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Volumn 179, Issue 1-2, 2000, Pages 1-33

Brain ischemia and reperfusion: Molecular mechanisms of neuronal injury

Author keywords

Apoptosis; Brain ischemia; Growth factors; Lipid peroxidation; Signal transduction; Translation initiation

Indexed keywords

ADENOSINE; ADENOSINE TRIPHOSPHATE; ADRENALIN; ANTIOXIDANT; ARACHIDONIC ACID; CALCINEURIN; CALCIUM ION; CALPAIN; CALPASTATIN; CASPASE; CASPASE 9; CASPASE INHIBITOR; CATECHOLAMINE; CYTOCHROME C; CYTOSKELETON PROTEIN; GLUTAMIC ACID; GROWTH FACTOR; GROWTH FACTOR RECEPTOR; INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 4 G; IRON; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE INHIBITOR; OXYGEN RADICAL; PHOSPHOLIPASE; PROTEIN; PROTEIN KINASE; PROTEIN TYROSINE KINASE; SPECTRIN; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 0034306357     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-510X(00)00386-5     Document Type: Review
Times cited : (750)

References (458)
  • 1
    • 0007565709 scopus 로고    scopus 로고
    • Direct costs were calculated by Thomas A. Hodgson, chief economist and acting director, Division of Health and Utilization Analysis, OAEHP, NCHS, CDC. Estimates of indirect costs were made by Thomas J. Thom, statistician in the Division of Epidemiology and Clinical Applications, NHLBI.
  • 3
    • 0022590982 scopus 로고
    • Randomized clinical study of thiopental loading in comatose survivors of cardiac arrest
    • (1986) New Engl J Med , vol.314 , pp. 397-401
  • 4
    • 0025727272 scopus 로고
    • A randomized clinical study of a calcium-entry blocker (lidoflazine) in the treatment of comatose survivors of cardiac arrest
    • (1991) New Engl J Med , vol.324 , pp. 1225-1231
  • 5
    • 0043204506 scopus 로고    scopus 로고
    • A randomized trial of trilazad mesylate in patients with acute stroke
    • (1996) Stroke , vol.27 , pp. 1453-1458
  • 10
    • 0007481636 scopus 로고
    • Resuscitation and artificial hypothermia, New York: Consultants Bureau
    • (1962)
    • Negovskii, V.A.1
  • 16
    • 0023926783 scopus 로고
    • Attenuation of post-ischemic cerebral hypoperfusion by the 21-aminosteroid U74006F
    • (1988) Stroke , vol.10 , pp. 340-344
    • Hall, E.D.1    Yonkers, P.A.2
  • 23
    • 0026777223 scopus 로고
    • Pathophysiology and treatment of focal cerebral ischemia. I. Pathophysiology
    • (1992) J Neurosurg , vol.77 , pp. 169-184
    • Siesjo, B.K.1
  • 29
    • 0021972222 scopus 로고
    • Lipid peroxidation-induced inhibition of gamma-aminobutyric acid uptake in rat brain synaptosomes: protection by glucocorticoids
    • (1985) J Neurochem , vol.44 , pp. 1282-1286
    • Braughler, J.M.1
  • 42
    • 0025221754 scopus 로고
    • Regional difference in free fatty acids release and the action of phospholipase during ischemia in rat brain
    • (1990) No To Shinkei , vol.42 , pp. 979-986
    • Umemura, A.1
  • 51
    • 0018261933 scopus 로고
    • Interactions between iron metabolism and oxygen activation
    • Oxygen free radicals and tissue damage, New York: Excerpta Medica
    • (1979) Ciba foundation symposium , vol.65 vol. , pp. 57-66
    • Crichton, R.R.1
  • 53
    • 0025854274 scopus 로고
    • The double-edged role of nitric oxide in brain function and superoxide-mediated injury
    • (1991) J Dev Physiol , vol.15 , pp. 53-59
    • Beckman, J.S.1
  • 61
    • 0025697262 scopus 로고
    • Malondialdehyde and thiobarbituric acid reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury
    • (1990) Free Radic Biol Med , vol.9 , pp. 515-540
    • Janero, D.R.1
  • 68
    • 84909844730 scopus 로고
    • Traffic of products and membranes through the Golgi complex
    • Silverstein K.S.C. (Ed.), Transport of macromolecules in cellular systems, Berlin: Dahlem Konferenzen
    • (1978) , pp. 341-362
    • Farquhar, M.G.1
  • 70
    • 0028209776 scopus 로고
    • Ischemia-induced changes in cerebral mitochondrial free fatty acids, phospholipids, and respiration in the rat
    • (1994) J Neurochem , vol.62 , pp. 1921-1928
    • Sun, D.1    Gilboe, D.D.2
  • 90
    • 0021681873 scopus 로고
    • Role of cholesterogenesis and isoprenoid synthesis in DNA replication and cell growth
    • (1984) J Lipid Res , vol.25 , pp. 1462-1468
    • Siperstein, M.D.1
  • 92
    • 0024415274 scopus 로고
    • Lipid peroxidation and cancer: a critical reconsideration
    • (1989) Tumori , vol.75 , pp. 351-357
    • Dianzani, M.U.1
  • 94
    • 0001070415 scopus 로고
    • A neutral calcium-activated protease from the soluble fraction of rat brain
    • (1984) J Biol Chem , vol.239 , pp. 149-155
    • Guroff, G.1
  • 103
    • 0001116875 scopus 로고
    • Plasticity and pathology: brain calpains as modifiers of synaptic structure
    • Mellgren R.L., Murachi T. (Eds.), Intracellular calcium-dependent proteolysis, Boca Raton: CRC Press
    • (1990) , pp. 251-264
    • Seubert, P.1    Lynch, G.2
  • 108
    • 0027215039 scopus 로고
    • Protective effects of calpain inhibitors against neuronal damage caused by cytotoxic hypoxia in vitro and ischemia in vivo
    • (1993) Brain Res , vol.609 , pp. 67-70
    • Rami, A.1    Krieglstein, J.2
  • 113
    • 0002968282 scopus 로고
    • The structure of the calpains and the calpain gene
    • Mellgren R.L., Murachi T. (Eds.), Intracellular calcium-dependent proteolysis, Boca Raton: CRC Press
    • (1990) , pp. 25-35
    • Suzuki, K.1
  • 114
    • 0002397847 scopus 로고
    • Structure-function relationships of calpastatins
    • Mellgren R.L., Murachi T. (Eds.), Intracellular calcium-dependent proteolysis, Boca Raton: CRC Press
    • (1990) , pp. 37-54
    • Maki, M.1    Hatanaka, M.2    Takano, E.3    Murachi, T.4
  • 116
    • 0003042319 scopus 로고
    • Regulation of calcium-dependent protease activity in vitro: clues for determining their physiological functions
    • Mellgren R.L., Murachi T. (Eds.), Intracellular calcium-dependent proteolysis, Boca Raton: CRC Press
    • (1990) , pp. 103-114
    • Croall, D.E.1    DeMartino, G.N.2
  • 148
    • 0025325042 scopus 로고
    • In vitro ischemia and protein synthesis in the rat hippocampal slice: the role of calcium and NMDA receptor activation
    • (1990) Brain Res , vol.515 , pp. 27-38
    • Raley-Susman, K.M.1    Lipton, P.2
  • 156
  • 157
    • 0025352294 scopus 로고
    • Differential stimulation of initiation factors eIF-4F, eIF-4B, eIF-3 and ribosomal protein S6 by insulin and phorbal esters
    • (1990) J Biol Chem , vol.265 , pp. 10611-10616
    • Morley, S.J.1    Traugh, J.A.2
  • 159
    • 0025896734 scopus 로고
    • Platelet-derived growth factor stimulates phosphorylation of the 25 kDa mRNA cap binding protein (eIF-4E) in human lung fibroblasts
    • (1991) FEBS Lett , vol.283 , pp. 219-222
    • Bu, X.1    Hagedorn, C.H.2
  • 164
    • 0032481114 scopus 로고    scopus 로고
    • Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines
    • (1998) Oncogene , vol.17 , pp. 2921-2931
    • Clemens, M.J.1    Bushell, M.2    Morley, S.J.3
  • 173
    • 0025264356 scopus 로고
    • Cap binding protein complex that restores protein synthesis in heat-shocked Erlich cell lysates contains highly phosphorylated eIF-4E
    • (1990) J Biol Chem , vol.265 , pp. 5333-5336
    • Lamphear, B.J.1    Panniers, R.2
  • 179
    • 0030021166 scopus 로고    scopus 로고
    • Internal initiation of translation directed by the 5'-untranslated region of the mRNA for eIF-4G, a factor involved in the picornovirus-induced switch from cap-dependent to internal initiation
    • (1996) J Biol Chem , vol.27 , pp. 623-626
    • Gan, W.1    Rhoads, R.E.2
  • 180
    • 0029976319 scopus 로고    scopus 로고
    • The C-terminal domain of eukaryotic protein synthesis initiation factor eIF-4G is sufficient to support cap-independent translation in the absence of eIF-4E
    • (1996) EMBO J , vol.15 , pp. 1371-1382
    • Ohlmann, T.1    Rau, M.2    Pain, V.M.3    Morley, S.J.4
  • 186
    • 0028171125 scopus 로고
    • eIF-2 kinases: regulators of general and gene-specific translation initiation
    • (1994) TIBS , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 187
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • (1993) J Biol Chem , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 191
    • 0033512306 scopus 로고    scopus 로고
    • HSP90 binds and regulates the ligand-inducible alpha subunit of eukaryotic translation initiation factor kinase GCN2
    • (1999) Mol Cell Biol , vol.19 , pp. 8422-8432
    • Donze, O.1    Picard, D.2
  • 194
    • 0027216202 scopus 로고
    • Critical evaluation of postmortem changes in human cisternal fluid. Enzymes, electrolytes, acid-base balance, glucose and glycolysis, free amino acids, and ammonia. Correlation to total brain ischemia
    • (1993) J Forensic Sci , vol.38 , pp. 603-616
    • Karkeela, J.T.1
  • 196
    • 0027171069 scopus 로고
    • Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: implications for activation of the protein kinase GCN2
    • (1993) Mol Cell Biol , vol.13 , pp. 5099-5111
    • Rolfes, R.J.1    Hinnebusch, A.G.2
  • 198
    • 0023633792 scopus 로고
    • Inhibition of rabbit reticulocyte lysate protein synthesis by heavy metal ions involves the phosphorylation of the α-subunit of the eukaryotic initiation factor 2
    • (1987) J Biol Chem , vol.262 , pp. 15939-15945
    • Hurst, R.1    Schatz, J.R.2    Matts, R.L.3
  • 202
    • 0029039746 scopus 로고
    • Mechanism of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase
    • (1995) J Virol , vol.69 , pp. 5195-5198
    • Thomas, D.C.1    Samuel, C.E.2
  • 203
    • 0029007407 scopus 로고
    • PKR: a new name and new roles
    • (1995) TIBS , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 212
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 231
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 234
    • 0028279506 scopus 로고
    • Regulation of protein phosphatase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture
    • (1994) J Biol Chem , vol.269 , pp. 12514-12520
    • Srinivasan, M.1    Begum, N.2
  • 246
    • 0030017753 scopus 로고    scopus 로고
    • A eukaryotic translation initiation factor 2-associated 67 kDa glycoprotein partially reverses protein synthesis inhibition by activated double-stranded RNA-dependent protein kinase in intact cells
    • (1996) Biochemistry , vol.35 , pp. 8275-8280
    • Rehemtulla, W.S.1    Gupta, N.K.2    Kaufman, R.J.3
  • 260
    • 0032697485 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand receptors signal NF-κB and JNK activation and apoptosis through distinct pathways
    • (1999) J Biol Chem , vol.274 , pp. 30603-30610
    • Hu, W.H.1    Johnson, H.2    Shu, H.B.3
  • 273
    • 0033575220 scopus 로고    scopus 로고
    • Apoptosis promotes a caspase-induced amino-terminal truncation of IκBα that functions as a stable inhibitor of NF-κB
    • (1999) J Biol Chem , vol.274 , pp. 20664-20670
    • Reuther, J.Y.1    Baldwin, A.S.2
  • 294
    • 0031788661 scopus 로고    scopus 로고
    • Cytochrome-c release from brain mitochondria is independent of the mitochondrial permeability transition
    • (1998) FEBS Lett , vol.439 , pp. 373-376
    • Andreyev, A.Y.1    Fiskum, G.2
  • 324
  • 325
    • 0344731406 scopus 로고    scopus 로고
    • Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-κB
    • (1999) Mol Cell Biol , vol.19 , pp. 4653-4663
    • Gil, J.1    Alcami, J.2    Esteban, M.3
  • 326
    • 0007564505 scopus 로고    scopus 로고
    • Kaufman RJ, Kumar KU, Wu S, Srivastava SP. Regulation of the double-stranded RNA-dependent protein kinase (PKR) and its role in apoptosis. Translational control. Cold Spring Harbor Laboratories, 1998:330.
  • 330
    • 0001061413 scopus 로고    scopus 로고
    • Intracellular calcium-release channels: regulators of cell life and death
    • (1997) Am J Physiol , vol.272
    • Marks, A.M.1
  • 334
    • 0027937489 scopus 로고
    • Immunophilins mediate the neuroprotective effects of FK506 in focal cerebral ischemia
    • (1994) Nature , vol.371 , pp. 336-339
    • Sharkey, J.1    Butcher, S.P.2
  • 341
    • 0027363385 scopus 로고
    • Peptidylproline cis-trans-isomerases: immunophilins
    • (1993) Eur J Biochem , vol.216 , pp. 689-707
    • Galat, A.1
  • 342
  • 358
    • 0025267015 scopus 로고
    • The regulation and function of c-fos and other immediate early genes in the nervous system
    • (1990) Neuron , vol.4 , pp. 477-485
    • Sheng, M.1    Greenberg, M.E.2
  • 368
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock proteins and glucose regulated proteins
    • (1986) Cell , vol.46 , pp. 959-969
    • Pelham, H.R.B.1
  • 370
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 377
    • 0022243905 scopus 로고
    • Synthesis of a stress protein following transient ischemia in the gerbil
    • (1985) J Neurochem , vol.45 , pp. 1635-1641
    • Nowak T.S., Jr.1
  • 391
    • 0007481674 scopus 로고    scopus 로고
    • The control of cell proliferation. In: Watson JD, Hopkins NH, Roberts JW, Stietz JA, Weiner AM, editors. Molecular biology of the gene. 4th ed. Menlo Park, CA: Benjamin/Cummings, 1987:962-92.
  • 393
    • 0025165823 scopus 로고
    • Proliferation and differentiation of neuronal stem cells regulated by nerve growth factor
    • (1990) Nature , vol.347 , pp. 762-765
    • Cattaneo, E.1    McKay, R.2
  • 394
    • 0018090354 scopus 로고
    • Insulin receptors are widely distributed in the central nervous system of the rat
    • (1978) Nature , vol.272 , pp. 827-829
    • Havarankova, J.1    Roth, J.2
  • 398
    • 0026334402 scopus 로고
    • NGF and β-FGF protect rat hippocampal and human cortical neurons against hypoglycemic damage by stabilizing calcium homeostasis
    • (1991) Neuron , vol.7 , pp. 1031-1041
    • Cheng, B.1    Mattson, M.P.2
  • 404
    • 0025937732 scopus 로고
    • Regulation and physiological function of insulin-like growth factors in the central nervous system
    • (1991) Adv Exp Med Biol , vol.293 , pp. 419-430
    • Lauterio, T.J.1
  • 413
    • 0025732785 scopus 로고
    • Post-ischemic seizures and necrotizing ischemic brain damage: neuroprotective effect of post-ischemic diazepam and insulin
    • (1991) Neurology , vol.41 , pp. 423-428
    • Voll, C.L.1    Auer, R.N.2
  • 441
    • 0034708456 scopus 로고    scopus 로고
    • The Ras/phosphatidylinositol 3-kinase and Ras/ERK pathways function as independent survival modules each of which inhibits a distinct apoptotic signaling pathway in sympathetic neurons
    • (2000) J Biol Chem , vol.275 , pp. 8817-8824
    • Xue, L.1    Murray, J.H.2    Tolkovsky, A.M.3
  • 443
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologs Akt1 and Akt2: amplification of Akt1 in a primary human gastric adenocarcinoma
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 449
    • 0030013326 scopus 로고    scopus 로고
    • Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-1 phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase
    • (1996) Mol Cell Biol , vol.16 , pp. 2857-2864
    • Mendez, R.1    Myers, M.G.2    White, M.F.3    Rhoads, R.E.4
  • 451
    • 0039002254 scopus 로고    scopus 로고
    • Two different signal transduction pathways are implicated in the regulation of initiation factor 2B activity in insulin-like growth factor-1-stimulated neuronal cells
    • (2000) J Biol Chem , vol.275 , pp. 19192-19197
    • Quevedo, C.1    Alcazar, A.2    Salinas, M.3


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