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Volumn 56, Issue 6, 1999, Pages 620-631

PC12 and neuro 2a cells have different susceptibilities to acetylcholinesterase-amyloid complexes, amyloid25-35 fragment, glutamate, and hydrogen peroxide

Author keywords

A amyloid; Acetylcholinesterase; Glutathione; Neuro 2a; Oxidative stress; PC12

Indexed keywords

17ALPHA ESTRADIOL; ACETYLCHOLINESTERASE; AMYLOID; ESTRADIOL; GLUTAMIC ACID; GLUTATHIONE; HYDROGEN PEROXIDE; LACTATE DEHYDROGENASE; PEPTIDE FRAGMENT; REACTIVE OXYGEN METABOLITE; TRITON X 100;

EID: 0033564579     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(19990615)56:6<620::AID-JNR8>3.0.CO;2-F     Document Type: Article
Times cited : (62)

References (68)
  • 1
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-β-peptide fragments by forming a complex with growing fibrils
    • Alvarez A, Opazo C, Alarcón R, Garrido J, Inestrosa NC. 1997. Acetylcholinesterase promotes the aggregation of amyloid-β-peptide fragments by forming a complex with growing fibrils. J Mol Biol 272:348-361.
    • (1997) J Mol Biol , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcón, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 3
    • 0030728765 scopus 로고    scopus 로고
    • Amyloid β-protein toxicity and oxidative stress in Alzheimer's disease
    • Behl C. 1997. Amyloid β-protein toxicity and oxidative stress in Alzheimer's disease. (Review). Cell Tissue Res 290:471-480.
    • (1997) Cell Tissue Res , vol.290 , pp. 471-480
    • Behl, C.1
  • 4
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. 1994. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 6
    • 0028971169 scopus 로고
    • 17β Estradiol protects neurons from oxidative stress-induced cell death in vitro
    • Behl C, Widmann M, Trapp T, Holsboer F. 1995. 17β Estradiol protects neurons from oxidative stress-induced cell death in vitro. Biochem Biophys Res Commun 216:473-482.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 473-482
    • Behl, C.1    Widmann, M.2    Trapp, T.3    Holsboer, F.4
  • 7
    • 0344492699 scopus 로고    scopus 로고
    • Estrogen protects neuronal cells against the cytotoxicity of the acetylcholinesterase-amyloid-β-peptide complexes
    • Bonnefont A, Muñoz FJ, Inestrosa NC. 1998. Estrogen protects neuronal cells against the cytotoxicity of the acetylcholinesterase-amyloid-β-peptide complexes. FEBS Lett 441:220-224.
    • (1998) FEBS Lett , vol.441 , pp. 220-224
    • Bonnefont, A.1    Muñoz, F.J.2    Inestrosa, N.C.3
  • 8
    • 0026011175 scopus 로고
    • Increased excitotoxic vulnerability of cortical cultures of with reduced levels of glutathione
    • Bridges RJ, Koh J-Y, Hatalsky CG, Cotman CW. 1991. Increased excitotoxic vulnerability of cortical cultures of with reduced levels of glutathione. Eur J Pharmacol 192:199-200.
    • (1991) Eur J Pharmacol , vol.192 , pp. 199-200
    • Bridges, R.J.1    Koh, J.-Y.2    Hatalsky, C.G.3    Cotman, C.W.4
  • 9
    • 0030061861 scopus 로고    scopus 로고
    • Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments
    • Bronfman FC, Soto C, Tapia L, Tapia V, Inestrosa NC. 1996. Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments. J Cell Physiol 166:360-366.
    • (1996) J Cell Physiol , vol.166 , pp. 360-366
    • Bronfman, F.C.1    Soto, C.2    Tapia, L.3    Tapia, V.4    Inestrosa, N.C.5
  • 11
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P. 1993. Oxidative stress, glutamate, and neurodegenerative disorders. Science 262:689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 16
    • 0030927533 scopus 로고    scopus 로고
    • Role of glutathione metabolism in the glutamate induced programmed cell death of neuronal-like PC12 cells
    • Froissard P, Monrocq H, Duval D. 1997. Role of glutathione metabolism in the glutamate induced programmed cell death of neuronal-like PC12 cells. Eur J Pharmacol 12:93-99.
    • (1997) Eur J Pharmacol , vol.12 , pp. 93-99
    • Froissard, P.1    Monrocq, H.2    Duval, D.3
  • 17
    • 0029924284 scopus 로고    scopus 로고
    • Estrogens attenuate and corticosterone exacerbates excitotoxicity, oxidative injury, and amyloid β-peptide toxicity in hippocampal neurons
    • Goodman Y, Bruce AJ, Cheng B, Mattson MP. 1996. Estrogens attenuate and corticosterone exacerbates excitotoxicity, oxidative injury, and amyloid β-peptide toxicity in hippocampal neurons. J Neurochem 66:1836-1844
    • (1996) J Neurochem , vol.66 , pp. 1836-1844
    • Goodman, Y.1    Bruce, A.J.2    Cheng, B.3    Mattson, M.P.4
  • 18
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • Goodman Y, Mattson MP. 1994. Secreted forms of β-amyloid precursor protein hippocampal neurons against amyloid β-peptide-induced oxidative injury. Exp Neurol 128:1-12.
    • (1994) Exp Neurol , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 19
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene LA, Tischler AS. 1976. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc Natl Acad Sci USA 73:2424-2428.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 20
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. 1992. Reactive oxygen species and the central nervous system. J Neurochem. 59:1609-1623.
    • (1992) J Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 21
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris ME, Hensley K, Butterfield DA, Leedle RA, Carney JM. 1995. Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp Neurol 131:193-202.
    • (1995) Exp Neurol , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 22
    • 0030054709 scopus 로고    scopus 로고
    • Generation of reactive oxygen intermediates after treatment of blasts of acute myeloblastic leukemia with cytosine arabinoside: Role of bcl-2
    • Hedley DW, McCulloch EA. 1996. Generation of reactive oxygen intermediates after treatment of blasts of acute myeloblastic leukemia with cytosine arabinoside: role of bcl-2. Leukemia 10:1143-1149.
    • (1996) Leukemia , vol.10 , pp. 1143-1149
    • Hedley, D.W.1    McCulloch, E.A.2
  • 23
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa NC, Alvarez A, Pérez CA, Moreno RD, Vicente M, Linker C, Casanueva OI, Soto C, Garrido J. 1996. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16:881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 24
    • 0032420997 scopus 로고    scopus 로고
    • Cellular and molecular basis of estrogen's neuroprotection: Potential relevance to Alzheimer's disease
    • Inestrosa NC, Marzolo MP, Bonnefont AB. 1998. Cellular and molecular basis of estrogen's neuroprotection: potential relevance to Alzheimer's disease. Mol Neurobiol 17:73-86.
    • (1998) Mol Neurobiol , vol.17 , pp. 73-86
    • Inestrosa, N.C.1    Marzolo, M.P.2    Bonnefont, A.B.3
  • 25
    • 0019782643 scopus 로고
    • Cellular localization of the molecular forms of acetylcholinesterase in rat pheochromocytoma PC12 cells treated with nerve growth factor
    • Inestrosa NC, Reiness CG, Reichardt LF, Hall ZW. 1981. Cellular localization of the molecular forms of acetylcholinesterase in rat pheochromocytoma PC12 cells treated with nerve growth factor. J Neurosci 1:1260-1267.
    • (1981) J Neurosci , vol.1 , pp. 1260-1267
    • Inestrosa, N.C.1    Reiness, C.G.2    Reichardt, L.F.3    Hall, Z.W.4
  • 26
    • 0023219731 scopus 로고
    • Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues
    • Inestrosa NC, Roberts WL, Marshall TL, Rosenberry TL. 1987. Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues. J Biol Chem 262:4441-4444.
    • (1987) J Biol Chem , vol.262 , pp. 4441-4444
    • Inestrosa, N.C.1    Roberts, W.L.2    Marshall, T.L.3    Rosenberry, T.L.4
  • 27
    • 0025240761 scopus 로고
    • Role of nerve growth factor in oxidant-antioxidant balance and neuronal injury. I. Stimulation of hydrogen peroxide resistance
    • Jackson GR, Apffel L, Werrbach-Perez K, Perez-Polo JR. 1990. Role of nerve growth factor in oxidant-antioxidant balance and neuronal injury. I. Stimulation of hydrogen peroxide resistance. J Neurosci Res 25:360-368.
    • (1990) J Neurosci Res , vol.25 , pp. 360-368
    • Jackson, G.R.1    Apffel, L.2    Werrbach-Perez, K.3    Perez-Polo, J.R.4
  • 29
    • 0002064084 scopus 로고
    • Neuroblastoma: Cell culture analyses of a differentiated stem cell system
    • Klebe RJ, Ruddle FH. 1969. Neuroblastoma: cell culture analyses of a differentiated stem cell system. J Cell Biol 43:69a.
    • (1969) J Cell Biol , vol.43
    • Klebe, R.J.1    Ruddle, F.H.2
  • 30
    • 0023221068 scopus 로고
    • Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay
    • Koh JY, Choi DW. 1987. Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay. J Neurosci Methods 20:83-90.
    • (1987) J Neurosci Methods , vol.20 , pp. 83-90
    • Koh, J.Y.1    Choi, D.W.2
  • 31
    • 0030986669 scopus 로고    scopus 로고
    • Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis
    • Kruman I, Bruce-Keller AJ, Bredesen D, Waeg G, Mattson MP. 1997. Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis. J Neurosci 17:5089-100.
    • (1997) J Neurosci , vol.17 , pp. 5089-5100
    • Kruman, I.1    Bruce-Keller, A.J.2    Bredesen, D.3    Waeg, G.4    Mattson, M.P.5
  • 33
    • 0027221998 scopus 로고
    • NMDA-dependent superoxide production and neurotoxicity
    • Lafon-Cazal M, Pietri S, Culcasi M, Bockaert J. 1993. NMDA-dependent superoxide production and neurotoxicity. Nature 364:535-537.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 34
    • 0028982274 scopus 로고
    • P21 ras as a common signaling target of reactive free radicals and cellular redox stress
    • Lander HM, Ogiste JS, Teng KK, Novogrodsky A. 1995. p21 ras as a common signaling target of reactive free radicals and cellular redox stress. J Biol Chem 270:21195-21198.
    • (1995) J Biol Chem , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4
  • 35
    • 0030859290 scopus 로고    scopus 로고
    • Activation of the receptor for advanced glycation end products triggers a p21 (ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress
    • Lander HM, Tauras JM, Ogiste JS, Hori O, Moss RA, Schmidt AM. 1997. Activation of the receptor for advanced glycation end products triggers a p21 (ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress. J Biol Chem 272:17810-17814.
    • (1997) J Biol Chem , vol.272 , pp. 17810-17814
    • Lander, H.M.1    Tauras, J.M.2    Ogiste, J.S.3    Hori, O.4    Moss, R.A.5    Schmidt, A.M.6
  • 36
    • 0031882875 scopus 로고    scopus 로고
    • Glutathione depletion exacerbates impairment by oxidative stress of phosphoinositide hydrolysis, AP-1, and NF-kappa B activation by cholinergic stimulation
    • Li X, Song L, Jope RS. 1998. Glutathione depletion exacerbates impairment by oxidative stress of phosphoinositide hydrolysis, AP-1, and NF-kappa B activation by cholinergic stimulation. Brain Res Mol Brain Res 53:196-205.
    • (1998) Brain Res Mol Brain Res , vol.53 , pp. 196-205
    • Li, X.1    Song, L.2    Jope, R.S.3
  • 37
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y, Peterson DA, Kimura H, Schubert D. 1997. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J Neurochem 69:581-593.
    • (1997) J Neurochem , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 38
    • 0030695856 scopus 로고    scopus 로고
    • Cytotoxic amyloid peptides inhibit cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis
    • Liu Y, Schubert D. 1997. Cytotoxic amyloid peptides inhibit cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis. J Neurochem 69:2285-2293.
    • (1997) J Neurochem , vol.69 , pp. 2285-2293
    • Liu, Y.1    Schubert, D.2
  • 40
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide
    • Mark RJ, Lovell MA, Markesbery WR, Uchida K, Mattson MP. 1997. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide. J Neurochem 68:255-264.
    • (1997) J Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 41
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • Markesbery WR. 1997. Oxidative stress in Alzheimer's disease. Free Rad Biol Med 23:134-147.
    • (1997) Free Rad Biol Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 42
    • 0002641558 scopus 로고    scopus 로고
    • Central role of oxyradicals in the mechanism of amyloid β-peptide cytotoxicity
    • Mattson MP. 1997a. Central role of oxyradicals in the mechanism of amyloid β-peptide cytotoxicity. Alzheimers Dis Rev 2:1-14.
    • (1997) Alzheimers Dis Rev , vol.2 , pp. 1-14
    • Mattson, M.P.1
  • 43
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson MP. 1997b. Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 77:1081-1132.
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 44
    • 0029150526 scopus 로고
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons. J Neurochem 65:1740-1751.
    • (1995) J Neurochem , vol.65 , pp. 1740-1751
    • Mattson, M.P.1    Lovell, M.A.2    Furukawa, K.3    Markesbery, W.R.4
  • 45
    • 0031465727 scopus 로고    scopus 로고
    • Estrogens stabilize mitochondrial function and protect neural cells against the pro-apoptotic action of mutant presenilin-1
    • Mattson MP, Robinson N, Guo Q. 1997. Estrogens stabilize mitochondrial function and protect neural cells against the pro-apoptotic action of mutant presenilin-1. NeuroReport 8:3817-3821.
    • (1997) Neuroreport , vol.8 , pp. 3817-3821
    • Mattson, M.P.1    Robinson, N.2    Guo, Q.3
  • 46
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. 1988. Glutathione metabolism and its selective modification. J Biol Chem 263:17205-17208.
    • (1988) J Biol Chem , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 47
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxic assays
    • Mosmann T. 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxic assays. J Immunol Methods 65:55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 48
    • 0024678458 scopus 로고
    • Glutamate toxicity in a neural cell line involves inhibition of cystine transport leading to oxidative stress
    • Murphy TH, Miyamoto M, Sastre A, Schnaar RL, Coyle JT. 1989. Glutamate toxicity in a neural cell line involves inhibition of cystine transport leading to oxidative stress. Neuron 2:1547-1558.
    • (1989) Neuron , vol.2 , pp. 1547-1558
    • Murphy, T.H.1    Miyamoto, M.2    Sastre, A.3    Schnaar, R.L.4    Coyle, J.T.5
  • 49
    • 0027496238 scopus 로고
    • A radical hypothesis for neurodegeneration
    • Olanow CW. 1993. A Radical hypothesis for neurodegeneration. Trends Neurosci 16:439-444.
    • (1993) Trends Neurosci , vol.16 , pp. 439-444
    • Olanow, C.W.1
  • 50
    • 0027424797 scopus 로고
    • Role of nerve growth factor in oxidant homeostasis: Glutathione metabolism
    • Pan Z, Perez-Polo R. 1993. Role of nerve growth factor in oxidant homeostasis: glutathione metabolism. J Neurochem 61:1713-1721.
    • (1993) J Neurochem , vol.61 , pp. 1713-1721
    • Pan, Z.1    Perez-Polo, R.2
  • 51
    • 0030592834 scopus 로고    scopus 로고
    • Increased uptake of L-cysteine and L-cystine by nerve growth factor in rat pheochromocytoma cells
    • Pan Z, Perez-Polo R. 1996. Increased uptake of L-cysteine and L-cystine by nerve growth factor in rat pheochromocytoma cells. Brain Res 740:21-26.
    • (1996) Brain Res , vol.740 , pp. 21-26
    • Pan, Z.1    Perez-Polo, R.2
  • 52
    • 0030757990 scopus 로고    scopus 로고
    • Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress
    • Pereira CM, Oliveira CR. 1997. Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress. Free Rad Biol Med 23:637-647.
    • (1997) Free Rad Biol Med , vol.23 , pp. 637-647
    • Pereira, C.M.1    Oliveira, C.R.2
  • 53
    • 0025885501 scopus 로고
    • Mechanism of cell death
    • Timiras PS, Giacobini E, Vernadakis A, editors. New York: Plenum
    • Perez-Polo R. 1991. Mechanism of cell death. In: Timiras PS, Giacobini E, Vernadakis A, editors. Plasticity and regeneration of the nervous system. New York: Plenum. p 345-352.
    • (1991) Plasticity and Regeneration of the Nervous System , pp. 345-352
    • Perez-Polo, R.1
  • 55
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, Cotman CW. 1995. Structure-activity analyses of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity. J Neurochem 64:253-265.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 56
    • 0016687593 scopus 로고
    • Differentiation of neuroblastoma cells in culture
    • Prasad KN. 1975. Differentiation of neuroblastoma cells in culture. Biol Rev 50:129-265.
    • (1975) Biol Rev , vol.50 , pp. 129-265
    • Prasad, K.N.1
  • 57
    • 0021240616 scopus 로고
    • Glutathione depletion and susceptibility
    • Reed DJ, Fariss MW. 1984. Glutathione depletion and susceptibility. Pharmacol Rev 36 Suppl. 25S-33S.
    • (1984) Pharmacol Rev , vol.36 , Issue.SUPPL.
    • Reed, D.J.1    Fariss, M.W.2
  • 59
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzyme activity in amyloid βprotein-resistant cells
    • Sagara Y, Dargush R, Klier FG, Schubert D, Behl C. 1996. Increased antioxidant enzyme activity in amyloid βprotein-resistant cells. J Neurosci 16:497-505.
    • (1996) J Neurosci , vol.16 , pp. 497-505
    • Sagara, Y.1    Dargush, R.2    Klier, F.G.3    Schubert, D.4    Behl, C.5
  • 61
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman MS, Ragan CI, Iversen LL. 1994. Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc Natl Acad Sci USA 91:1470-1474.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 62
    • 0001912805 scopus 로고    scopus 로고
    • Is Alzheimer's a disease of oxidative stress?
    • Smith MA, Sayre L, Perry G. 1996. Is Alzheimer's a disease of oxidative stress? Alzheimers Dis Rev 1:63-67.
    • (1996) Alzheimers Dis Rev , vol.1 , pp. 63-67
    • Smith, M.A.1    Sayre, L.2    Perry, G.3
  • 63
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid β-peptide
    • Soto C, Brañes MC, Alvarez J, Inestrosa NC. 1994. Structural determinants of the Alzheimer's amyloid β-peptide. J Neurochem 63:1191-1198.
    • (1994) J Neurochem , vol.63 , pp. 1191-1198
    • Soto, C.1    Brañes, M.C.2    Alvarez, J.3    Inestrosa, N.C.4
  • 64
    • 0026056595 scopus 로고
    • Glutathione dependent metabolism and detoxification of 4-hydroxy-2-nonenal
    • Spitz DR, Sullivan SJ, Malcolm RR, Roberts RJ. 1991. Glutathione dependent metabolism and detoxification of 4-hydroxy-2-nonenal. Free Rad Biol Med 11:415-423.
    • (1991) Free Rad Biol Med , vol.11 , pp. 415-423
    • Spitz, D.R.1    Sullivan, S.J.2    Malcolm, R.R.3    Roberts, R.J.4
  • 65
    • 0014481378 scopus 로고
    • Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Application to mammalian blood and other tissues
    • Tietze F. 1969. Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione: application to mammalian blood and other tissues. Anal Biochem 27:502-522.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 67
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirshner DA. 1990. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250:279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirshner, D.A.3
  • 68
    • 0027232517 scopus 로고
    • Basic FGF, NGF, and IGFs protect hippocampal neurons against iron-induced degeneration
    • Zhang Y, Tatsuno T, Carney J, Mattson MP. 1993. Basic FGF, NGF, and IGFs protect hippocampal neurons against iron-induced degeneration. J Cereb Blood Flow Metab 13:378-388.
    • (1993) J Cereb Blood Flow Metab , vol.13 , pp. 378-388
    • Zhang, Y.1    Tatsuno, T.2    Carney, J.3    Mattson, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.