Endoplasmic reticulum: A primary target in various acute disorders and degenerative diseases of the brain

Cell Calcium

Volumn 34, Issue 4-5, 2003, Pages 365-383

  Paschen, Wulf ^a  

^a MAX PLANCK INSTITUTE FOR NEUROLOGICAL RESEARCH   (Germany)

Author keywords

Degenerative disease; Endoplasmic reticulum; Ischemia; Stroke; Unfolded protein response; Xbp1 processing

Indexed keywords

CALCIUM; CELL MEMBRANE PROTEIN; ENDONUCLEASE; INITIATION FACTOR 2; MESSENGER RNA; NEUROTOXIN; OXYGEN RADICAL; PHOSPHOTRANSFERASE; PROTEASOME; SECRETORY PROTEIN; TRANSCRIPTION FACTOR; UBIQUITIN;

ACUTE DISEASE; ANIMAL CELL; BIOACCUMULATION; BRAIN DISEASE; BRAIN INJURY; BRAIN ISCHEMIA; BRAIN NERVE CELL; CALCIUM CELL LEVEL; CALCIUM DEPLETION; CALCIUM SIGNALING; CELL COMPARTMENTALIZATION; CELL FUNCTION; CELL PROTECTION; CYTOPLASM; DEGENERATIVE DISEASE; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; EPILEPTIC STATE; GENETIC CODE; HUMAN; HUMAN CELL; MITOCHONDRION; NEUROPATHOLOGY; NEUROTOXICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN SYNTHESIS; REVIEW; RNA TRANSLATION; STRESS; TRANSLATION INITIATION;

EUKARYOTA;

EID: 0043037253     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0143-4160(03)00139-8     Document Type: Article

References (160)

1. W.K. Hass, Beyond cerebral blood flow, metabolism and ischemic thresholds: an examination of the role of calcium in the initiation of cerebral infarction, in: J.S. Meyer, H. Lechner, M. Reivich, E.O. Ott, A. Aranibar (Eds.), Cerebral Vascular Disease, vol. 3, Excerpta Medica, Amsterdam, 1981, pp. 3-17.
2. B.K. Siesjö, Cell damage in the brain: a speculative synthesis, J. Cereb. Blood Flow. Metabol. 1 (1981) 155-185.
3. F.A.X. Schanne, A.B. Kane, E.E. Young, J.L. Farber, Calcium dependence of toxic cell death: a final common pathway, Science 206 (1979) 700-702.
4. T. Kristian, B.K. Siesjö, Calcium-related damage in ischemia, Life Sci. 59 (1996) 357-367.
5. B.K. Siesjö, P. Siesjö, Mechanisms of secondary brain damage, Eur. J. Anaesth. 13 (1996) 247-268.
6. A.N. Murphy, D.E. Bredesen, G. Cortopassi, E. Wang, G. Fiskum, Bcl-2 potentiates the maximal calcium uptake capacity of neural cell mitochondria, Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 9893-9898.
7. 2+ determine nerve growth factor dependence of synaptic ganglion cells, Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 6421-6425.
8. 2+, Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 3892-3896.
9. J.Y. Koh, C.W. Cotman, Programmed cell death: its possible contribution to neurotoxicity mediated by calcium channel antagonists, Brain Res. 587 (1992) 233-240.
10. M.L. Leski, S.L. Valentine, J.T. Coyle, L-type voltage-gated calcium channels modulate kainic acid neurotoxicity in cerebellar granule cells, Brain Res. 828 (1999) 27-40.
11. C.P. Turner, D. Pulciani, S.A. Rivkees, Reduction in intracellular calcium levels induces injury in developing neurons, Exp. Neurol. 178 (2002) 21-32.
12. R. Sattler, M.P. Charlton, M. Hafner, M. Tymianski, Distinct influx pathways, not calcium load, determine neuronal vulnerability to calcium neurotoxicity, J. Neurochem. 71 (1998) 2349-2364.
13. W. Paschen, Disturbances in calcium homeostasis within the endoplasmic reticulum may contribute to the development of ischemic cell damage, Med. Hypoth. 47 (1996) 283-288.
14. W. Paschen, J. Doutheil, Disturbances of the functioning of endoplasmic reticulum: a key mechanism underlying neuronal cell injury? J. Cereb. Blood Flow. Metabol. 19 (1999) 1-18.
15. W. Paschen, Role of calcium in neuronal cell injury: which subcellular compartment is involved? Brain Res. Bull. 53 (2000) 409-413.
16. W. Paschen, Dependence of vital cell function on endoplasmic reticulum calcium levels: implications for the mechanisms underlying neuronal cell injury in different pathological states, Cell Calcium 29 (2001) 1-11.
17. W. Paschen, A. Frandsen, Endoplasmic reticulum dysfunction: a common denominator for cell injury in acute and degenerative diseases of the brain? J. Neurochem. 79 (2001) 719-725.
18. M.P. Mattson, S.L. Chan, Neuronal and glial calcium signaling in Alzheimer's disease, Cell Calcium 34 (2003) 385-397.
19. A.M. Hofer, T.E. Machen, Techniques for in situ measurement of calcium in intracellular inositol 1,4,5-triphosphate-sensitive stores using the fluorescent indicator mag-Fura-2, Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 2598-2602.
20. 19F NMR, J. Biol. Chem. 271 (1996) 7398-7403.
21. L.D. Pozzomiller, N.B. Pivovarova, R.D. Leapman, R.A. Buchanan, T.S. Reese, S.B. Andrews, Activity-dependent calcium sequestration in dentrites of hippocampal neurons in brain slices, J. Neurosci. 17 (1997) 8729-8738.
22. 2+ pool and induces apoptosis in human hepatoma cells, Cell Biol. Intern. 17 (1993) 969-970.
23. Y. Furuya, P. Lundmo, A.D. Short, D.L. Gill, J.T. Isaacs, The role of calcium, pH, and cell proliferation in the programmed (apoptotic) death of androgen-independent prostatic cancer cells induced by thapsigargin, Cancer Res. 54 (1994) 6167-6175.
24. Y. Kaneko, A. Tsukamoto, Thapsigargin-induced persistent intracellular calcium pool depletion and apoptosis in human hepatoma cells, Cancer Lett. 97 (1994) 147-155.
25. 2+-induced apoptosis on cultured embryonic rat cortical neurons, Brain Res. 652 (1994) 65-70.
26. P. Waring, J. Beaver, Cyclosporin A rescues thymocytes from apoptosis induced by very low concentrations of thapsigargin: effects on mitochondrial function, Exp. Cell Res. 227 (1996) 264-276.
27. 2+ stores in induction and suppression of apoptosis in S49 cells, Am. J. Physiol. Cell Physiol. 41 (1997) C1241-C1249.
28. T.S. McCormick, K.S. McColl, C.W. Distelhorst, Mouse lymphoma cells destined to undergo apoptosis in response to thapsigargin treatment fail to generate a calcium-mediated grp78/grp94 stress response, J. Biol. Chem. 272 (1997) 6087-6092.
29. R. Nath, K.J. Raser, I. Hajimohammadreza, K.K. Wang, Thapsigargin induces apoptosis in SH-SY5Y neuroblastoma cells and cerebrocortical cultures, Biochem. Mol. Biol. Int. 43 (1997) 197-205.
30. G.A. Preston, J.C. Barrett, J.A. Biermann, E. Murphy, Effects of alterations in calcium homeostasis on apoptosis during neoplastic progression, Cancer Res. 57 (1997) 537-542.
31. X.-M. Qi, H. He, H. Zhong, C.W. Distelhorst, Baculovirus p35 and Z-VAD-fmk inhibit thapsigargin-induced apoptosis of breast cancer cells, Oncogene 15 (1997) 1207-1212.
32. T. Takadera, T. Ohyashiki, Apoptotic cell death and CPP32-like activation induced by thapsigargin and their prevention by nerve growth factor in PC12 cells, Biochim. Biophys. Acta Mol. Cell Res. 1401 (1998) 63-71.
33. H. Wei, W. Wei, D.E. Bredesen, D.C. Perry, Bcl-2 protects against apoptosis in neuronal cell line caused by thapsigargin-induced depletion of intracellular calcium stores, J. Neurochem. 70 (1998) 2305-2314.
34. 2+ stores and arachidonic acid metabolism, J. Clin. Invest. 101 (1998) 1623-1632.
35. C. Wang, H.N. Nguyen, J.L. Maguire, D.C. Perry, Role of intracellular calcium stores in cell death from oxygen-glucose deprivation in a neuronal cell line, J. Cereb. Blood Flow. Metabol. 22 (2002) 206-214.
36. O. Garaschuk, Y. Yaari, A. Konnerth, Release and sequestration of calcium by ryanodine-sensitive stores in hippocampal neurons, J. Physiol. 502 (1997) 13-20.
37. M.J. Berridge, Neuronal calcium signaling, Neuron 21 (1998) 13-26.
38. H.F. Lodish, N. Kong, Perturbation of cellular calcium blocks exit of secretory proteins from rough endoplasmic reticulum, J. Biol. Chem. 265 (1990) 10893-10899.
39. T.K. Gosh, J. Bian, A.D. Short, S.L. Rybak, D.L. Gill, Persistent intracellular calcium pool depletion by thapsigargin and its influence on cell growth, J. Biol. Chem. 266 (1991) 24690-24697.
40. G. Kuznetsov, M.A. Brostrom, C.O. Brostrom, Demonstration of a calcium requirement for secretory protein processing and export. Differential effects of calcium and dithiothreitol, J. Biol. Chem. 265 (1992) 3932-3939.
41. H.F. Lodish, N. Kong, L. Wikström, Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum, J. Biol. Chem. 267 (1992) 12753-12760.
42. R.J. Kaufman, Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls, Genes Dev. 13 (1999) 1211-1233.
43. H.P. Harding, Y. Zhang, D. Ron, Protein translation and folding are coupled by an endoplasmic reticulum-resident kinase, Nature 397 (1999) 271-274.
44. A.G. Hinnebusch, Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes, in: N. Sonenberg, J.W.B. Hershes, M.B. Mathews (Eds.), Translational Control of Gene Expression, Cold Spring Habor Laboratory Press, Cold Spring Habor, 2000, pp. 185-243.
45. D. Ron, H. Harding, PERK and translational control by stress in the endoplasmic reticulum, in: N. Sonenberg, J.W.B. Hershes, M.B. Mathews (Eds.), Translational Control of Gene Expression, Cold Spring Habor Laboratory Press, Cold Spring Habor, 2000, pp. 547-560.
46. R.J. Schneider, Translational control during heat shock, in: N. Sonenberg, J.W.B. Hershes, M.B. Mathews (Eds.), Translational Control of Gene Expression, Cold Spring Habor Laboratory Press, Cold Spring Habor, 2000, pp. 581-594.
47. H.K. Cooper, T. Zalewska, S. Kawakami, K.-A. Hossmann, The effect of ischemia and recirculation on protein synthesis in the brain, J. Neurochem. 28 (1977) 929-934.
48. P. Kleihues, K.-A. Hossmann, A.E. Pegg, K. Kobayashi, V. Zimmermann, Resuscitation of the monkey brain after one hour complete ischemia. III. Indications of metabolic recovery, Brain Res. 95 (1975) 61-73.
49. J. Burda, M.E. Martin, A. Garcia, A. Alcazar, J.L. Fando, M. Salinas, Phosphorylation of the α-subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischemia in the rat, Biochem. J. 302 (1994) 335-338.
50. D.J. DeGracia, R.W. Neumar, B.C. White, G.S. Krause, Global brain ischemia and reperfusion: modifications in eukaryotic initiation factors associated with inhibition of translational initiation, J. Neurochem. 67 (1996) 2005-2012.
51. S. Althausen, T. Mengesdorf, G. Mies, L. Oláh, A.C. Nairn, C.G. Proud, W. Paschen, Changes in the phosphorylation of initiation factor eIF2α elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischemia in mice, J. Neurochem. 78 (2001) 779-787.
52. T. Mengesdorf, C.G. Proud, G. Mies, W. Paschen, Mechanisms underlying suppression of protein synthesis induced by transient cerebral ischemia in mouse brain, Exp. Neurol. 177 (2002) 538-546.
53. J. Doutheil, S. Althausen, C. Gissel, W. Paschen, Activation of MYD116 (gadd34) expression following transient forebrain ischemia of rat: implications for a role of disturbances of endoplasmic reticulum calcium homeostasis, Mol. Brain Res. 63 (1999) 225-232.
54. 2+ and ionophore A23187 on protein synthesis in intact rabbit reticulocytes, Int. J. Biochem. 23 (1991) 605-608.
55. X. Shen, R.E. Ellis, K. Lee, C.Y. Liu, K. Yang, A. Solomon, H. Yoshida, R. Morimoto, D.M. Kunit, K. Mori, R.J. Kaufman, Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development, Cell 107 (2001) 893-903.
56. H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, K. Mori, 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.
57. M. Calfon, H. Zeng, F. Urano, J.H. Till, S.R. Hubbart, H.P. Harding, S.G. Clark, D. Ron, IRE1 couples endoplasmic reticulum load to secretory capacity by processing XBP1 mRNA, Nature 415 (2002) 92-96.
58. W. Paschen, J. Doutheil, C. Gissel, M. Treiman, Depletion of neuronal endoplasmic reticulum calcium stores by thapsigargin: effect on protein synthesis, J. Neurochem. 67 (1996) 1735-1743.
59. J. Doutheil, C. Gissel, U. Oschlies, K.-A. Hossmann, W. Paschen, Relation of neuronal endoplasmic reticulum calcium homeostasis to ribosomal aggregation and protein synthesis: implications for stress-induced suppression of protein synthesis, Brain Res. 775 (1997) 43-51.
60. C. Gissel, J. Doutheil, W. Paschen, Activation of heme oxygenase-1 expression by disturbances of endoplasmic reticulum calcium homeostasis in rat neuronal cell culture, Neurosci. Lett. 231 (1997) 1-4.
61. T. Linden, J. Doutheil, W. Paschen, Role of calcium in the activation of erp72 and heme oxygenase-1 expression on depletion of endoplasmic reticulum calcium stores in rat neuronal cell cultures, Neurosci. Lett. 245 (1998) 103-106.
62. R. Kumar, S. Azam, J.M. Sullivan, C. Owen, D.R.C. Cavener, P. Zhang, D. Ron, H.P. Harding, J.-J. Chen, A. Han, B.C. White, G.S. Krause, D.J. DeGracia, Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK, J. Neurochem. 77 (2001) 1418-1421.
63. W. Paschen, C. Aufenberg, S. Hotop, T. Mengesdorf, Transient cerebral ischemia activates processing of xbp1 mRNA indicative of endoplasmic reticulum stress, J. Cereb. Blood Flow. Metabol. 23 (2003) 449-461.
64. S. Wang, F.M. Longo, J. Chen, M. Butman, S.H. Graham, K.G. Haglid, F.R. Sharp, Induction of glucose regulated protein (grp78) and inducible heat-shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal cerebral ischemia, Neurochem. Int. 23 (1993) 575-582.
65. T. Higashi, H. Takechi, Y. Uemura, H. Kikuchi, K. Nagata, Differential induction of mRNA species encoding several classes of stress proteins following focal cerebral ischemia in rats, Barin Res. 650 (1994) 239-248.
66. D.H. Lowenstein, R.P. Gwinn, M.S. Seren, R.P. Simon, T.K. McIntosh, Increased expression of mRNA encoding calbindin-D28K, the glucose regulated protein, or the 72 kDa heat-shock protein in three models of acute CNS injury, Brain Res. Mol. Brain Res. 22 (1994) 299-308.
67. W. Paschen, C. Gissel, T. Linden, J. Doutheil, Erp72 expression activated by transient cerebral ischemia or disturbances of neuronal endoplasmic reticulum calcium stores, Metabol. Brain Dis. 13 (1998) 55-68.
68. W. Paschen, C. Gissel, T. Linden, S. Althausen, J. Doutheil, Activation of gadd153 expression through transient cerebral ischemia: evidence that ischemia causes endoplasmic reticulum dysfunction, Brain Res. Mol. Brain Res. 60 (1998) 115-122.
69. Y, Yagita, K. Kitagawa, A. Taguchi, T. Ohtsuki, K. Kawabara, T. Mabuchi, M. Matsumoto, T. Yanagihara, M. Hori, Molecular cloning of a novel member of the HSP110 family of genes, ischemia-responsive protein 94 kDa (irp94), expressed in rat brain after transient forebrain ischemia, J. Neurochem. 72 (1999) 1544-1551.
70. S.W. Kim, I.S. Yoo, H.S. Koh, O.Y. Kwon, Ischemia-responsive protein (irp94) is up-regulated by endoplasmic reticulum stress, Z. Naturforsch. 56 (2001) 1169-1171.
71. A. Yamaguchi, O. Hori, D.M. Stern, E. Hartmann, S. Ogawa, M. Tohyama, Stress-associated endoplasmic reticulum 1 (SERP1)/ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation, J. Cell Biol. 147 (1999) 1195-1204.
72. 2+-ATPase: relationship between global protein synthesis and expression and translation of individual genes, Biochem. J. 356 (2001) 805-812.
73. J.N. Keller, F.F. Huang, H. Zhu, J. Yu, Y.S. Ho, M.S. Kindy, Oxidative stress-associated impairment of proteasome activity during ischemia-reperfusion injury, J. Cereb. Blood Flow. Metabol. 20 (2000) 1467-1473.
74. B.R. Hu, M.E. Martone, Y.Z. Yones, C.L. Liu, Protein aggregation after transient cerebral ischemia, J. Neurosci. 20 (2000) 3191-3199.
75. T. Mengesdorf, P.H. Jensen, G. Mies, C. Aufenberg, W. Paschen, 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.
76. A. Pisani, P. Bonsi, D. Centonze, P. Giacomini, P. Calabresi, Involvement of intracellular calcium stores during oxygen/glucose deprivation in striatal large aspiny interneurons, J. Cereb. Blood Flow. Metabol. 20 (2000) 839-846.
77. 2+-ATPase, J. Neurochem. 68 (1997) 1124-1134.
78. 2+-ATPase, Brain Res. 834 (1999) 32-41.
79. K. Kohno, T. Higuchi, S. Ohta, K. Kohno, Y. Kumon, S. Sakaki, Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil, Neurosci. Lett. 224 (1997) 17-20.
80. J. Doutheil, S. Althausen, M. Treiman, W. Paschen, Effect of nitric oxide on endoplasmic reticulum calcium homeostasis, protein synthesis and energy metabolism, Cell Calcium 27 (2000) 107-115.
81. 2+ stores and protein synthesis in human endothelial cells, Circ. Res. 76 (1995) 388-395.
82. 2+-transport and protection by stobadine, Biochem. Mol. Biol. Int. 36 (1995) 569-577.
83. 2+-ATPase by peroxynitrite, Free Radic. Res. 24 (1996) 243-259.
84. W. Paschen, T. Mengesdorf, S. Althausen, S. Hotop, Peroxidative stress selectively down-regulates the neuronal stress response activated under conditions of endoplasmic reticulum dysfunction, J. Neurochem. 76 (2001) 1916-1924.
85. A. Frandsen, A. Schousboe, Mobilization of dantrolene-sensitive intracellular calcium pools is involved in the cytotoxicity induced by quisqualate and N-methyl-D-aspartate but not by 2-amino-3-(3-hydroxy-5-methylisoxaxol-4-yl)propionate and kainate in cultured cerebral cortical neurons, Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 2590-2594.
86. H.F. Weih, D.C. Perry, Dantrolene is cytoprotective in two models of neuronal cell death, J. Neurochem. 67 (1996) 2390-2398.
87. L. Zhang, Y. Andou, S. Masuda, A. Milani, K. Kataoka, Dantrolene protects against ischemic, delayed neuronal death in gerbil brain, Neurosci. Lett. 158 (1993) 105-108.
88. A. Asai, N. Tanahashi, J.-H. Qiu, N. Saito, S. Chi, N. Kawahara, K. Tanaka, T. Kirino, Selective proteasomal dysfunction in the hippocampal CA1 region after transient forebrain ischemia, J. Cereb. Blood Flow. Metabol. 22 (2002) 705-710.
89. B.-R. Hu, S. Janelidze, M.D. Ginsberg, R. Busto, M. Perez-Pinzon, T.J. Sick, B.K. Siesjö, C.L. Liu, Protein aggregation after focal cerebral ischemia and reperfusion, J. Cereb. Blood Flow. Metabol. 21 (2001) 865-875.
90. Y. Imai, M. Soda, R. Takahashi, Parkin suppress unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity, J. Biol. Chem. 275 (2000) 35661-35664.
91. B.R. Hu, M.E. Martone, C.L. Liu, Protein aggregation and delayed neuronal death after brain ischemia, Society for Neuroscience Meeting Orlando, 2002, abstract 488.11.
92. N.F. Bence, R.M. Sampat, R.R. Kopito, Impairment of the ubiquitin-proteasomal system by protein aggregation, Science 292 (2001) 1552-1555.
93. K.T. Bush, A.L. Goldberg, S.K. Nigam, Proteasome inhibition leads to a heat-shock response, induction of emdoplasmic reticulum chaperons, and thermotolerance, J. Biol. Chem. 272 (1997) 9086-9092.
94. R.Y. Hampton, ER stress response: getting the UPR hand on misfolded proteins, Curr. Biol. 10 (2000) R518-R521.
95. J. Zimmermann, D. Erdmann, I. Lalande, R. Grossenbacher, M. Noorani, P. Furst, Proteasome inhibitor induced gene expression profiles reveal overexpression of transcription factors ATF3, GADD153 and MAD1, Oncogene 19 (2000) 2913-2920.
96. M. Berg, T. Bruhn, A. Frandsen, A. Schousboe, Kainic acid-induced seizures and brain damage in the rat: role of calcium homeostasis, J. Neurosci. Res. 40 (1995) 641-646.
97. M. Niebauer, M. Gruenthal, Neuroprotective effects of early vs. late administartion of dantrolene in experimental status epilepticus, Neuropharmacology 38 (1999) 1343-1348.
98. 2+ uptake, J. Neurochem. 75 (2000) 1209-1218.
99. A receptor associated mechanisms, Neurosci. Lett. 265 (1999) 95-98.
100. O.J. Castejon, Electron microscopic analysis of cortical biopsies in patients with traumatic brain injuries and dysfunction of neurobehavioural system, J. Submicr. Cytol. Pathol. 30 (1998) 145-156.
101. O.J. Castejon, Morphological astrocytic changes in complicated human brain trauma: a light and electron microscopic study, Brain Injury 12 (1998) 409-427.
102. J.W. Putney, C.M.P. Ribeiro, Signaling pathways between the plasma membrane and endoplasmic reticulum calcium stores, Cell Mol. Life Sci. 57 (2000) 1272-1286.
103. 2+ release: an intimate connection, Trends Biochem. Sci. 25 (2000) 215-221.
104. J. Häcki, L. Egger, L. Monney, S. Conus, T. Rosse, I. Fellay, C. Borner, Apoptotic cross-talk between the endoplasmic reticulum and mitochondria controlled by Bcl-2, Oncogene 19 (2000) 2286-2295.
105. P. Boya, I. Cohen, N. Zamzami, H.L.A. Vieira, G. Kroemer, Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization, Cell Death Diff. 9 (2002) 465-467.
106. M. Germain, J.P. Mathai, G.C. Shore, BH-3-only BIP functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria, J. Biol. Chem. 277 (2002) 18053-18060.
107. O. Hori, F. Ichinoda, T. Tamatani, A. Yamaguchi, N. Sato, K. Ozawa, Y. Kitao, M. Miyazaki, H.P. Harding, D. Ron, M. Tohyama, D.M. Stern, S. Ogawa, Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease, J. Cell Biol. 157 (2002) 1151-1160.
108. N. Noshita, T. Sugawara, M. Fujimura, Y. Morita-Fujimura, P.H. Chan, Manganese superoxide dismutase affects cytochrome c release and caspase 9 activation after transient focal cerebral ischemia in mice, J. Cereb. Blood Flow Metabol. 21 (2001) 557-567.
109. C.M. Coughlan, K.C. Breen, Factors influencing the processing of function of the amyloid beta precursor protein: a potential therapeutic target in Alzheimer's disease? Pharmacol. Therap. 86 (2000) 111-144.
110. M.P. Mattson, F.M. LaFerla, S.L. Chan, M.A. Leissring, P.N. Shepel, J.D. Geiger, Calcium signaling in the ER: its role in neuronal plasticity and neurodegenerative disorders, Trends Neurosci. 23 (2000) 222-229.
111. M.P. Mattson, S.L. Chan, Dysregulation of cellular calcium homeostasis in Alzheimer's disease: bad genes and bad habits, J. Mol. Neurosci. 17 (2001) 205-224.
112. F.M. LaFerla, Calcium dysregulation and intracellular signaling in Alzheimer's disease, Nature Rev. Neurosci. 3 (2002) 862-872.
113. A. Verkhratsky, O.H. Petersen, The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death, Eur. J. Pharmacol. 447 (2002) 141-154.
114. K.K.K. Chung, V.L. Dawson, T.M. Dawson, The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders, Trends Neurosci. 24 (11, Suppl. 1) (2001) S7-S14.
115. T. Katayama, K. Imaizumi, N. Sato, K. Miyoshi, T. Kudo, J. Hitomi, T. Morihara, T. Yoneda, F. Gomi, Y. Mori, J. Nakano, J. Takeda, T. Tsuda, Y. Itoyama, O. Murayama, A. Takashima, P. St. George-Hyslop, M. Takeda, M. Tohyama, Presenilin-1 mutations down-regulate the signalling pathway of the unfolded protein response, Nature Cell Biol. 1 (1999) 479-485.
116. K. Miyoshi, T. Katayama, K. Imaizumi, M. Taniguchi, Y. Mori, J. Hitomi, D.S. Yui, T. Manabe, F. Gomi, T. Yoneda, M. Tohyama, Characterization of mouse Ire1 alpha: cloning, mRNA localization in the brain and functional analysis in neural cell line, Mol. Brain Res. 85 (2000) 68-76.
117. N. Sato, F. Urano, J.Y. Leem, S.-H. Kim, M. Li, D. Donoviel, A. Bernstein, A.S. Lee, D. Ron, M.L. Veselits, S.S. Sisodia, G. Thinakaran, Up-regulation of BIP and CHOP by the unfolded-protein response is independent of presenilin expression, Nature Cell Biol. 2 (2000) 863-870.
118. Y. Yasuda, T. Kudo, T. Katayama, K. Imaizumi, M. Yatera, M. Okochi, H. Yamamori, N. Matsumoto, T. Kida, A. Fukumori, M. Okumura, M. Tohyama, M. Takeda, FAD-linked presenilin-1 mutations impede translation regulation under ER stress, Biochem. Biophys. Res. Commun. 296 (2002) 313-318.
119. N.S. Langstrom, J.P. Anderson, H.G. Lindroos, B. Winblad, W.C. Wallace, Alzheimer's disease-associated reduction of polysomal mRNA translation, Mol. Brain Res. 5 (1989) 259-269.
120. J.A. Watt, C.J. Pike, A.J. Walencewicz-Wasserman, C.W. Cotman, Ultrastructural analysis of β-amyloid apoptosis in cultured hippocampal neurons, Brain Res. 661 (1994) 147-156.
121. Q. Guo, K. Furukawa, B.L. Sopher, D.G. Pham, N. Robinson, G.M. Martin, M.P. Mattson, Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid beta-peptide, NeuroReport 8 (1996) 379-383.
122. Q. Guo, B.L. Sopher, M.W. Miller, C.B. Ware, G.M. Martin, M.P. Mattson, Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock in mice, Nature Med. 5 (1999) 101-107.
123. Q. Guo, L. Sebastian, B.L. Sopher, M.W. Miller, G.W. Glazner, C.B. Ware, G.M. Martin, M.P. Mattson, Neurotrophic factors [activity-dependent neurotrophic factor (ADNF) and basic fibroblast growth factor (bFGF)] interrupt excitotoxic neurodegenerative cascades promoted by a presenilin-1 mutation, Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 4125-4130.
124. 2+ entry in human neuroblastoma (SH-SY5Y) cells expressing a familial Alzheimer's disease presenilin-1 mutation, Brain Res. 949 (2002) 105-111.
125. H.T. Orr, Beyond the Qs in the polyglutamine diseases, Genes Dev. 15 (2001) 925-932.
126. D. Martindale, A. Hackam, A. Wieczorek, L. Ellerby, C. Wellington, D. McCutcheon, R. Singaraja, P. Kazemiesfarjani, R. Devon, S.U. Kim, D.E. Bredesen, F. Tufaro, M.R. Hayden, Length of huntingtin and its polyglutamin tract influences localization and frequency of intracellular aggregates, Nature Gen. 18 (1998) 150-154.
127. K.L. Moulder, O. Onodera, J.P. Burke, W.J. Strittmatter, E.M. Johnson Jr., Generation of neuronal intranuclear inclusions by polyglutamine-GFP: analysis of inclusion clearance and toxicity as a function of polyglutamine length, J. Neurosci. 19 (1999) 705-715.
128. Y. Kouroku, E. Fujita, A. Jimbo, T. Kikuchi, T. Yamagata, M.Y. Momoi, E. Kominami, K. Kuida, K. Sakamaki, S. Yonehara, T. Momoi, Polyglutamine aggregates stimulate ER stress signals and caspase 12 activation, Hum. Mol. Gen. 11 (2002) 1505-1515.
129. H. Nishito, A. Matsuzawa, K. Tobiume, K. Saegusa, K. Takeda, K. Inoue, K. Hori, A. Kakizuka, H. Ichijo, ASK1 is essential for endoplasmic reticulum stress-induced cell death triggered by expanded polyglutamine repeats, Genes Dev. 16 (2002) 1345-1355.
130. H. Shimura, N. Hattori, S. Kubo, Y. Mizuno, S. Asakawa, S. Minoshima, N. Shimizu, K. Iwai, T. Chiba, K. Tanaka, T. Suzuki, Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase, Nature Gen. 25 (2000) 302-305.
131. Y. Zhang, J. Gao, K.K.K. Chung, H. Huang, V.L. Dawson, T.M. Dawson, Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCCrel-1, Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 13354-13359.
132. M.D. Ledesma, C. Galvan, B. Hellias, C. Dotti, P.H. Jensen, Astracytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress, J. Neurochem. 83 (2002) 1431-1440.
133. K.J. Travers, C.K. Patil, L. Wodicka, D.J. Lockhardt, J.S. Weissman, P. Walter, Functional and genomic analysis reveal an essential coordination between the unfolded protein response and ER-associated degradation, Cell 101 (2000) 249-258.
134. C. Caspersen, P.S. Pedersen, M. Treiman, The sarco/endoplasmic reticulum calcium ATPase 2b is an endoplasmic reticulum stress-inducible protein, J. Biol. Chem. 275 (2000) 22363-22372.
135. T. Sorimachi, H. Abe, S. Takeuchi, R. Tanaka, Ischemic depolarization monitoring: evaluation of protein synthesis in the hippocampal CA1 after brief unilateral ischemia in a gerbil model, J. Neurosurg. 97 (2002) 104-111.
136. W. Bodsch, K. Takahashi, A. Barbier, B. Grosse Ophoff, K.-A. Hossmann, Cerebral protein synthesis and ischemia, Progr. Brain Res. 63 (1985) 197-210.
137. R. Thilmann, Y. Xie, P. Kleihues, M. Kiessling, Persistent inhibition of protein synthesis precedes delayed neuronal death in post-ischemic gerbil hippocampus, Acta Neuropathol. (Berlin) 71 (1986) 88-93.
138. M.D. Linnik, R.H. Zobrist, M.D. Hatfield, Evidence supporting a role for programmed cell death in focal cerebral ischemia in rats, Stroke 24 (1993) 2002-2009.
139. J.P. MaManus, A.M. Buchan, I.E. Hill, I. Rasquina, E. Preston, Global ischemia can cause DNA fragmentation indicative of apoptosis in rat brain, Neurosci. Lett. 164 (1993) 89-92.
140. M. Okamoto, M. Matsumoto, T. Ohtsuki, A. Taguchi, K. Mikoshiba, T. Yanagihara, T. Kamada, Internucleosomal DNA cleavage involved in ischemia-induced neuronal death, Biochem. Biophys. Res. Commun. 196 (1993) 1356-1362.
141. J.P. MacManus, A.M. Buchan, Apoptosis after stroke: fact or fashion? J. Neurotrauma 17 (2000) 899-914.
142. M.P. Mattson, W. Duan, W.A. Pedersen, C. Culmsee, Neurodegenerative disorders and ischemic brain diseases, Apotosis 6 (2001) 69-81.
143. S.H. Graham, J. Chen, Programmed cell death in cerebral ischemia, J. Cereb. Blood Flow. Metabol. 21 (2001) 99-109.
144. H.P. Harding, Y.H. Zhang, A. Pertolotti, H.Q. Zeng, D. Ron, PERK is essential for translational regulation and cell survival during the unfolded protein response, Mol. Cell 5 (2000) 897-904.
145. -/- mice reveal a role for translational control in secretory cell survival, Mol. Cell 7 (2001) 1153-1163.
146. S. Oyadomari, E. Araki, M. Mori, Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells, Apoptosis 7 (2002) 335-345.
147. 2+ increases and cell death, J. Biol. Chem. 273 (1998) 12858-12862.
148. K.T. Bush, S.K. George, P.L. Zhang, S.K. Nigam, Pre-treatment with inducers of ER molecular chaperones protects epithelial cells subjected to ATP depletion, Am. J. Physiol. 277 (1999) F211-F218.
149. J. Lee, A.J. Bruce-Keller, Y. Kruman, S.L. Chan, M.P. Mattson, 2-Deoxy-D-glucose protects hippocampal neurons against excitotoxic and oxidative injury: evidence for the involvement of stress proteins, J. Neurosci. Res. 57 (1999) 48-61.
150. Z.F. Yu, H. Luo, W.M. Fu, M.P. Mattson, The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis, Exp. Neurol. 155 (1999) 302-314.
151. M.A. Brostrom, C.O. Brostrom, Calcium dependent regulation of protein synthesis in intact mammalian cells, Ann. Rev. Physiol. 52 (1990) 557-590.
152. T.S. McCormick, K.S. McColl, C.W. Distelhorst, Mouse lymphoma cells destined to undergo apoptosis in response to thapsigargin fail to generate a calcium-mediated grp78/grp94 stress response, J. Biol. Chem. 272 (1997) 6087-6092.
153. 2+ increases and cell death, J. Biol. Chem. 273 (1998) 12858-12862.
154. J. Lee, A.J. Bruce-Keller, Y. Kruman, S.L. Chan, M.P. Mattson, 2-Deoxy-D-glucose protects hippocampal neurons against excitotoxic and oxidative injury: evidence for the involvement of stress proteins, J. Neurosci. Res. 57 (1999) 48-61.
155. Z.F. Yu, H. Luo, W.M. Fu, M.P. Mattson, The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis, Exp. Neurol. 155 (1999) 302-314.
156. M. Aoki, M. Tamatani, A. Taniguchi, Y. Bando, K. Kasai, Y. Miyoshi, Y. Nakamura, M.P. Vitek, M. Tohyama, H. Tanaka, H. Sugimoto, Hypothermic treatment restores glucose regulated protein (GRP78) expression in ischemic brain, Mol. Brain Res. 95 (2001) 117-128.
157. T.S. Nowak Jr., Protein synthesis and the heat-shock/stress response after ischemia, Cereb. Brain Metabol. Rev. 2 (1990) 345-366.
158. S.M. Massa, R.A. Swanson, F.R. Sharp, The stress response in brain, Cereb. Brain Metabol. Rev. 8 (1996) 95-158.
159. A. Hara, T. Iwai, M. Niwa, T. Uematsu, N. Yoshimi, T. Tanaka, H. Mori, Immunohistochemical detection of Bax and Bcl-2 proteins in gerbil hippocampus following transient forebrain ischemia, Brain Res. 711 (1996) 249-253.
160. J. Chen, S.H. Graham, M. Nakayama, R.L. Zhu, K.L. Jin, R.A. Stetler, R.P. Simon, Apoptosis repressor genes Bcl-2 and Bcl-x-long are expressed in the rat following global ischemia, J. Cereb. Blood Flow. Metabol. 17 (1997) 2-10.