메뉴 건너뛰기




Volumn 26, Issue 8, 2004, Pages 827-834

Ischemic neuronal cell death and organellae damage

Author keywords

Apoptosis; Calcium; Cell death; Organelle

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ANTAGONIST; CYTOCHROME C; GENOMIC DNA; GUANINE NUCLEOTIDE EXCHANGE FACTOR; LAMOTRIGINE; LIPID; PHENYTOIN; PHOSPHOTRANSFERASE; PROTEINASE; TRIACYLGLYCEROL LIPASE;

EID: 10344240894     PISSN: 01616412     EISSN: None     Source Type: Journal    
DOI: 10.1179/016164104X3770     Document Type: Review
Times cited : (52)

References (81)
  • 1
    • 0016197163 scopus 로고
    • Cerebral infarction: Evolution of histopathological changes after occlusion of a middle cerebral artery in primates
    • Garcia JH, Kamijyo Y. Cerebral infarction: evolution of histopathological changes after occlusion of a middle cerebral artery in primates. Exp Neurol 1974; 33: 408-421
    • (1974) Exp Neurol , vol.33 , pp. 408-421
    • Garcia, J.H.1    Kamijyo, Y.2
  • 2
    • 0020526630 scopus 로고
    • Intracellular pH in the brain following transient ischemia
    • Mabe H, Blomqvist P, Siesjo BK. Intracellular pH in the brain following transient ischemia. J Cereb Blood Flow Metab 1983; 3: 109-114
    • (1983) J Cereb Blood Flow Metab , vol.3 , pp. 109-114
    • Mabe, H.1    Blomqvist, P.2    Siesjo, B.K.3
  • 3
    • 0024429317 scopus 로고
    • Dynamics of extracellular metabolites in the striatum after middle cerebral artery occlusion in the rat monitored by intracerebral microdialysis
    • Hillered L, Hallstrom A, Segersvard S, et al. Dynamics of extracellular metabolites in the striatum after middle cerebral artery occlusion in the rat monitored by intracerebral microdialysis. J Cereb Blood Flow Metab 1989; 9: 607-616
    • (1989) J Cereb Blood Flow Metab , vol.9 , pp. 607-616
    • Hillered, L.1    Hallstrom, A.2    Segersvard, S.3
  • 4
    • 0029834603 scopus 로고    scopus 로고
    • Immediate early gene expression in response to cerebral ischemia. Friend or foe?
    • Akins PT, Liu PK, Hsu CY. Immediate early gene expression in response to cerebral ischemia. Friend or foe? Stroke 1996; 27: 1682-1687
    • (1996) Stroke , vol.27 , pp. 1682-1687
    • Akins, P.T.1    Liu, P.K.2    Hsu, C.Y.3
  • 5
    • 0021363366 scopus 로고
    • Brain injury, edema, and vascular permeability changes induced by oxygen-derived free radicals
    • Chan PH, Schmidley JW, Fishman RA, et al. Brain injury, edema, and vascular permeability changes induced by oxygen-derived free radicals. Neurology 1984; 34: 315-320
    • (1984) Neurology , vol.34 , pp. 315-320
    • Chan, P.H.1    Schmidley, J.W.2    Fishman, R.A.3
  • 6
    • 0033789565 scopus 로고    scopus 로고
    • Free radical pathways in CNS injury
    • Lewen A, Matz P, Chan PH. Free radical pathways in CNS injury. J Neurotrauma 2000; 17: 871-890
    • (2000) J Neurotrauma , vol.17 , pp. 871-890
    • Lewen, A.1    Matz, P.2    Chan, P.H.3
  • 7
    • 0026522027 scopus 로고
    • The effect of the NMDA receptor antagonist MK-801 on cerebral blood flow and infarct volume in experimental focal stroke
    • Buchan AM, Slivka A, Xue D. The effect of the NMDA receptor antagonist MK-801 on cerebral blood flow and infarct volume in experimental focal stroke. Brain Res 1992; 574: 171-177
    • (1992) Brain Res , vol.574 , pp. 171-177
    • Buchan, A.M.1    Slivka, A.2    Xue, D.3
  • 8
    • 10344259267 scopus 로고
    • Measurement of regional cerebral blood flow by intra-carotid injection of xenon 133 in cerebral vascular accidents
    • Geraud J, Bes A, Delpla M, et al. Measurement of regional cerebral blood flow by intra-carotid injection of xenon 133 in cerebral vascular accidents. Acta Neurol Scand Suppl 1965; 14: 169-175
    • (1965) Acta Neurol Scand Suppl , vol.14 , pp. 169-175
    • Geraud, J.1    Bes, A.2    Delpla, M.3
  • 9
    • 0027058613 scopus 로고
    • Energy metabolism at the cellular level of the CNS
    • Hertz L, Peng L. Energy metabolism at the cellular level of the CNS. Can J Physiol Pharmacol 1992; 70: S145
    • (1992) Can J Physiol Pharmacol , vol.70
    • Hertz, L.1    Peng, L.2
  • 10
    • 10344255002 scopus 로고
    • Carbohydrate and energy metabolism of the central nervous system: Biochemical approach
    • Amsterdam: North-Holland Publishing Company
    • Bachelard HS. Carbohydrate and energy metabolism of the central nervous system: biochemical approach. Handbook of Neurology. Amsterdam: North-Holland Publishing Company, 1976; 27: 1
    • (1976) Handbook of Neurology , vol.27 , pp. 1
    • Bachelard, H.S.1
  • 11
    • 0021707433 scopus 로고
    • Elevation of the extracellular concentrations of glutamate and aspartate in rat hippocampus during transient cerebral ischemia monitored by intracerebral microdialysis
    • Benveniste H, Drejer J, Schousboe A, et al. Elevation of the extracellular concentrations of glutamate and aspartate in rat hippocampus during transient cerebral ischemia monitored by intracerebral microdialysis. J Neurochem 1984; 43: 1369-1374
    • (1984) J Neurochem , vol.43 , pp. 1369-1374
    • Benveniste, H.1    Drejer, J.2    Schousboe, A.3
  • 12
    • 0031840150 scopus 로고    scopus 로고
    • Calcium metabolism of focal and penumbral tissues in rats subjected to transient middle cerebral artery occlusion
    • Kristian T, Gido G, Kuroda S, et al. Calcium metabolism of focal and penumbral tissues in rats subjected to transient middle cerebral artery occlusion. Exp Brain Res 1998; 120: 503-509
    • (1998) Exp Brain Res , vol.120 , pp. 503-509
    • Kristian, T.1    Gido, G.2    Kuroda, S.3
  • 13
    • 0028979311 scopus 로고
    • Na+ channels as targets for neuroprotective drugs
    • Taylor CP, Meldrum BS. Na+ channels as targets for neuroprotective drugs. Trends Pharmacol Sci 1995; 16: 309-316
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 309-316
    • Taylor, C.P.1    Meldrum, B.S.2
  • 14
    • 0024513668 scopus 로고
    • Phenytoin protects against ischemia-produced neuronal cell death
    • Taft WC, Clifton GL, Blair RE, et al. Phenytoin protects against ischemia-produced neuronal cell death. Brain Res 1989; 483: 143-148
    • (1989) Brain Res , vol.483 , pp. 143-148
    • Taft, W.C.1    Clifton, G.L.2    Blair, R.E.3
  • 15
    • 0028939058 scopus 로고
    • Neuroprotective properties of the novel antiepileptic lamotrigine in a gerbil model of global cerebral ischemia
    • Wiard RP, Dickerson MC, Beek O, et al. Neuroprotective properties of the novel antiepileptic lamotrigine in a gerbil model of global cerebral ischemia. Stroke 1995; 26: 466-472
    • (1995) Stroke , vol.26 , pp. 466-472
    • Wiard, R.P.1    Dickerson, M.C.2    Beek, O.3
  • 16
    • 0028799654 scopus 로고
    • Calcium: Still center-stage in hypoxic-ischemic neuronal death
    • Choi D. Calcium: still center-stage in hypoxic-ischemic neuronal death. Trends Neurosci 1995; 18: 58-60
    • (1995) Trends Neurosci , vol.18 , pp. 58-60
    • Choi, D.1
  • 17
    • 0027474041 scopus 로고
    • Glutamate receptor-induced 45Ca2+ accumulation in cortical cell culture correlates with subsequent neuronal degeneration
    • Hartley DM, Kurth MC, Bjerkness L, et al. Glutamate receptor-induced 45Ca2+ accumulation in cortical cell culture correlates with subsequent neuronal degeneration. J Neurosci 1993; 13: 1993-2000
    • (1993) J Neurosci , vol.13 , pp. 1993-2000
    • Hartley, D.M.1    Kurth, M.C.2    Bjerkness, L.3
  • 18
    • 0026752505 scopus 로고
    • Calcium ions and oxidative cell injury
    • Orrenius S, Burkitt MJ, Kass GE, et al. Calcium ions and oxidative cell injury. Ann Neurol 1992; 32 Suppl: S33-S42
    • (1992) Ann Neurol , vol.32 , Issue.SUPPL.
    • Orrenius, S.1    Burkitt, M.J.2    Kass, G.E.3
  • 19
    • 0035134235 scopus 로고    scopus 로고
    • Calcium antagonists for ischemic stroke. A systematic review
    • Horn J, Limburg M. Calcium antagonists for ischemic stroke. A systematic review. Stroke 2001; 32: 570-576
    • (2001) Stroke , vol.32 , pp. 570-576
    • Horn, J.1    Limburg, M.2
  • 20
    • 0023225212 scopus 로고
    • The therapeutic value of nimodipine in experimental focal cerebral ischemia. Neurological outcome and histopathological findings
    • Germano IM, Bartkowski HM, Cassel ME, et al. The therapeutic value of nimodipine in experimental focal cerebral ischemia. Neurological outcome and histopathological findings. J Neurosurg 1987; 67: 81-87
    • (1987) J Neurosurg , vol.67 , pp. 81-87
    • Germano, I.M.1    Bartkowski, H.M.2    Cassel, M.E.3
  • 21
    • 0019270386 scopus 로고
    • Membrane lipids in the pathogenesis of brain edema: Phospholipids and arachidonic acid, the earliest membrane components changed at the onset of ischemia
    • Bazan NG, Rodriguez de Turco EB. Membrane lipids in the pathogenesis of brain edema: phospholipids and arachidonic acid, the earliest membrane components changed at the onset of ischemia. Adv Neurol 1980; 28: 197-205
    • (1980) Adv Neurol , vol.28 , pp. 197-205
    • Bazan, N.G.1    Rodriguez De Turco, E.B.2
  • 22
    • 0027081205 scopus 로고
    • Enhancement of hippocampal excitatory synaptic transmission by platelet-activating factor
    • Clark GD, Happel LT, Zorumski CF, et al. Enhancement of hippocampal excitatory synaptic transmission by platelet-activating factor. Neuron 1992; 9: 1211-1216
    • (1992) Neuron , vol.9 , pp. 1211-1216
    • Clark, G.D.1    Happel, L.T.2    Zorumski, C.F.3
  • 23
    • 0028229156 scopus 로고
    • Platelet-activating factor and retinoic acid synergistically activate the inducible prostaglandin synthase gene
    • Bazan NG, Fletcher BS, Herschman HR, et al. Platelet-activating factor and retinoic acid synergistically activate the inducible prostaglandin synthase gene. Proc Natl Acad Sci USA 1994; 91: 5252-5256
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5252-5256
    • Bazan, N.G.1    Fletcher, B.S.2    Herschman, H.R.3
  • 24
    • 0000994567 scopus 로고    scopus 로고
    • Oxidative stress: Adaptation, damage, repair and death
    • Halliwell B, Gutteridge JMC, eds, New York: Oxford University Press
    • Halliwell B, Gutteridge JMC. Oxidative stress: adaptation, damage, repair and death. In: Halliwell B, Gutteridge JMC, eds, Free Radicals in Biology and Medicine. New York: Oxford University Press, 1999
    • (1999) Free Radicals in Biology and Medicine
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 25
    • 0010737535 scopus 로고    scopus 로고
    • Loss of neuronal calcium homeostasis in ischemia
    • Welch KMA, Caplan LR, Reis DJ, et al., eds, San Diego: Academic Press
    • Erecinska M, Silver IA. Loss of neuronal calcium homeostasis in ischemia. In: Welch KMA, Caplan LR, Reis DJ, et al., eds, Primer on Cerebrovascular Diseases. San Diego: Academic Press, 1997
    • (1997) Primer on Cerebrovascular Diseases
    • Erecinska, M.1    Silver, I.A.2
  • 26
    • 0025295264 scopus 로고
    • Intracelluar and extracellular changes of [Ca2+] in hypoxia and ischemia in rat brain in vivo
    • Silver IA, Erecinska M. Intracelluar and extracellular changes of [Ca2+] in hypoxia and ischemia in rat brain in vivo. J Gen Physiol 1990; 95: 837-866
    • (1990) J Gen Physiol , vol.95 , pp. 837-866
    • Silver, I.A.1    Erecinska, M.2
  • 27
    • 0027501890 scopus 로고
    • Upregulation of calpain activity in neonatal rat brain after hypoxic-ischemia
    • Ostwald K, Hagberg H, Andine P, et al. Upregulation of calpain activity in neonatal rat brain after hypoxic-ischemia. Brain Res 1993; 630: 289-294
    • (1993) Brain Res , vol.630 , pp. 289-294
    • Ostwald, K.1    Hagberg, H.2    Andine, P.3
  • 28
    • 0028098014 scopus 로고
    • Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia
    • Hong SC, Goto Y, Lanzino G, et al. Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia. Stroke 1994; 25: 663-669
    • (1994) Stroke , vol.25 , pp. 663-669
    • Hong, S.C.1    Goto, Y.2    Lanzino, G.3
  • 29
    • 0042657790 scopus 로고    scopus 로고
    • Calpain induces proteolysis of neuronal cytoskeleton in ischemic gerbil forebrain
    • Yokota M, Saido TC, Kamitani H, et al. Calpain induces proteolysis of neuronal cytoskeleton in ischemic gerbil forebrain. Brain Res 2003; 984: 122-132
    • (2003) Brain Res , vol.984 , pp. 122-132
    • Yokota, M.1    Saido, T.C.2    Kamitani, H.3
  • 30
    • 0026529437 scopus 로고
    • Effect of brain ischemia on protein kinase C
    • Domanska-Janik K, Zalewska T. Effect of brain ischemia on protein kinase C. J Neurochem 1992; 58: 1432-1439
    • (1992) J Neurochem , vol.58 , pp. 1432-1439
    • Domanska-Janik, K.1    Zalewska, T.2
  • 31
    • 0030982798 scopus 로고    scopus 로고
    • Evidence that the early loss of membrane protein kinase C is a necessary step in the excitatory amino acid-induced death of primary cortical neurons
    • Durkin JP, Tremblay R, Chakravarthy B, et al. Evidence that the early loss of membrane protein kinase C is a necessary step in the excitatory amino acid-induced death of primary cortical neurons. J Neurochem 1997; 68: 1400-1412
    • (1997) J Neurochem , vol.68 , pp. 1400-1412
    • Durkin, J.P.1    Tremblay, R.2    Chakravarthy, B.3
  • 32
    • 0037146915 scopus 로고    scopus 로고
    • Coordinate expression of survival p-ERK and proapoptotic cytochrome c signals in rat brain neurons after transient MCAO
    • Li F, Omori N, Sato K, et al. Coordinate expression of survival p-ERK and proapoptotic cytochrome c signals in rat brain neurons after transient MCAO. Brain Res 2002; 958: 83-88
    • (2002) Brain Res , vol.958 , pp. 83-88
    • Li, F.1    Omori, N.2    Sato, K.3
  • 33
    • 0029132704 scopus 로고
    • Ischemic delayed neuronal death. A mitochondrial hypothesis
    • Abe K, Aoki M, Kawagoe J, et al. Ischemic delayed neuronal death. A mitochondrial hypothesis. Stroke 1995; 26: 1478-1489
    • (1995) Stroke , vol.26 , pp. 1478-1489
    • Abe, K.1    Aoki, M.2    Kawagoe, J.3
  • 34
    • 0027216632 scopus 로고
    • Changes of mitochondrial DNA and heat shock protein gene expressions in gerbil hippocampus after transient forebrain ischemia
    • Abe K, Kawagoe J, Aoki M, et al. Changes of mitochondrial DNA and heat shock protein gene expressions in gerbil hippocampus after transient forebrain ischemia. J Cereb Blood Flow Metab 1993; 13: 773-780
    • (1993) J Cereb Blood Flow Metab , vol.13 , pp. 773-780
    • Abe, K.1    Kawagoe, J.2    Aoki, M.3
  • 35
    • 0025673972 scopus 로고
    • Delayed decreases in specific brain mitochondrial electron transfer complex activities and cytochrome concentrations following anoxia/ischemia
    • Wagner KR, Kleinholz M, Myers RE. Delayed decreases in specific brain mitochondrial electron transfer complex activities and cytochrome concentrations following anoxia/ischemia. J Neurol Sci 1990; 100: 142-151
    • (1990) J Neurol Sci , vol.100 , pp. 142-151
    • Wagner, K.R.1    Kleinholz, M.2    Myers, R.E.3
  • 36
    • 0028816908 scopus 로고
    • Early immunohistochemical changes of microtubule based motor proteins in gerbil hippocampus after transient ischemia
    • Aoki M, Abe K, Yoshida T, et al. Early immunohistochemical changes of microtubule based motor proteins in gerbil hippocampus after transient ischemia. Brain Res 1995; 669: 189-196
    • (1995) Brain Res , vol.669 , pp. 189-196
    • Aoki, M.1    Abe, K.2    Yoshida, T.3
  • 38
    • 0033570503 scopus 로고    scopus 로고
    • Mitochondrial release of cytochrome c corresponds to the selective vulnerability of hippocampal CA1 neurons in rats after transient global cerebral ischemia
    • Sugawara T, Fujimura M, Morita-Fujimura Y, et al. Mitochondrial release of cytochrome c corresponds to the selective vulnerability of hippocampal CA1 neurons in rats after transient global cerebral ischemia. J Neurosci 1999; 19: RC39.
    • (1999) J Neurosci , vol.19
    • Sugawara, T.1    Fujimura, M.2    Morita-Fujimura, Y.3
  • 39
    • 0031737635 scopus 로고    scopus 로고
    • Cytosolic redistribution of cytochrome c after transient focal cerebral ischemia in rats
    • Fujimura M, Morita-Fujimura Y, Murakami K, et al. Cytosolic redistribution of cytochrome c after transient focal cerebral ischemia in rats. J Cereb Blood Flow Metab 1998; 18: 1239-1247
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 1239-1247
    • Fujimura, M.1    Morita-Fujimura, Y.2    Murakami, K.3
  • 40
    • 17444373424 scopus 로고    scopus 로고
    • Cytochrome C is released from mitochondria into the cytosol after cerebral anoxia or ischemia
    • Perez-Pinzon MA, Xu GP, Born J, et al. Cytochrome C is released from mitochondria into the cytosol after cerebral anoxia or ischemia. J Cereb Blood Flow Metab 1999; 19: 39-43
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 39-43
    • Perez-Pinzon, M.A.1    Xu, G.P.2    Born, J.3
  • 42
    • 0037191413 scopus 로고    scopus 로고
    • Subcellular localization of a promoter and an inhibitor of apoptosis (Smac/DIABLO and XIAP) during brain ischemia/reperfusion
    • Shibata M, Hattori H, Sasaki T, et al. Subcellular localization of a promoter and an inhibitor of apoptosis (Smac/DIABLO and XIAP) during brain ischemia/reperfusion. Neuroreport 2002; 13: 1985-1988
    • (2002) Neuroreport , vol.13 , pp. 1985-1988
    • Shibata, M.1    Hattori, H.2    Sasaki, T.3
  • 43
    • 0042838034 scopus 로고    scopus 로고
    • Interaction between XIAP and Smac/DIABLO in the mouse brain after transient focal cerebral ischemia
    • Saito A, Hayashi T, Okuno S, et al. Interaction between XIAP and Smac/DIABLO in the mouse brain after transient focal cerebral ischemia. J Cereb Blood Flow Metab 2003; 23: 1010-1019
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 1010-1019
    • Saito, A.1    Hayashi, T.2    Okuno, S.3
  • 44
    • 0033121301 scopus 로고    scopus 로고
    • Cytosolic Ca2+ changes during in vitro ischemia in rat hippocampal slices: Major roles for glutamate and Na+-dependent Ca2+ release from mitochondria
    • Zhang Y, Lipton P. Cytosolic Ca2+ changes during in vitro ischemia in rat hippocampal slices: major roles for glutamate and Na+-dependent Ca2+ release from mitochondria. J Neurosci 1999; 19: 3307-3315
    • (1999) J Neurosci , vol.19 , pp. 3307-3315
    • Zhang, Y.1    Lipton, P.2
  • 45
    • 0033495895 scopus 로고    scopus 로고
    • Blockade of the mitochondrial permeability transition pore diminishes infarct size in the rat after transient middle cerebral artery occlusion
    • Matsumoto S, Friberg H, Ferrand-Drake M, et al. Blockade of the mitochondrial permeability transition pore diminishes infarct size in the rat after transient middle cerebral artery occlusion. J Cereb Blood Flow Metab 1999; 19: 736-741
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 736-741
    • Matsumoto, S.1    Friberg, H.2    Ferrand-Drake, M.3
  • 46
    • 0035045290 scopus 로고    scopus 로고
    • Intracellular Bax translocation after transient cerebral ischemia: Implications for a role of the mitochondrial apoptotic signaling pathway in ischemic neuronal death
    • Cao G, Minami M, Pei W, et al. Intracellular Bax translocation after transient cerebral ischemia: implications for a role of the mitochondrial apoptotic signaling pathway in ischemic neuronal death. J Cereb Blood Flow Metab 2001; 21: 321-333
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 321-333
    • Cao, G.1    Minami, M.2    Pei, W.3
  • 47
    • 0034703589 scopus 로고    scopus 로고
    • Immunohistochemical expression of Bcl-2, Bax and cytochrome c following focal cerebral ischemia and effect of hypothermia in rat
    • Prakasa Babu P, Yoshida Y, Su M, et al. Immunohistochemical expression of Bcl-2, Bax and cytochrome c following focal cerebral ischemia and effect of hypothermia in rat. Neurosci Lett 2000; 291: 196-200
    • (2000) Neurosci Lett , vol.291 , pp. 196-200
    • Prakasa Babu, P.1    Yoshida, Y.2    Su, M.3
  • 48
    • 0036548511 scopus 로고    scopus 로고
    • The permeability transition pore signals apoptosis by directing Bax translocation and multimerization
    • De Giorgi F, Lartigue L, Bauer MK, et al. The permeability transition pore signals apoptosis by directing Bax translocation and multimerization. FASEB J 2002; 16: 607-609
    • (2002) FASEB J , vol.16 , pp. 607-609
    • De Giorgi, F.1    Lartigue, L.2    Bauer, M.K.3
  • 49
    • 0021968895 scopus 로고
    • Changes in brain energy metabolism and protein synthesis following transient bilateral ischemia in the gerbil
    • Nowak TS Jr, Fried RL, Lust WD, et al. Changes in brain energy metabolism and protein synthesis following transient bilateral ischemia in the gerbil. J Neurochem 1985; 44: 487-494
    • (1985) J Neurochem , vol.44 , pp. 487-494
    • Nowak Jr., T.S.1    Fried, R.L.2    Lust, W.D.3
  • 50
    • 0030730131 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2B (eIF2B)
    • Webb BL, Proud CG. Eukaryotic initiation factor 2B (eIF2B). Int J Biochem Cell Biol 1997; 29: 1127-1131
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 1127-1131
    • Webb, B.L.1    Proud, C.G.2
  • 51
    • 0032079873 scopus 로고    scopus 로고
    • Regulation of translation initiation factors by signal transduction
    • Kleijn M, Scheper GC, Voorma HO, et al. Regulation of translation initiation factors by signal transduction. Eur J Biochem 1998; 253: 531-544
    • (1998) Eur J Biochem , vol.253 , pp. 531-544
    • Kleijn, M.1    Scheper, G.C.2    Voorma, H.O.3
  • 52
    • 0023878562 scopus 로고
    • The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2
    • Rowlands AG, Panniers R, Henshaw EC. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J Biol Chem 1988; 263: 5526-5533
    • (1988) J Biol Chem , vol.263 , pp. 5526-5533
    • Rowlands, A.G.1    Panniers, R.2    Henshaw, E.C.3
  • 53
    • 0034889904 scopus 로고    scopus 로고
    • Changes in the phosphorylation of initiation factor eIF-2alpha, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice
    • Althausen S, Mengesdorf T, Mies G, et al. Changes in the phosphorylation of initiation factor eIF-2alpha, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice. J Neurochem 2001; 78: 779-787
    • (2001) J Neurochem , vol.78 , pp. 779-787
    • Althausen, S.1    Mengesdorf, T.2    Mies, G.3
  • 54
    • 0035901755 scopus 로고    scopus 로고
    • Ischemia-induced inhibition of the initiation factor 2α phosphatase activity in the rat brain
    • de la Vega CM, Burda J, Salinas M. Ischemia-induced inhibition of the initiation factor 2α phosphatase activity in the rat brain. Neuroreport 2001; 12: 1021-1025
    • (2001) Neuroreport , vol.12 , pp. 1021-1025
    • De La Vega, C.M.1    Burda, J.2    Salinas, M.3
  • 55
    • 0033534592 scopus 로고    scopus 로고
    • Activation of MYD116 (gadd34) expression following transient forebrain ischemia of rat: Implications for a role of disturbances of endoplasmic reticulum calcium homeostasis
    • Doutheil J, Althausen S, Gissel C, et al. Activation of MYD116 (gadd34) expression following transient forebrain ischemia of rat: implications for a role of disturbances of endoplasmic reticulum calcium homeostasis. Brain Res Mol Brain Res 1999; 63: 225-232
    • (1999) Brain Res Mol Brain Res , vol.63 , pp. 225-232
    • Doutheil, J.1    Althausen, S.2    Gissel, C.3
  • 56
    • 0034996080 scopus 로고    scopus 로고
    • Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK
    • Kumar R, Azam S, Sullivan JM, et al. Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK. J Neurochem 2001; 77: 1418-1421
    • (2001) J Neurochem , vol.77 , pp. 1418-1421
    • Kumar, R.1    Azam, S.2    Sullivan, J.M.3
  • 57
    • 0041568574 scopus 로고    scopus 로고
    • Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death
    • Hayashi T, Saito A, Okuno S, et al. Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death. J Cereb Blood Flow Metab 2003; 23: 949-961
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 949-961
    • Hayashi, T.1    Saito, A.2    Okuno, S.3
  • 58
    • 0141925706 scopus 로고    scopus 로고
    • Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal cell death
    • Hayashi T, Saito A, Okuno S, et al. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal cell death. J Cereb Blood Flow Metab 2003; 23: 1117-1128
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 1117-1128
    • Hayashi, T.1    Saito, A.2    Okuno, S.3
  • 59
    • 0032979420 scopus 로고    scopus 로고
    • Disturbances of the functioning of endoplasmic reticulum: A key mechanism underlying neuronal cell injury?
    • Paschen W, Doutheil J. Disturbances of the functioning of endoplasmic reticulum: a key mechanism underlying neuronal cell injury? J Cereb Blood Flow Metab 1999; 19: 1-18
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 1-18
    • Paschen, W.1    Doutheil, J.2
  • 62
    • 0037428823 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplasmic reticulum resident caspase, after permanent focal ischemia in rat
    • Mouw G, Zechel JL, Gamboa J, et al. Activation of caspase-12, an endoplasmic reticulum resident caspase, after permanent focal ischemia in rat. Neuroreport 2003; 14: 183-186
    • (2003) Neuroreport , vol.14 , pp. 183-186
    • Mouw, G.1    Zechel, J.L.2    Gamboa, J.3
  • 63
    • 0037426614 scopus 로고    scopus 로고
    • Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice
    • Shibata M, Hattori H, Sasaki T, et al. Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice. Neuroscience 2003; 118: 491-499
    • (2003) Neuroscience , vol.118 , pp. 491-499
    • Shibata, M.1    Hattori, H.2    Sasaki, T.3
  • 64
    • 0037442851 scopus 로고    scopus 로고
    • ER stress induces caspase-8 activation, stimulating cytochrome c release and caspase-9 activation
    • Jimbo A, Fujita E, Kouroku Y, et al. ER stress induces caspase-8 activation, stimulating cytochrome c release and caspase-9 activation. Exp Cell Res 2003; 283: 156-166
    • (2003) Exp Cell Res , vol.283 , pp. 156-166
    • Jimbo, A.1    Fujita, E.2    Kouroku, Y.3
  • 65
    • 0037386064 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response during global brain ischemia and reperfusion
    • Kumar R, Krause GS, Yoshida H, et al. Dysfunction of the unfolded protein response during global brain ischemia and reperfusion. J Cereb Blood Flow Metab 2003; 23: 462-471
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 462-471
    • Kumar, R.1    Krause, G.S.2    Yoshida, H.3
  • 66
    • 0037385160 scopus 로고    scopus 로고
    • Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress
    • Paschen W, Aufenberg C, Hotop S, et al. Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress. J Cereb Blood Flow Metab 2003; 23: 449-461
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 449-461
    • Paschen, W.1    Aufenberg, C.2    Hotop, S.3
  • 67
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signaling organelle
    • Berridge MJ. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 2002; 32: 235-249
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 69
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami N, Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat Rev Mol Cell Biol 2001; 2: 67-71
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 70
    • 0037441521 scopus 로고    scopus 로고
    • Brefeldin A-induced neurotoxicity in cultured spinal cord neurons
    • Kikuchi S, Shinpo K, Tsuji S, et al. Brefeldin A-induced neurotoxicity in cultured spinal cord neurons. J Neurosci Res 2003; 71: 591-599
    • (2003) J Neurosci Res , vol.71 , pp. 591-599
    • Kikuchi, S.1    Shinpo, K.2    Tsuji, S.3
  • 71
    • 0036943001 scopus 로고    scopus 로고
    • The Golgi apparatus is fragmented in spinal cord motor neurons of amyotrophic lateral sclerosis with basophilic inclusions
    • Fujita Y, Okamoto K, Sakurai A, et al. The Golgi apparatus is fragmented in spinal cord motor neurons of amyotrophic lateral sclerosis with basophilic inclusions. Acta Neuropathol (Berl) 2002; 103: 243-247
    • (2002) Acta Neuropathol (Berl) , vol.103 , pp. 243-247
    • Fujita, Y.1    Okamoto, K.2    Sakurai, A.3
  • 72
    • 0037115055 scopus 로고    scopus 로고
    • Identification of an axotomy-induced glycosylated protein, AIGP1, possibly involved in cell death triggered by endoplasmic reticulum-Golgi stress
    • Aoki S, Su Q, Li H, et al. Identification of an axotomy-induced glycosylated protein, AIGP1, possibly involved in cell death triggered by endoplasmic reticulum-Golgi stress. J Neurosci 2002; 22: 10751-10760
    • (2002) J Neurosci , vol.22 , pp. 10751-10760
    • Aoki, S.1    Su, Q.2    Li, H.3
  • 73
    • 0036710540 scopus 로고    scopus 로고
    • Ultrastructural and MRI study of the substantia nigra evolving exofocal post-ischemic neuronal death in the rat
    • Zhao F, Kuroiwa T, Miyasaka N, et al. Ultrastructural and MRI study of the substantia nigra evolving exofocal post-ischemic neuronal death in the rat. Neuropathology 2002; 22: 91-105
    • (2002) Neuropathology , vol.22 , pp. 91-105
    • Zhao, F.1    Kuroiwa, T.2    Miyasaka, N.3
  • 75
    • 0029124499 scopus 로고
    • Cell death. Programmed, apoptosis, necrosis, and other
    • Zakeri Z, Bursch W, Tenniswood M, et al. Cell death. Programmed, apoptosis, necrosis, and other. Cell Death Diff 1995; 2: 87-96
    • (1995) Cell Death Diff , vol.2 , pp. 87-96
    • Zakeri, Z.1    Bursch, W.2    Tenniswood, M.3
  • 76
    • 0036143203 scopus 로고    scopus 로고
    • Recent insights into the mechanism of glucocorticosteroid-induced apoptosis
    • Distelhorst CW. Recent insights into the mechanism of glucocorticosteroid-induced apoptosis. Cell Death Differ 2002; 9: 6-19
    • (2002) Cell Death Differ , vol.9 , pp. 6-19
    • Distelhorst, C.W.1
  • 77
    • 17744402995 scopus 로고    scopus 로고
    • Evaluation of lipid peroxidation, cathepsin L and acid phosphatase activities in experimental brain ischemia-reperfusion
    • Islekel H, Islekel S, Guner G, et al. Evaluation of lipid peroxidation, cathepsin L and acid phosphatase activities in experimental brain ischemia-reperfusion. Brain Res 1999; 843: 18-24
    • (1999) Brain Res , vol.843 , pp. 18-24
    • Islekel, H.1    Islekel, S.2    Guner, G.3
  • 78
    • 0038641715 scopus 로고    scopus 로고
    • 3-Aminopropanol, formed during cerebral ischemia, is a potent lysosomotrophic neurotoxin
    • Li W, Yuan XM, Ivanova S, et al. 3-aminopropanol, formed during cerebral ischemia, is a potent lysosomotrophic neurotoxin. Biochem J 2003; 371: 429-436
    • (2003) Biochem J , vol.371 , pp. 429-436
    • Li, W.1    Yuan, X.M.2    Ivanova, S.3
  • 79
    • 0032745303 scopus 로고    scopus 로고
    • Early decrease of XRCC1, a DNA base excision repair protein, may contribute to DNA fragmentation after transient focal cerebral ischemia in mice
    • Fujimura M, Morita-Fujimura Y, Sugawara T, et al. Early decrease of XRCC1, a DNA base excision repair protein, may contribute to DNA fragmentation after transient focal cerebral ischemia in mice. Stroke 1999; 30: 2456-2463
    • (1999) Stroke , vol.30 , pp. 2456-2463
    • Fujimura, M.1    Morita-Fujimura, Y.2    Sugawara, T.3
  • 80
    • 0034793211 scopus 로고    scopus 로고
    • Neuronal expression of the DNA repair protein Ku70 after ischemic preconditioning corresponds to tolerance to global cerebral ischemia
    • Sugawara T, Noshita N, Lewen A, et al. Neuronal expression of the DNA repair protein Ku70 after ischemic preconditioning corresponds to tolerance to global cerebral ischemia. Stroke 2001; 32: 2388-2393
    • (2001) Stroke , vol.32 , pp. 2388-2393
    • Sugawara, T.1    Noshita, N.2    Lewen, A.3
  • 81
    • 0242490147 scopus 로고    scopus 로고
    • Inducible repair of oxidative DNA lesions in the rat brain after transient focal ischemia and reperfusion
    • Lan J, Li W, Zhang F, et al. Inducible repair of oxidative DNA lesions in the rat brain after transient focal ischemia and reperfusion. J Cereb Blood Flow Metab 2003; 23: 1324-1339
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 1324-1339
    • Lan, J.1    Li, W.2    Zhang, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.