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Volumn 69, Issue 1, 1997, Pages 273-284

Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β- peptide: Role of the lipid peroxidation product 4-hydroxynonenal

Author keywords

Alzheimer's disease; ATP; Cerebral cortex; Excitotoxicity; Malondialdehyde; Mitochondrial respiration; Superoxide anion radical; Synaptic metabolism

Indexed keywords

4 HYDROXYNONENAL; AMYLOID BETA PROTEIN; GLUCOSE; GLUTAMIC ACID;

EID: 0030966546     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69010273.x     Document Type: Article
Times cited : (430)

References (111)
  • 1
    • 0027280338 scopus 로고
    • Pathological implications of nitric oxide, superoxide and peroxynitrite formation
    • Beckman J. S. and Crow J. P. (1993) Pathological implications of nitric oxide, superoxide and peroxynitrite formation. Biochem. Soc. Trans. 21, 330-334.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 330-334
    • Beckman, J.S.1    Crow, J.P.2
  • 2
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J. B., Lesley R., and 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
  • 3
    • 0024423656 scopus 로고
    • NMDA and non-NMDA receptors are co-localized at individual excitatory synapses in cultured rat hippocampus
    • Bekkers J. and Stevens C. (1989) NMDA and non-NMDA receptors are co-localized at individual excitatory synapses in cultured rat hippocampus. Nature 341, 230-233.
    • (1989) Nature , vol.341 , pp. 230-233
    • Bekkers, J.1    Stevens, C.2
  • 4
    • 0029145084 scopus 로고
    • Are reactive oxygen species involved in Alzheimer's disease?
    • Benzi G. and Moretti A. (1995) Are reactive oxygen species involved in Alzheimer's disease? Neurobiol. Aging 16, 661-674.
    • (1995) Neurobiol. Aging , vol.16 , pp. 661-674
    • Benzi, G.1    Moretti, A.2
  • 5
    • 1842289775 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a product of lipid peroxidation, impairs signal transduction of metabotropic glutamate receptors in hippocampal neurons
    • Blanc E. M., Kelly J. F., Mark R. J., and Mattson M. P. (1996) 4-Hydroxynonenal, a product of lipid peroxidation, impairs signal transduction of metabotropic glutamate receptors in hippocampal neurons. Soc. Neurosci. Abstr. 22, 809.
    • (1996) Soc. Neurosci. Abstr. , vol.22 , pp. 809
    • Blanc, E.M.1    Kelly, J.F.2    Mark, R.J.3    Mattson, M.P.4
  • 6
    • 0027426832 scopus 로고
    • Metabolic alterations common to neural and non-neural cells in Alzheimer's disease
    • Blass J. P. (1993) Metabolic alterations common to neural and non-neural cells in Alzheimer's disease. Hippocampus 3, 45-54.
    • (1993) Hippocampus , vol.3 , pp. 45-54
    • Blass, J.P.1
  • 7
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 8
    • 0029684403 scopus 로고    scopus 로고
    • Genetic control of neural cell apoptosis
    • Bredesen D. E. (1996) Genetic control of neural cell apoptosis. Perspect. Dev. Neurobiol. 3, 101-109.
    • (1996) Perspect. Dev. Neurobiol. , vol.3 , pp. 101-109
    • Bredesen, D.E.1
  • 9
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • Brown R. H. Jr. (1995) Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 80, 687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown Jr., R.H.1
  • 10
    • 0028986916 scopus 로고
    • β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., and Yankner B. A. (1995) β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 11
    • 0028178837 scopus 로고
    • β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D. A., Hensley K., Harris M., Mattson M. P., and Carney J. (1994) β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200, 710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.P.4    Carney, J.5
  • 12
    • 0027526419 scopus 로고
    • Release of excess amyloid β protein from a mutant amyloid β protein precursor
    • Cai X.-D., Golde T. E., and Younkin S. G. (1993) Release of excess amyloid β protein from a mutant amyloid β protein precursor. Science 259, 514-516.
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.G.3
  • 13
    • 0026521942 scopus 로고
    • IGF-I and IGF-II protect cultured hippocampal and septal neurons against calcium-mediated hypoglycemic damage
    • Cheng B. and Mattson M. P. (1992) IGF-I and IGF-II protect cultured hippocampal and septal neurons against calcium-mediated hypoglycemic damage. J. Neurosci. 12, 1558-1566.
    • (1992) J. Neurosci. , vol.12 , pp. 1558-1566
    • Cheng, B.1    Mattson, M.P.2
  • 15
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman C. W. and Anderson A. J. (1995) A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol. Neurobiol. 10, 19-45.
    • (1995) Mol. Neurobiol. , vol.10 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 16
    • 0028972701 scopus 로고
    • Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity
    • Cummings B. J. and Cotman C. W. (1995) Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity. Lancet 346, 1524-1528.
    • (1995) Lancet , vol.346 , pp. 1524-1528
    • Cummings, B.J.1    Cotman, C.W.2
  • 17
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky S. and Scheff S. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol. 27, 457-464.
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • DeKosky, S.1    Scheff, S.2
  • 20
    • 0026730350 scopus 로고
    • Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks T., Dyrks E., Hartmann T., Masters C., and Beyreuther K. E. (1992) Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J. Biol. Chem. 267, 18210-18217.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, T.3    Masters, C.4    Beyreuther, K.E.5
  • 21
  • 22
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R. J., and Zollner H. (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11, 81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 23
    • 0026498085 scopus 로고
    • Evidence for a concerted reaction between lipid hydroperoxides and polypeptides
    • Freuebis J., Parthasarathy S., and Steinberg D. (1992) Evidence for a concerted reaction between lipid hydroperoxides and polypeptides. Proc. Natl. Acad. Sci. USA 89, 10588-10592.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10588-10592
    • Freuebis, J.1    Parthasarathy, S.2    Steinberg, D.3
  • 24
    • 0027990369 scopus 로고
    • Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal
    • Friguet B., Stadman E. R., and Szweda L. I. (1994) Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. J. Biol. Chem. 269, 21639-21643.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21639-21643
    • Friguet, B.1    Stadman, E.R.2    Szweda, L.I.3
  • 26
    • 0026607033 scopus 로고
    • Synaptosomal plasma and mitochondrial membrane potentials during anoxia
    • Gibson G. E., Nielsen P., and Toral-Barza L. (1992) Synaptosomal plasma and mitochondrial membrane potentials during anoxia. Neurosci. Lett. 138, 133-136.
    • (1992) Neurosci. Lett. , vol.138 , pp. 133-136
    • Gibson, G.E.1    Nielsen, P.2    Toral-Barza, L.3
  • 27
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • Goodman Y. and Mattson M. P. (1994) Secreted forms of β-amyloid precursor protein protect 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
  • 28
    • 0030026613 scopus 로고    scopus 로고
    • Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid β-peptide toxicity
    • Goodman Y. and Mattson M. P. (1996) Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid β-peptide toxicity. J. Neurochem. 66, 869-872.
    • (1996) J. Neurochem. , vol.66 , pp. 869-872
    • Goodman, Y.1    Mattson, M.P.2
  • 29
    • 0027959041 scopus 로고
    • Nordihydroguaiaretic acid protects hippocampal neurons against amyloid β-peptide toxicity, and attenuates free radical and calcium accumulation
    • Goodman Y., Steiner M. R., Steiner S. M., and Mattson M. P. (1994) Nordihydroguaiaretic acid protects hippocampal neurons against amyloid β-peptide toxicity, and attenuates free radical and calcium accumulation. Brain Res. 654, 171-176.
    • (1994) Brain Res. , vol.654 , pp. 171-176
    • Goodman, Y.1    Steiner, M.R.2    Steiner, S.M.3    Mattson, M.P.4
  • 30
    • 0029924284 scopus 로고    scopus 로고
    • Estrogens attenuate and corticosterone exacerbates excitotoxicity, oxidative injury, and amyloid β-peptide toxicity in hippocampal neurons
    • Goodman Y., Bruce A. J., Cheng B., and Mattson M. P. (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
  • 31
    • 0024363934 scopus 로고
    • Excitatory amino acids and Alzheimer's disease
    • Greenamyre J. T. and Young A. B. (1989) Excitatory amino acids and Alzheimer's disease. Neurobiol. Aging 10, 593-602.
    • (1989) Neurobiol. Aging , vol.10 , pp. 593-602
    • Greenamyre, J.T.1    Young, A.B.2
  • 32
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's beta-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris M. E., Hensley K., Butterfield D. A., Leedle R. A., and Carney J. M. (1995) Direct evidence of oxidative injury produced by the Alzheimer's beta-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
  • 33
    • 0027430156 scopus 로고
    • Dihydrorhodamine 123: A fluorescent probe for superoxide generation?
    • Henderson L. and Chappell J. B. (1993) Dihydrorhodamine 123: a fluorescent probe for superoxide generation? Eur. J. Biochem. 217, 273-280.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 273-280
    • Henderson, L.1    Chappell, J.B.2
  • 34
    • 0028180518 scopus 로고
    • A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer's disease
    • Hensley K., Carney J. M., Mattson M. P., Aksenova M., Harris M., Wu J. F., Floyd R., and Butterfield D. A. (1994) A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer's disease. Proc. Natl Acad. Sci. USA 91, 3270-3274.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.4    Harris, M.5    Wu, J.F.6    Floyd, R.7    Butterfield, D.A.8
  • 35
    • 0028985210 scopus 로고
    • Amyloid β-peptide spin trapping. I. Peptide enzyme toxicity is related to free radical spin trap reactivity
    • Hensley K., Aksenova M., Carney J. M., Harris M., and Butterfield D. A. (1995) Amyloid β-peptide spin trapping. I. Peptide enzyme toxicity is related to free radical spin trap reactivity. Neuroreport 6, 489-492.
    • (1995) Neuroreport , vol.6 , pp. 489-492
    • Hensley, K.1    Aksenova, M.2    Carney, J.M.3    Harris, M.4    Butterfield, D.A.5
  • 36
    • 0026408618 scopus 로고
    • Abnormalities of glucose metabolism in Alzheimer's disease
    • Hoyer S. (1991) Abnormalities of glucose metabolism in Alzheimer's disease. Ann. NY Acad. Sci. 640, 53-58.
    • (1991) Ann. NY Acad. Sci. , vol.640 , pp. 53-58
    • Hoyer, S.1
  • 39
    • 84855303577 scopus 로고
    • Oxygen free radicals and brain dysfunction
    • Jesberger J. A. and Richardson J. S. (1991) Oxygen free radicals and brain dysfunction. Int. J. Neurosci. 5, 1-17.
    • (1991) Int. J. Neurosci. , vol.5 , pp. 1-17
    • Jesberger, J.A.1    Richardson, J.S.2
  • 40
    • 0022633583 scopus 로고
    • Modification of human low-density lipoprotein by the lipid peroxidation product 4-hydroxynonenal
    • Jurgens G., Lang J., and Esterbauer H. (1986) Modification of human low-density lipoprotein by the lipid peroxidation product 4-hydroxynonenal. Biochim. Biophys. Acta 875, 103-114.
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 103-114
    • Jurgens, G.1    Lang, J.2    Esterbauer, H.3
  • 41
    • 0027519515 scopus 로고
    • Atherogenic lipoproteins in man: Immunostaining of human autopsy aorta with antibodies to modified apolipoprotein B and apolipoprotein A
    • Jurgens G., Chen Q., Esterbauer H., Mair S., Ledinski G., and Dinges H. P. (1993) Atherogenic lipoproteins in man: immunostaining of human autopsy aorta with antibodies to modified apolipoprotein B and apolipoprotein A. Arterioscler. Thromb. 13, 1689-1699.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1689-1699
    • Jurgens, G.1    Chen, Q.2    Esterbauer, H.3    Mair, S.4    Ledinski, G.5    Dinges, H.P.6
  • 42
    • 0024419325 scopus 로고
    • Reduced glucose transporter at the blood-brain barrier and in cerebral cortex in Alzheimer's disease
    • Kalaria R. N. and Harik S. I. (1989) Reduced glucose transporter at the blood-brain barrier and in cerebral cortex in Alzheimer's disease. J. Neurochem. 53, 1083-1088.
    • (1989) J. Neurochem. , vol.53 , pp. 1083-1088
    • Kalaria, R.N.1    Harik, S.I.2
  • 43
    • 1842290363 scopus 로고    scopus 로고
    • Amyloid β-peptide and LPA disrupt calcium homeostasis, and induce oxyradical production and mitochondrial dysfunction in synapses
    • Keller J., Steiner S. M., and Mattson M. P. (1996) Amyloid β-peptide and LPA disrupt calcium homeostasis, and induce oxyradical production and mitochondrial dysfunction in synapses. Soc. Neurosci. Abstr. 22, 2115.
    • (1996) Soc. Neurosci. Abstr. , vol.22 , pp. 2115
    • Keller, J.1    Steiner, S.M.2    Mattson, M.P.3
  • 46
    • 0025110182 scopus 로고
    • β-Amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage
    • Koh J.-Y., Yang L. L., and Cotman C. W. (1990) β-Amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage. Brain Res. 533, 315-320.
    • (1990) Brain Res. , vol.533 , pp. 315-320
    • Koh, J.-Y.1    Yang, L.L.2    Cotman, C.W.3
  • 49
    • 0029866196 scopus 로고    scopus 로고
    • 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition
    • Kristal B. S., Park B. K., and Yu B. P. (1996) 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition. J. Biol. Chem. 271, 6033-6038.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6033-6038
    • Kristal, B.S.1    Park, B.K.2    Yu, B.P.3
  • 50
    • 0021943367 scopus 로고
    • Reduced calcium uptake by rat brain mitochondria and synaptosomes in response to aging
    • Leslie S. W., Chandler L. J., Barr E. M., and Farrar R. P. (1985) Reduced calcium uptake by rat brain mitochondria and synaptosomes in response to aging. Brain Res. 329, 177-183.
    • (1985) Brain Res. , vol.329 , pp. 177-183
    • Leslie, S.W.1    Chandler, L.J.2    Barr, E.M.3    Farrar, R.P.4
  • 52
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Lovell M. A., Ehmann W. D., Butler S. M., and Markesbery W. R. (1995) Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurology 45, 1594-1601.
    • (1995) Neurology , vol.45 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 54
    • 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 R. J., Lovell M. A., Markesbery W. R., Uchida K., and Mattson M. P. (1997a) 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
  • 55
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose uptake in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R. J., Pang Z., Geddes J. W., Uchida K., and Mattson M. P. (19976) Amyloid β-peptide impairs glucose uptake in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci. 17, 1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 56
    • 0025273543 scopus 로고
    • Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and calcium influx in cultured hippocampal neurons
    • Mattson M. P. (1990) Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and calcium influx in cultured hippocampal neurons. Neuron 4, 105-117.
    • (1990) Neuron , vol.4 , pp. 105-117
    • Mattson, M.P.1
  • 57
    • 0029973120 scopus 로고    scopus 로고
    • Programmed cell life: Anti-apoptotic signaling and therapeutic strategies in neurodegenerative disorders
    • Mattson M. P. and Furukawa K. (1996) Programmed cell life: anti-apoptotic signaling and therapeutic strategies in neurodegenerative disorders. Restorative Neurol. Neurosci. 9, 191-205.
    • (1996) Restorative Neurol. Neurosci. , vol.9 , pp. 191-205
    • Mattson, M.P.1    Furukawa, K.2
  • 58
    • 0023931488 scopus 로고
    • Outgrowth-regulating actions of glutamate in isolated hippocampal pyramidal neurons
    • Mattson M. P., Dou P., and Kater S. B. (1988)Outgrowth-regulating actions of glutamate in isolated hippocampal pyramidal neurons. J. Neurosci. 8, 2087-2100.
    • (1988) J. Neurosci. , vol.8 , pp. 2087-2100
    • Mattson, M.P.1    Dou, P.2    Kater, S.B.3
  • 59
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M. P., Cheng B., Davis D., Bryant K., Lieberburg I., and Rydel R. E. (1992) β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 379-389.
    • (1992) J. Neurosci. , vol.12 , pp. 379-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 60
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson M. P., Tomaselli K., and Rydel R. E. (1993) Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res. 621, 35-49.
    • (1993) Brain Res. , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.2    Rydel, R.E.3
  • 61
    • 0029175202 scopus 로고
    • Calcium, free radicals, and excitotoxic neuronal death in primary cell culture
    • Mattson M. P., Barger S. W., Begley J. G., and Mark R. J. (1995) Calcium, free radicals, and excitotoxic neuronal death in primary cell culture. Methods Cell Biol. 46, 187-216.
    • (1995) Methods Cell Biol. , vol.46 , pp. 187-216
    • Mattson, M.P.1    Barger, S.W.2    Begley, J.G.3    Mark, R.J.4
  • 62
    • 0000131472 scopus 로고    scopus 로고
    • Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia
    • Tanzi R. E. and Wasco W., eds, Humana Press, Totowa, New Jersey
    • Mattson M. P., Furukawa K., Bruce A. J., Mark R. J., and Blanc E. (1996) Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia, in Molecular Mechanisms of Dementia (Tanzi R. E. and Wasco W., eds), pp. 103-143. Humana Press, Totowa, New Jersey.
    • (1996) Molecular Mechanisms of Dementia , pp. 103-143
    • Mattson, M.P.1    Furukawa, K.2    Bruce, A.J.3    Mark, R.J.4    Blanc, E.5
  • 63
    • 0028128554 scopus 로고
    • Immunohistochemical localization of the neuron-specific glucose transporter (GLUT3) to neuropil in adult rat brain
    • McCall A. L., Van Bueren A. M., Moholt-Siebert M., Cherry N. J., and Woodward W. R. (1994) Immunohistochemical localization of the neuron-specific glucose transporter (GLUT3) to neuropil in adult rat brain. Brain Res. 659, 292-297.
    • (1994) Brain Res. , vol.659 , pp. 292-297
    • McCall, A.L.1    Van Bueren, A.M.2    Moholt-Siebert, M.3    Cherry, N.J.4    Woodward, W.R.5
  • 64
    • 0025954861 scopus 로고
    • Immunofluorescent localization of three Na, K-ATPase isozymes in the rat central nervous system: Both neurons and glia can express more than one Na, K-ATPase
    • McGrail K. M., Phillips J. M., and Sweadner K. J. (1991) Immunofluorescent localization of three Na, K-ATPase isozymes in the rat central nervous system: both neurons and glia can express more than one Na, K-ATPase. J. Neurosci. 11, 381-391.
    • (1991) J. Neurosci. , vol.11 , pp. 381-391
    • McGrail, K.M.1    Phillips, J.M.2    Sweadner, K.J.3
  • 66
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Moccoci P., MacGarvey M. S., and Beal M. F. (1994) Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann. Neurol. 36, 747-751.
    • (1994) Ann. Neurol. , vol.36 , pp. 747-751
    • Moccoci, P.1    MacGarvey, M.S.2    Beal, M.F.3
  • 67
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival
    • Mosmann T. (1983) Rapid colorimetric assay for cellular growth and survival. J. Immunol. Methods 65, 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 68
    • 0028448460 scopus 로고
    • The use of tetrazolium salts to determine sites of damage to the mitochondrial electron transport chain in intact cells following in vitro photodynamic therapy with photofrin II
    • Musser D. A. and Oseroff A. R. (1994) The use of tetrazolium salts to determine sites of damage to the mitochondrial electron transport chain in intact cells following in vitro photodynamic therapy with photofrin II. Photochem. Photobiol. 59, 621-626.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 621-626
    • Musser, D.A.1    Oseroff, A.R.2
  • 69
    • 0028897831 scopus 로고
    • Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal
    • Nadkarni D. V. and Sayre L. M. (1995) Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal. Chem. Res. Toxicol. 8, 284-291.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 284-291
    • Nadkarni, D.V.1    Sayre, L.M.2
  • 71
    • 0023895734 scopus 로고
    • Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A., Reilly J. A., Lysko P. G., and Henneberry R. C. (1988) Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 451, 205-212.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3    Henneberry, R.C.4
  • 72
    • 0018290792 scopus 로고
    • Acute dendrotoxic changes in the hippocampus of kainate treated rats
    • Olney J. W., Fuller T., and Gubareff T. D. (1979) Acute dendrotoxic changes in the hippocampus of kainate treated rats. Brain Res. 176, 91-100.
    • (1979) Brain Res. , vol.176 , pp. 91-100
    • Olney, J.W.1    Fuller, T.2    Gubareff, T.D.3
  • 73
    • 0029145776 scopus 로고
    • Synaptosomal glutamate transport in thioacetamide-induced hepatic encephalopathy in the rat
    • Oppong K. N., Bartlett K., Record C. O., and Mardini H. (1995) Synaptosomal glutamate transport in thioacetamide-induced hepatic encephalopathy in the rat. Hepatology 22, 553-558.
    • (1995) Hepatology , vol.22 , pp. 553-558
    • Oppong, K.N.1    Bartlett, K.2    Record, C.O.3    Mardini, H.4
  • 75
    • 0028326937 scopus 로고
    • Alterations of cerebral metabolism in probable Alzheimer's disease: A preliminary study
    • Pettegrew J. W., Panchalingam K., Klunk W. E., McClure R. J., and Muenz L. R. (1994) Alterations of cerebral metabolism in probable Alzheimer's disease: a preliminary study. Neurobiol. Aging 15, 117-132.
    • (1994) Neurobiol. Aging , vol.15 , pp. 117-132
    • Pettegrew, J.W.1    Panchalingam, K.2    Klunk, W.E.3    McClure, R.J.4    Muenz, L.R.5
  • 76
    • 0006948801 scopus 로고
    • The impairment of mitochondrial membrane potential and mass in proliferating lymphocytes from vitamin e deficient animals is recovered by glutathione
    • Pieri C., Recchioni R., Marcheselli F., Moroni F., Marra M., and Benatti C. (1995) The impairment of mitochondrial membrane potential and mass in proliferating lymphocytes from vitamin E deficient animals is recovered by glutathione. Cell. Mol. Biol. 41, 755-762.
    • (1995) Cell. Mol. Biol. , vol.41 , pp. 755-762
    • Pieri, C.1    Recchioni, R.2    Marcheselli, F.3    Moroni, F.4    Marra, M.5    Benatti, C.6
  • 77
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C. J., Burdick D., Walencewicz A. J., Glabe C. G., and Cotman C. W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 78
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike C. J., Walencewicz-Wasserman A. J., Kosmoski J., Cribbs D. H., Glabe C. G., and Cotman C. W. (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
  • 80
    • 0026009926 scopus 로고
    • 4-Hydroxynonenal reduces junctional communication between endothelial cells in culture
    • Radu A. and Moldovan N. (1991) 4-Hydroxynonenal reduces junctional communication between endothelial cells in culture. Exp. Cell Res. 196, 121-126.
    • (1991) Exp. Cell Res. , vol.196 , pp. 121-126
    • Radu, A.1    Moldovan, N.2
  • 82
    • 0025348650 scopus 로고
    • Inhibition of pro-oxidant mitochondrial pyridine nucleotide hydrolysis and calcium release by 4-hydroxynonenal
    • Richter C. H. and Meier P. H. (1990) Inhibition of pro-oxidant mitochondrial pyridine nucleotide hydrolysis and calcium release by 4-hydroxynonenal. Biochem. J. 269, 735-737.
    • (1990) Biochem. J. , vol.269 , pp. 735-737
    • Richter, C.H.1    Meier, P.H.2
  • 83
    • 0027410845 scopus 로고
    • Mitochondrial calcium release induced by prooxidants
    • Richter C. and Schlegel J. (1993) Mitochondrial calcium release induced by prooxidants. Toxicol. Lett. 67, 119-127.
    • (1993) Toxicol. Lett. , vol.67 , pp. 119-127
    • Richter, C.1    Schlegel, J.2
  • 86
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides
    • Shearman M. S., Hawtin S. R., and Tailor V. J. (1995) The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides. J. Neurochem. 65, 218-227.
    • (1995) J. Neurochem. , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 88
    • 0025352542 scopus 로고
    • Altered glucose metabolism in Alzheimer's disease
    • Sims N. R. (1990) Altered glucose metabolism in Alzheimer's disease. Ann. Neurol. 27, 691-693.
    • (1990) Ann. Neurol. , vol.27 , pp. 691-693
    • Sims, N.R.1
  • 92
    • 0025259422 scopus 로고
    • 2-resistant cell lines. Do aldehyde by-products of lipid peroxidation contribute to oxidative stress?
    • 2-resistant cell lines. Do aldehyde by-products of lipid peroxidation contribute to oxidative stress? Biochem. J. 267, 453-459.
    • (1990) Biochem. J. , vol.267 , pp. 453-459
    • Spitz, D.R.1    Malcolm, R.R.2    Roberts, R.J.3
  • 93
    • 0028903712 scopus 로고
    • Activity-dependent action potential invasion and calcium influx into hippocampal CA1 dendrites
    • Spruston N., Schiller Y., Stuart G., and Sakmann B. (1995) Activity-dependent action potential invasion and calcium influx into hippocampal CA1 dendrites. Science 268, 297-300.
    • (1995) Science , vol.268 , pp. 297-300
    • Spruston, N.1    Schiller, Y.2    Stuart, G.3    Sakmann, B.4
  • 94
    • 0025334082 scopus 로고
    • Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro
    • Subbarao K. V., Richardson J. S., and Ang L. C. (1990) Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro. J. Neurochem. 55, 342-345.
    • (1990) J. Neurochem. , vol.55 , pp. 342-345
    • Subbarao, K.V.1    Richardson, J.S.2    Ang, L.C.3
  • 96
    • 0027058504 scopus 로고
    • Overlapping and diverse distribution of Na-K ATPase isozymes in neurons and glia
    • Sweadner K. J. (1991) Overlapping and diverse distribution of Na-K ATPase isozymes in neurons and glia. Can. J. Physiol. Pharmacol. (Suppl.) 70, S255-S259.
    • (1991) Can. J. Physiol. Pharmacol. , vol.70 , Issue.SUPPL.
    • Sweadner, K.J.1
  • 97
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry R. D., Masliah E., Salmon D. P., Butters N., DeTeresa R., Hill R., Hansen L. A., and Katzman R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 98
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase
    • Uchida K. and Stadtman E. R. (1993) Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 268, 6388-6393.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 99
    • 0027946778 scopus 로고
    • Michael addition-type-4-hydroxy-2-nonenal adducts in modified low-density lipoproteins: Markers for atherosclerosis
    • Uchida K., Toyokuni S., Nishikawa K., Kawakishi S., Oda H., Hiai H., and Stadtman E. R. (1994) Michael addition-type-4-hydroxy-2-nonenal adducts in modified low-density lipoproteins: markers for atherosclerosis. Biochemistry 33, 12487-12494.
    • (1994) Biochemistry , vol.33 , pp. 12487-12494
    • Uchida, K.1    Toyokuni, S.2    Nishikawa, K.3    Kawakishi, S.4    Oda, H.5    Hiai, H.6    Stadtman, E.R.7
  • 101
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra A., Trotti D., Tromba C., Floridi S., and Racagni G. (1994) Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14, 2924-2932.
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 102
    • 0029906188 scopus 로고    scopus 로고
    • Monoclonal antibodies for detection of 4-hydroxynonenal modified proteins
    • Waeg G., Dimsity G., and Esterbauer H. (1996) Monoclonal antibodies for detection of 4-hydroxynonenal modified proteins. Free Radic. Res. 25, 149-159.
    • (1996) Free Radic. Res. , vol.25 , pp. 149-159
    • Waeg, G.1    Dimsity, G.2    Esterbauer, H.3
  • 103
    • 0002358665 scopus 로고
    • The separation of synaptic vesicles from nerve ending particles (synaptosomes)
    • Whittaker V. P., Michaelson J. A., and Kirkland R. J. A. (1964) The separation of synaptic vesicles from nerve ending particles (synaptosomes). Biochem. J. 90, 293-303.
    • (1964) Biochem. J. , vol.90 , pp. 293-303
    • Whittaker, V.P.1    Michaelson, J.A.2    Kirkland, R.J.A.3
  • 104
    • 0025051227 scopus 로고
    • Relationships between the mitochondrial transmembrane potential, ATP concentration, and cytotoxicity in isolated rat hepatocytes
    • Wu E. Y., Smith M. T., Bellomo G., and DiMonte D. (1990) Relationships between the mitochondrial transmembrane potential, ATP concentration, and cytotoxicity in isolated rat hepatocytes. Arch. Biochem. Biophys. 282, 358-362.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 358-362
    • Wu, E.Y.1    Smith, M.T.2    Bellomo, G.3    DiMonte, D.4
  • 107
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner B. A. (1996) Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 108
    • 0021049342 scopus 로고
    • +-dependent D-glucose uptake by intestinal brush border membrane vesicles
    • +-dependent D-glucose uptake by intestinal brush border membrane vesicles. Biochem. Pharmacol. 32, 3453-3457.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 3453-3457
    • Yokota, K.1    Nishi, Y.2    Takesue, Y.3
  • 109
    • 0027232517 scopus 로고
    • Basic FGF, NGF, and IGFs protect hippocampal neurons against iron-induced degeneration
    • Zhang Y., Tatsuno T., Carney J., and Mattson M. P. (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
  • 111
    • 0029811118 scopus 로고    scopus 로고
    • Actions of neurotoxic β-amyloid on calcium homeostasis and viability of PC12 cells are blocked by antioxidants but not by calcium channel antagonists
    • Zhou Y., Gopalakrishnan V., and Richardson J. S. (1996) Actions of neurotoxic β-amyloid on calcium homeostasis and viability of PC12 cells are blocked by antioxidants but not by calcium channel antagonists. J. Neurochem. 67, 1419-1425.
    • (1996) J. Neurochem. , vol.67 , pp. 1419-1425
    • Zhou, Y.1    Gopalakrishnan, V.2    Richardson, J.S.3


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