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Volumn 69, Issue 3, 1997, Pages 978-985

β-Amyloid-induced neurotoxicity of a hybrid septal cell line associated with increased tau phosphorylation and expression of β-amyloid precursor protein

Author keywords

Alzheimer's disease; Tau phosphorylation; Amyloid; Amyloid precursor protein

Indexed keywords

AMYLOID BETA PROTEIN; PROTEIN PRECURSOR;

EID: 1842404212     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69030978.x     Document Type: Article
Times cited : (49)

References (43)
  • 2
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediated amyloid β protein toxicity
    • Behl C., Davis J. B., Lesley R., and Schubert D. (1994) Hydrogen peroxide mediated 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
  • 4
    • 0029925968 scopus 로고    scopus 로고
    • Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons
    • Burack M. A. and Halpain S. (1996) Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons. Neuroscience 72, 167-184.
    • (1996) Neuroscience , vol.72 , pp. 167-184
    • Burack, M.A.1    Halpain, S.2
  • 5
    • 0028986916 scopus 로고
    • 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
  • 7
    • 0029123294 scopus 로고
    • The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures
    • Davis D. R., Brion J. P., Couck A. M., Gallo J. M., Hanger D. P., Ladhani K., Lewis C., Miller C. C., Rupniak T., Smith C., and Anderton B. H. (1995) The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures. Biochem. J. 309, 941-949.
    • (1995) Biochem. J. , vol.309 , pp. 941-949
    • Davis, D.R.1    Brion, J.P.2    Couck, A.M.3    Gallo, J.M.4    Hanger, D.P.5    Ladhani, K.6    Lewis, C.7    Miller, C.C.8    Rupniak, T.9    Smith, C.10    Anderton, B.H.11
  • 9
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M., Spillantini M. G., Cairns N. J., and Crowther R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 10
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M., Jakes R., Crowther R. A., Cohen P., Vanmechelen E., Vandermeerens M., and Cras P. (1994) Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J. 301, 871-877.
    • (1994) Biochem. J. , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeerens, M.6    Cras, P.7
  • 11
    • 0028179001 scopus 로고
    • Secreted β-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation
    • Greenberg S. M., Koo E. H., Selkoe D. J., Qiu W. Q., and Kosik K. S. (1994) Secreted β-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation. Proc. Natl. Acad. Sci. USA 91, 7104-7108.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7104-7108
    • Greenberg, S.M.1    Koo, E.H.2    Selkoe, D.J.3    Qiu, W.Q.4    Kosik, K.S.5
  • 12
    • 0026484738 scopus 로고
    • Tau pathology in a case of familial Alzheimer's disease with a valine to glycine mutation at position 717 in the amyloid precursor protein
    • Hanger D. P., Mann D. M., Neary D., and Anderton B. H. (1992) Tau pathology in a case of familial Alzheimer's disease with a valine to glycine mutation at position 717 in the amyloid precursor protein. Neurosci. Lett. 145, 178-180.
    • (1992) Neurosci. Lett. , vol.145 , pp. 178-180
    • Hanger, D.P.1    Mann, D.M.2    Neary, D.3    Anderton, B.H.4
  • 14
    • 0026539331 scopus 로고
    • Alzheimer's disease: A cell biological perspective
    • Kosik K. S. (1992) Alzheimer's disease: a cell biological perspective. Science 256, 780-783.
    • (1992) Science , vol.256 , pp. 780-783
    • Kosik, K.S.1
  • 16
    • 0029056516 scopus 로고
    • Cell death induced by β-amyloid 1-40 in MES23.5 hybrid clone: The role of nitric oxide and NMDA-gated channel activation leading to apoptosis
    • Le W. D., Colom L., Xie W. J., Smith R. G., Alexianu M., and Appel S. H. (1995a) Cell death induced by β-amyloid 1-40 in MES23.5 hybrid clone: the role of nitric oxide and NMDA-gated channel activation leading to apoptosis. Brain Res. 686, 49-60.
    • (1995) Brain Res. , vol.686 , pp. 49-60
    • Le, W.D.1    Colom, L.2    Xie, W.J.3    Smith, R.G.4    Alexianu, M.5    Appel, S.H.6
  • 18
    • 0029917884 scopus 로고    scopus 로고
    • Regulation of tau phosphorylation in Alzheimer's disease
    • Lee V. M.-Y. (1996) Regulation of tau phosphorylation in Alzheimer's disease. Ann. NY Acad. Sci. 777, 107-113.
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 107-113
    • Lee, V.M.-Y.1
  • 20
    • 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. (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
  • 21
    • 0028989637 scopus 로고
    • Alzheimer's-associated phospho-tau epitope in human neuroblastoma cell cultures: Up-regulation by fibronectin and laminin
    • Martin H., Lambert M. P., Barber K., Hinton S., and Klein W. L. (1995) Alzheimer's-associated phospho-tau epitope in human neuroblastoma cell cultures: up-regulation by fibronectin and laminin. Neuroscience 66, 769-779.
    • (1995) Neuroscience , vol.66 , pp. 769-779
    • Martin, H.1    Lambert, M.P.2    Barber, K.3    Hinton, S.4    Klein, W.L.5
  • 22
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E. S., Shin R. W., Billingsley M. L., Van deVoorde A., O'Connor M., Trojanowski J. Q., and Lee V. M.-Y. (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    Van DeVoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 23
    • 0029037264 scopus 로고
    • Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD
    • Mattson M. P. (1995) Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD. Neurobiol. Aging 16, 447-463.
    • (1995) Neurobiol. Aging , vol.16 , pp. 447-463
    • Mattson, M.P.1
  • 24
    • 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, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 26
    • 0027422751 scopus 로고
    • Genetic and molecular advances in Alzheimer's disease
    • Mullan M. and Crawford F. (1993) Genetic and molecular advances in Alzheimer's disease. Trends Neurosci. 16, 398-403.
    • (1993) Trends Neurosci. , vol.16 , pp. 398-403
    • Mullan, M.1    Crawford, F.2
  • 27
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • Multhaup G., Schlicksupp A., Hesse L., Beher D., Ruppert T., Masters C. L., and Beyreuther K. (1996) The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I). Science 271, 1406-1409.
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 28
    • 0029015370 scopus 로고
    • Neuronal kinase stimulation leads to aberrant tau phosphorylation and neurotoxicity
    • Nuydens R., De Jong M., Nuyens R., Cornelissen E., and Geerts H. (1995) Neuronal kinase stimulation leads to aberrant tau phosphorylation and neurotoxicity. Neurobiol. Aging 16, 465-477.
    • (1995) Neurobiol. Aging , vol.16 , pp. 465-477
    • Nuydens, R.1    De Jong, M.2    Nuyens, R.3    Cornelissen, E.4    Geerts, H.5
  • 29
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L. Jr., Feiner L., Lang E., Szendrei G. I., Goedert M., and Lee V. M. (1994) Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J. Neurosci. Res. 39, 669-673.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.6
  • 30
    • 1842410391 scopus 로고
    • Oxidative stress and neuronal insult: Tau dephosphorylation is an early event
    • Pang Z., Bondada V., and Geddes J. W. (1995) Oxidative stress and neuronal insult: tau dephosphorylation is an early event. Soc. Neurosci. Abstr. 21, 774.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 774
    • Pang, Z.1    Bondada, V.2    Geddes, J.W.3
  • 31
    • 0026508741 scopus 로고
    • Differential effects of neurotrophic factors on neurotransmitter development in the IMR-32 human neuroblastoma cell line
    • Rabinovsky E. D., Le W. D., and McManaman J. L. (1992) Differential effects of neurotrophic factors on neurotransmitter development in the IMR-32 human neuroblastoma cell line. J. Neurosci. 12, 171-179.
    • (1992) J. Neurosci. , vol.12 , pp. 171-179
    • Rabinovsky, E.D.1    Le, W.D.2    McManaman, J.L.3
  • 32
    • 0024810385 scopus 로고
    • The regulation of amyloid β protein precursor secretion and its modulatory role in cell adhesion
    • Schubert D., Jin L. W., Saitoh T., and Cole G. (1989) The regulation of amyloid β protein precursor secretion and its modulatory role in cell adhesion. Neuron 3, 689-694.
    • (1989) Neuron , vol.3 , pp. 689-694
    • Schubert, D.1    Jin, L.W.2    Saitoh, T.3    Cole, G.4
  • 33
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • Selkoe D. J. (1994) Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17, 489-517.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 34
    • 0342739366 scopus 로고
    • β-Amyloid 25-35 (βA) induced tau-immunoreactivity following injections into the amygdala of rats in vivo
    • Sigurdsson E. M., Hejna M. J., Magnuson D. J., Lee J. M., and Lorens S. A. (1995) β-Amyloid 25-35 (βA) induced tau-immunoreactivity following injections into the amygdala of rats in vivo. Soc. Neurosci. Abstr. 21, 1719.
    • (1995) Soc. Neurosci. Abstr. , vol.21 , pp. 1719
    • Sigurdsson, E.M.1    Hejna, M.J.2    Magnuson, D.J.3    Lee, J.M.4    Lorens, S.A.5
  • 35
    • 0028173843 scopus 로고
    • Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex
    • Sindou P., Lesort M., Couratier P., Yardin C., Esclaire F., and Hugon J. (1994) Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex. Brain Res. 646, 124-128.
    • (1994) Brain Res. , vol.646 , pp. 124-128
    • Sindou, P.1    Lesort, M.2    Couratier, P.3    Yardin, C.4    Esclaire, F.5    Hugon, J.6
  • 37
    • 0026646280 scopus 로고
    • Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat
    • Stephenson D. T., Rash K., and Clemens J. A. (1992) Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat. Brain Res. 593, 128-135.
    • (1992) Brain Res. , vol.593 , pp. 128-135
    • Stephenson, D.T.1    Rash, K.2    Clemens, J.A.3
  • 39
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid β-peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β
    • Takashima A., Noguchi K., Michel G., Mercken M., Hoshi M., Ishiguro K., and Imahori K. (1996) Exposure of rat hippocampal neurons to amyloid β-peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β. Neurosci. Lett. 203, 33-36.
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 40
    • 0026346393 scopus 로고
    • In vitro cell cultures as a model of the basal forebrain
    • (Napier T. C., Kalivas P. W., and Hanin I., eds), Plenum Press, New York
    • Wainer B. H., Lee H. T., Roback J. D., and Hammond D. N. (1991) In vitro cell cultures as a model of the basal forebrain, in The Basal Forebrain (Napier T. C., Kalivas P. W., and Hanin I., eds), pp. 415-434. Plenum Press, New York.
    • (1991) The Basal Forebrain , pp. 415-434
    • Wainer, B.H.1    Lee, H.T.2    Roback, J.D.3    Hammond, D.N.4
  • 42
    • 0029896354 scopus 로고    scopus 로고
    • Mechanism of neuronal degeneration in Alzheimer's disease
    • Yankner B. A. (1996) Mechanism of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 43
    • 0026779680 scopus 로고
    • Degeneration in vitro of post-mitotic neurons overexpressing the Alzheimer amyloid protein precursor
    • Yoshikawa K., Aizawa T., and Hayashi Y. (1992) Degeneration in vitro of post-mitotic neurons overexpressing the Alzheimer amyloid protein precursor. Nature 359, 64-67.
    • (1992) Nature , vol.359 , pp. 64-67
    • Yoshikawa, K.1    Aizawa, T.2    Hayashi, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.