. Eur. J. Neurosci. 18 (2003) 829-840
3. Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
4. Betarbet R., Sherer T.B., MacKenzie G., Garcia-Osuna M., Panov A.V., and Greenamyre J.T. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat. Neurosci. 3 (2000) 1301-1306
5. Bush K.T., Goldberg A.L., and Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperons, and thermotolerance. J. Biol. Chem. 272 (1997) 9086-9092
6. Calfon M., Zeng H., Urano F., Till J.H., Hubbard S.R., Harding H.P., Clark S.G., and Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415 (2002) 92-96
7. Chan S.L., Culmsee C., Haughey N., Klapper W., and Mattson M.P. Presenilin-1 mutations sensitize neurons to DNA damage-induced death by a mechanism involving perturbed calcium homeostasis and activation of calpains and caspase-12. Neurobiol. Dis. 11 (2002) 2-19
8. Chen D., Jin K., Kawaguchi K., Nakayama M., Zhou X., Xiong Z., Zhou A., Mao X.O., Greenberg D.A., Graham S.H., and Simon R.P. Ero1-L, an ischemia-inducible gene from rat brain with homology to global ischemia-induced gene 11 (Gii11), is localized to neuronal dendrites by a dispersed identifier (ID) element-dependent mechanism. J. Neurochem. 85 (2003) 670-679
9. Ciosk R., DePalma M., and Priess J.R. ATX-2, the C. elegans ortholog of ataxin 2, functions in translational regulation in the germline. Development 131 (2004) 4831-4841
10. Cooper H.K., Zalewska T., Kawakami S., Hossmann K.A., and Kleihues P. The effect of ischemia and recirculation on protein synthesis in the rat brain. J. Neurochem. 28 (1977) 929-934
11. DeGracia D.J., and Montie H.L. Cerebral ischemia and the unfolded protein response. J. Neurochem. 91 (2004) 1-8
12. Forman M.S., Lee V.M.Y., and Trojanowski J.Q. Unfolding pathways in neurodegenerative disease. Trends Neurosci. 26 (2003) 407-410
13. Forno L.S. Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol. 55 (1996) 259-272
14. Guo Q., Sopher B.L., Furukawa K., Pham D.G., Robinson N., Martin G.M., and Mattson M.P. Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: involvement of calcium and oxyradicals. J. Neurosci. 17 (1997) 4212-4222
15. Hacki J., Egger L., Monney L., Conus S., Rosse T., Fellay I., and Borner C. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 19 (2000) 2286-2295
16. Hampton R.Y. ER stress response: getting the UPR hand on misfolded proteins. Curr. Biol. 10 (2000) R518-R521
17. Harding H.P., Zhang Y., and Ron D. Protein translation and folding are coupled by an endoplasmic reticulum-resident kinase. Nature 397 (1999) 271-274
18. Hartmann T., Bieger S.C., Bruhl B., Tienari P.J., Ida N., Allsop D., Roberts G.W., Masters C.L., Dotti C.G., Unsicker K., and Beureuther K. Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nat. Med. 3 (1997) 1016-1020
19. Hayashi T., Saito A., Okuno S., Ferrand-Drake M., Dodd R.L., Nishi T., Maier C.M., Kinouchi H., and Chan P.H. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal death. J. Cereb. Blood Flow Metab. 23 (2003) 1117-1128
20. Haze K., Yoshida H., Yanagi H., Yura T., and Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 10 (1999) 3787-3799
21. Hoozemans J.J., Veerhuis R., Van Haastert E.S., Rozemuller J.M., Baas F., Eikelenboom P., and Scheper W. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol. 110 (2005) 165-172
22. Hoozemans J.J.M., van Haastert E.S., Eikelenboom P., de Vos R.A.I., Rozemuller J.M., and Scheper W. Activation of the unfolded protein response in Parkinson's disease. Biochem. Biophys. Res. Commun. 354 (2007) 707-711
23. Ilieva A.V., Ayala V., Jove M., Dalfo E., Cacabelos D., Povedano M., Bellmunt M.J., Ferrer I., Pamplona R., and Potero-Otin M. Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis. Brain 130 (2007) 3111-3123
24. Imai Y., Soda M., and Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275 (2000) 35661-35664
25. Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin. Cell 105 (2001) 891-902
26. Imbert G., Sausou F., Yvert G., Devys D., Trottier Y., Garnier J.M., Weber C., Mandel J.L., Cancel G., Abbas N., Durr A., Didierjean O., Stevanin G., Agid Y., and Brice A. Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity of expanded CAG/glutamine repeats. Nat. Genet. 14 (1996) 285-291
27. Ito D., Walker J.R., Thompson C.S., Moroz I., Lin W., Veselits M.L., Hakim A.M., Fienberg A.A., and Thinakaran G. Characterization of stanniocalcin 2, a novel target of the mammalian unfolded protein response with cytoprotective properties. Mol. Cell. Biol. 24 (2004) 9456-9469
28. Kanekura K., Nishimoto I., Aiso S., and Matsuoka M. Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem. 281 (2006) 30223-30233
29. Kanekura K., Suzuki H., and Aiso S. ER stress and unfolded protein response in amyotrophic lateral sclerosis. Mol. Neurobiol. 39 (2009) 81-89
30. Katayama T., Imaizumi K., Sato N., Miyoshi K., Kudo T., Hitomi J., Morihara T., Yoneda T., Gomi F., Mori Y., Nakano Y., Takeda J., Tsuda T., Itoyama Y., Murayama O., Takaashima A., St George-Hyslop P., Takeda M., and Tohyma M. Presenilin-1 mutations downregulate the signaling pathway of the unfolded-protein response. Nat. Cell Biol. 1 (1999) 479-485
31. Katayama T., Imaizumi K., Honda A., Yoneda T., Kudo T., Takeda M., Mori K., Rozmahel R., Fraser P., George-Hyslop P.S., and Tohyama M. Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations. J. Biol. Chem. 276 (2001) 43446-43454
32. Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational control. Gene Dev. 13 (1999) 1211-1233
33. Kieran D., Woods I., Villunger A., Strasser A., and Prehn J.H.M. Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice. Proc. Natl. Acad. Sci. U. S. A. 18 (2007) 20606-20611
34. Kim S.W., Park S., You K.H., and Kwon O.Y. Expression of the endoplasmic reticulum chaperone GRP94 gene in ischemic gerbil brain. Z. Naturforsch. [C] 58 (2003) 736-739
35. Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., and Shimizu N. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 (1998) 605-608
36. Kitano H., Nishimura H., Tachibana H., Yoshikawa H., and Matsuyama T. ORP150 ameliorates ischemia/reperfusion injury from middle cerebral artery occlusion in mouse brain. Brain Res. 1015 (2004) 122-128
37. Kleihues P., Hossmann K.A., Pegg A.E., Kobayashi K., and Zimmermann V. Resuscitation of the monkey brain after one hour complete ischemia. III. Indications of metabolic recovery. Brain Res. 95 (1975) 61-73
38. Koh H.S., Moon I.S., Lee Y.H., Shong M., and Kwon O.Y. Expression of an HSP110 family, ischemia-responsive protein (irp94), in the rat brain after transient forebrain ischemia. Z. Naturforsch. [C] 55 (2000) 449-454
39. Kouroku Y., Fujita E., Jimbo A., Kikuchi T., Yamagata T., Momoi M.Y., Kominami E., Kuida K., Sakamaki K., Yonehara S., and Momoi T. Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation. Hum. Mol. Gen. 11 (2002) 1505-1515
40. Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., Przuntek H., Epplen J.T., Schols L., and Riess O. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat. Genet. 18 (1998) 106-108
41. Kumar R., Azam S., Sullivan J.M., Owen C., Cavener D.R., Zhang P., Ron D., Harding H.P., Chen J.J., Han A., White B.C., Krause G.S., and DeGracia D.J. Brain ischemia and reperfusion activates the eukaryotic initiation factor 2alpha kinase, PERK. J. Neurochem. 77 (2001) 1418-1421
42. Kumar R., Krause G.S., Yoshida H., Mori K., and DeGracia D.J. Dysfunction of the unfolded protein response during global brain ischemia and reperfusion. J. Cereb. Blood Flow Metab. 23 (2003) 462-471
43. Kuwabara K., Matsumoto M., Ikeda J., Hori O., Ogawa S., Maeda Y., Kitagawa K., Imuta N., Kinoshita T., Stern D.M., Yanagi H., and Kamada T. Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain. J. Biol. Chem. 271 (1996) 5025-5032
44. Langston J.W., Ballard P., Tetrud J.W., and Irwin I. Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219 (1983) 979-980
45. Laybutt D.R., Preston A.M., Akerfeldt M.C., Kench J.G., Busch A.K., Biankin A.V., and Biden T.J. Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes. Diabetologia 50 (2007) 752-763
46. Leissring M.A., Akbari Y., Fanger C.M., Cahalan M.D., Mattson M.P., and LaFerla F.M. Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice. J. Cell Biol. 149 (2000) 793-798
47. Li M., Baumeister P., Roy B., Phan T., Foti D., Luo S., and Lee AS. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20 (2000) 5096-5106
48. Lilley B.N., and Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429 (2004) 834-840
49. Lin J.H., Walter P., and Yen T.S.B. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. Mech. Dis. 3 (2008) 399-425
50. Lindholm D., Wootz H., and Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ. 13 (2006) 385-392
51. Malhotra J.D., and Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 18 (2007) 716-731
52. Marciniak S.J., and Ron D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86 (2006) 1133-1149
53. Margolis R.L., and Ross C.A. Expansion explosion: new clues to the pathogenesis of repeat expansion neurodegenerative diseases. Trends Mol. Med. 7 (2001) 479-482
54. Martindale D., Hackam A., Wieczorek A., Ellerby L., Wellington C., McCutcheon K., Singaraja R., Kazemi-Esfarjani P., Devon R., Kim S.U., Bredesen D.E., Tufaro F., and Hayden M.R. Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat. Genet. 18 (1998) 150-154
55. Matsushita K., Matsuyama T., Nishimura H., Takaoka T., Kuwabara K., Tsukamoto Y., Sugita M., and Ogawa S. Marked, sustained expression of a novel 150-kDa oxygen-regulated stress protein, in severely ischemic mouse neurons. Mol. Brain Res. 60 (1998) 98-106
56. Mengesdorf T., Jensen P.H., Mies G., Aufenberg C., and Paschen W. Down-regulation of parkin protein in transient focal cerebral ischemia: a link between stroke and degenerative disease?. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 15042-15047
57. Milhavet O., Martindale J.L., Camandola S., Chan S.L., Gary D.S., Cheng A., Holbrook N.J., and Mattson M.P. Involvement of Gadd153 in the pathogenic action of presenilin-1 mutations. J. Neurochem. 83 (2002) 673-681
58. Miyazaki M., Ozawa K., Hori O., Kitao Y., Matsushita T., Ogawa S., and Matsuyama T. Expression of 150-kd oxygen-regulated protein in the hippocampus suppresses delayed neuronal death. J. Cereb. Blood Flow Metab. 22 (2002) 979-987
59. Nagata T., Ilieva H., Murakami T., Shiote M., Narai H., Ohta Y., Hayashi T., Shoji M., and Abe K. Increased ER stress during motor neuron degeneration is a mouse model of amyotrophic lateral sclerosis. Neurol. Res. 29 (2007) 767-771
60. Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., and Yuan J. Caspase-12 mediates endoplasmic reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 98-103
61. 2+ leak function of presenilin. J. Clin. Invest. 117 (2007) 1230-1239
62. Nishimura A.L., Mitne-Neto M., Silva H.C.A., Richieri-Costa A., Middleton S., Cascio D., Kok F., Oliveira J.R., Gillingwater T., Webb J., Skehel P., and Zatz M. A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am. J. Hum. Genet. 75 (2004) 822-831
63. Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., and Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16 (2002) 1345-1355
64. Nishitoh H., Kadowaki H., Nagai A., Maruyama T., Yokota T., Fukutomi H., Noguchi T., Matsuzawa A., Takeda K., and Ichijo H. ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev. 22 (2008) 1451-1464
65. Okada T., Yoshida H., Akazawa R., Negishi M., and Mori K. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366 (2002) 585-594
66. Oyadomari S., and Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11 (2004) 381-389
67. Paschen W. Disturbances in calcium homeostasis within the endoplasmic reticulum may contribute to the development of ischemic cell damage. Med. Hypotheses 47 (1996) 283-288
68. Paschen W. Endoplasmic reticulum: a primary target in various acute disorders and degenerative diseases of the brain. Cell Calcium 34 (2003) 365-383
69. Paschen W. Shutdown of translation: lethal or protective? Unfolded protein response versus apoptosis. J. Cereb. Blood Flow Metab. 23 (2003) 773-779
70. Paschen W., and Doutheil J. Disturbances of the functioning of endoplasmic reticulum: a key mechanism underlying neuronal cell injury?. J. Cereb. Blood Flow Metab. 19 (1999) 1-18
71. Paschen W., and Frandsen A. Endoplasmic reticulum dysfunction - a common denominator for cell injury in acute and degenerative diseases of the brain?. J. Neurochem. 79 (2001) 719-725
72. Paschen W., and Mengesdorf T. Cellular abnormalities linked to endoplasmic reticulum dysfunction in cerebrovascular disease - therapeutic potential. Pharmacol. Ther. 108 (2005) 362-375
73. Paschen W., and Mengesdorf T. Endoplasmic reticulum stress response in neurodegeneration. Cell Calcium 38 (2005) 409-415
74. Paschen W., Uto A., Djuricic B., and Schmitt J. Hemeoxygenase expression after reversible ischemia of rat brain. Neurosci. Lett. 180 (1994) 5-8
75. Paschen W., Gissel C., Linden T., and Doutheil J. Erp72 expression activated by transient cerebral ischemia or disturbances of neuronal endoplasmic reticulum calcium stores. Metab. Brain Dis. 13 (1998) 55-68
76. Paschen W., Gissel C., Linden T., Althausen S., and Doutheil J. Activation of gadd153 expression through transient cerebral ischemia: evidence that ischemia causes endoplasmic reticulum dysfunction. Mol. Brain Res. 60 (1998) 115-122
77. Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., Pike B., Root H., Rubenstein J., Boyer R., Stenroos E.S., Chandrasekharappa S., Athanessiadou A., Papapetropoulos T., Johnson W.G., Lazzarini A.M., Duvoisin R.C., Di Iorio G., Golbe L.I., and Nussbaum R.L. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 2045-2047
78. Pulst S.M., Nechiporuk A., Nechiporuk T., Gispert S., Chen X.N., Lopes-Cendes I., Pearlman S., Starkman S., Orozco-Diaz G., Lunkes A., DeJong P., Rouleau G.A., Auburger G., Korenberg J.R., Figueroa C., and Sahba S. Moderate expansion of a normal biallelic trinucleotide repeat in spinocerebellar ataxia type 2. Nat. Genet. 14 (1996) 269-276
79. Qi X., Okuma Y., Hosoi T., Kaneko M., and Nomura Y. Induction of murine HRD1 in experimental cerebral ischemia. Mol. Brain Res. 130 (2004) 30-38
80. Ralser M., Albrecht M., Nonhoff U., Lengauer T., Lehrach H., and Krobitsch S. An integrative approach to gain insight into the cellular function of human ataxin-2. J. Mol. Biol. 346 (2005) 203-214
81. Rao R.V., and Bredesen D.E. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr. Opin. Cell Biol. 16 (2004) 653-662
82. Reimertz C., Kogel D., Rami A., Chittenden T., and Prehn J.H.M. Gene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway. J. Cell Biol. 162 (2003) 587-597
83. Ross C.A., McInnis M.C., Margolis R.L., and Li S.-H. Genes with triplet repeats: candidate mediators of neuropsychiatric disorders. Trends Neurosci. 16 (1993) 254-260
84. Ryu E.J., Harding H.P., Angelastro J.M., Vitolo O.V., and Ron D. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J. Neurosci. 22 (2002) 10690-10698
85. Sanpei K., Takano H., Igarashi S., Sato T., Oyake M., Sasaki H., Wakisaka A., Tashiro K., Ishida Y., Ikeuchi T., Koide R., Saito M., Sato A., Tanaka T., Hanyu S., Takiyama Y., Nishizawa M., Shimizu N., Nomura Y., Segawa M., Iwabuchi K., Eguchi I., Tanaka H., Takahashi H., and Tsuji S. Identification of the spinocerebellar ataxia type 2 gene using a direct identification of repeat expansion and cloning technique, DIRECT. Nat. Genet. 14 (1996) 277-284
86. Satterfield T.A., and Pallanck L.J. Ataxin-2 and its Drosophila homolog ATX2, physically assemble with polyribosomes. Hum. Mol. Genet. 15 (2006) 2523-2532
87. Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., Shimizu N., Iwai K., Chiba T., Tanaka K., and Suzuki T. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nature 25 (2000) 302-305
88. Smith W.W., Jiang H., Pei Z., Tanaka Y., Morita H., Sawa A., Dawson V.L., Dawson T.M., and Ross C.A. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum. Mol. Gen. 14 (2005) 3801-3811
89. Suzuki H., Kanekura K., Levine T.P., Kohno K., Olkkonen V.M., Aiso S., and Matsuoka M. ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J. Neurochem. 108 (2009) 973-985
90. Tajiri S., Oyadomari S., Yano S., Morioka M., Gotoh T., Hamada J.I., Ushio Y., and Mori M. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ. 11 (2004) 403-415
91. Tamatani M., Matsuyama T., Yamaguchi A., Mitsuda N., Tsukamoto Y., Taniguchi M., Che Y.H., Ozawa K., Hori O., Nishimura H., Yamashita A., Okabe M., Yanagi H., Stern D.M., Ogawa S., and Tohyama M. ORP150 protects against hypoxia/ischemia-induced neuronal death. Nat. Med. 7 (2001) 317-323
92. Tang T.-S., Tu H., Chan E.Y.W., Maximov A., Wang Z., Wellington C.L., Hayden M.R., and Bezprozvanny I. Huntingtin and huntingtin-associated protein 1 influences neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39 (2003) 227-239
93. Teuling E., Ahmed S., Haasdijk E., Demmers J., Steinmetz M.O., Akhmanova A., Jaarsma D., and Hoogenraad C.C. Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates. J. Neurosci. 27 (2007) 9801-9815
94. Tobisawa S., Hozumi Y., Arawaka S., Koyama S., Wada M., Nagai M., Aoki M., Itoyama Y., Goto K., and Kato T. Mutant SOD1 linked to familial amyotrophic lateral sclerosis, but not wild-type SOD1, induces ER stress in COS7 cells and transgenic mice. Biochem. Biophys. Res. Commun. 303 (2003) 496-503
95. Treiman M. Regulation of the endoplasmic reticulum calcium storage during the unfolded protein response - significance in tissue ischemia?. Trends Cardiovasc. Med. 12 (2002) 57-62
96. 2+ leak channels, a function disrupted by familial Alzheimer's disease-linked mutations. Cell 126 (2006) 981-993
97. Uehara T., Nakamura T., Yao D., Shi Z.Q., Gu Z., Ma Y., Masliah E., Nomura Y., and Lipton S.A. S-nitrosylated protein-disulfide isomerase links protein misfolding to neurodegeneration. Nature 441 (2006) 513-517
98. Ungerstedt U., Ljungberg T., and Steg G. Behavioral, physiological, and neurochemical changes after 6-hydroxydopamine-induced degenegartion of the nigro-striatal dopamine neurons. Adv. Neurol. 5 (1974) 421-426
99. Unterberger U., Hoftberger R., Gelpi E., Flicker H., Budka H., and Voigtlander T. Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion disease in vivo. J. Neuropathol. Exp. Neurol. 65 (2006) 348-357
100. van de Loo S., Eich F., Nonis D., Auburger G., and Nowock J. Ataxin-2 associates with rough endoplasmic reticulum. Exp. Neurol. 215 (2009) 110-118
101. Walkinshaw G., and Waters C.M. Neurotoxin-induced cell death in neuronal PC12 cells is mediated by induction of apoptosis. Neuroscience 63 (2000) 975-987
102. Walter J., Capell A., Grunberg A., Pesold B., Schindzielorz A., Prior R., Podlisny M.B., Fraser P., Hyslop P.S., Selkoe D.J., and Haass C. The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2 (1996) 673-691
103. Yamaguchi A., Hori O., Stern D.M., Hartmann E., Ogawa S., and Tohyama M. Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. J. Cell Biol. 147 (1999) 1195-1204
104. Yamamuro A., Yoshioka Y., Ogita K., and Maeda S. Involvement of endoplasmic reticulum stress on the cell death induced by 6-hydroxydopamine in human neuroblastoma SH-SY5Y cells. Neurochem. Res. 31 (2006) 657-664
105. Yasuda Y., Kudo T., katayama T., Imaizumi K., Yatera M., Okochi M., Yamamori H., Matsumoto N., Kida T., Fukumori A., Okumura M., Toyama M., and Takeda M. FAD-linked presenilin-1 mutants impede translation regulation under ER stress. Biochem. Biophys Res. Commun. 296 (2002) 313-318
106. Ye Y., Shibata Y., Yun C., Ron D., and Rapoport T.A. A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 429 (2004) 841-847
107. Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., and Mori K. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20 (2000) 6755-6767
108. Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., and Mori K. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (C BF) and activating transcription factor 6alpha and 6beta that activates the mammalian unfolded protein response. Mol. Cell. Biol. 21 (2001) 1239-1248
109. Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
110. Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R., Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atares B., Llorens V., Gomez Tortosa E., del Ser T., Munoz D.G., and de Yebenes J.G. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol. 55 (2004) 164-173
111. 2+ release from intracellular stores. Neurobiol. Dis. 15 (2004) 269-278
112. Zimmermann J., Erdmann D., Lalande I., Grossenbacher R., Noorani M., and Furst P. Proteasome inhibitor induced gene expression profiles reveal overexpression of transcriptional regulators ATF3, GADD153 and MAD1. Oncogene 19 (2000) 2913-2920