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Volumn 973, Issue , 2002, Pages 323-333

Signal transduction through tyrosine-phosphorylated carboxy-terminal fragments of APP via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain

Author keywords

Adaptor proteins; Alzheimer's disease; Amyloid precursor protein; Astrocytes; MAPK

Indexed keywords

ADAPTOR PROTEIN; AMYLOID PRECURSOR PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE 1; PROTEIN SHC; THROMBIN;

EID: 0036959694     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2002.tb04660.x     Document Type: Conference Paper
Times cited : (33)

References (40)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • SELKOE, D.J. 2001. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81: 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 0030668423 scopus 로고    scopus 로고
    • Diagnostic criteria for neuropathologic assessment of Alzheimer's disease
    • BRAAK, H. & E. BRAAK. 1997. Diagnostic criteria for neuropathologic assessment of Alzheimer's disease. Neurobiol. Aging 18: S85-S88.
    • (1997) Neurobiol. Aging , vol.18
    • Braak, H.1    Braak, E.2
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • GLENNER, G.G. & C.W. WONG. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120: 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0020956552 scopus 로고
    • Cortical neuronal counts in normal elderly controls and demented patients
    • MOUNTJOY, C.Q., M. ROTH, N.J.R. EVANS & H.M. EVANS. 1983. Cortical neuronal counts in normal elderly controls and demented patients. Neurobiol. Aging 4: 1-11.
    • (1983) Neurobiol. Aging , vol.4 , pp. 1-11
    • Mountjoy, C.Q.1    Roth, M.2    Evans, N.J.R.3    Evans, H.M.4
  • 6
    • 0023276014 scopus 로고
    • Neocortical cell counts in normal human adult aging
    • TERRY, R.D., R. DE TERESA & L.A. HANSEN. 1987. Neocortical cell counts in normal human adult aging. Ann. Neurol. 21: 530-539.
    • (1987) Ann. Neurol. , vol.21 , pp. 530-539
    • Terry, R.D.1    De Teresa, R.2    Hansen, L.A.3
  • 7
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • KANG, J., H.G. LEMAIRE, A. UNTERBECK, et al. 1987. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325: 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 8
    • 0029935765 scopus 로고    scopus 로고
    • Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons
    • SIMONS, M., B. DE STROOPER, G. MULTHAUP, et al. 1996. Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons. J. Neurosci. 16: 899-908.
    • (1996) J. Neurosci. , vol.16 , pp. 899-908
    • Simons, M.1    De Strooper, B.2    Multhaup, G.3
  • 9
    • 0029862137 scopus 로고    scopus 로고
    • Age-dependent neuronal and synaptic degeneration in mice transgenic for the C terminus of the amyloid precursor protein
    • OSTER-GRANITE, M.L., D.L. MCPHIE, J. GREENAN & R.L. NEVE. 1996. Age-dependent neuronal and synaptic degeneration in mice transgenic for the C terminus of the amyloid precursor protein. J. Neurosci. 16: 6732-6741.
    • (1996) J. Neurosci. , vol.16 , pp. 6732-6741
    • Oster-Granite, M.L.1    McPhie, D.L.2    Greenan, J.3    Neve, R.L.4
  • 10
    • 0029888942 scopus 로고    scopus 로고
    • Transgenic mice expressing APP-C100 in the brain
    • NEVE, R.L., F.M. BOYCE & D.L. MCPHIE. 1996. Transgenic mice expressing APP-C100 in the brain. Neurobiol. Aging 17: 191-203.
    • (1996) Neurobiol. Aging , vol.17 , pp. 191-203
    • Neve, R.L.1    Boyce, F.M.2    McPhie, D.L.3
  • 11
    • 0030867815 scopus 로고    scopus 로고
    • Neuronal expression of beta-amy-loid precursor protein Alzheimer mutations causes intracellular accumulation of a C-terminal fragment containing both the amyloid beta and cytoplasmic domains
    • MCPHIE, D.L., R.K. LEE, C.B. ECKMAN, et al. 1997. Neuronal expression of beta-amy-loid precursor protein Alzheimer mutations causes intracellular accumulation of a C-terminal fragment containing both the amyloid beta and cytoplasmic domains. J. Biol. Chem. 272: 24743-24746.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24743-24746
    • McPhie, D.L.1    Lee, R.K.2    Eckman, C.B.3
  • 12
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • HAASS, C., E.H. KOO, A. MELLON, et al. 1992. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 327: 500-503.
    • (1992) Nature , vol.327 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3
  • 13
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • GOLDE, T.E., S. ESTUS, L.H. YOUNKIN, et al. 1992. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255: 728-730.
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3
  • 14
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • VASSAR, R., B.D. BENNETT, S. BABU-KAN, et al. 1999. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Kan, S.3
  • 15
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein beta-secretase from human brain
    • SINHA, S., J.P. ANDERSON, R. BARBOUR, et al. 1999. Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature 402: 537-540.
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3
  • 16
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity
    • YAN, R., M.J. BIENKOWSKI, M.E. SHUCK, et al. 1999. Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity. Nature 402: 533-537.
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 17
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: Implication for the pathogenesis of Alzheimer's disease
    • JARRETT, J.T., E.P. BERGER & P.T. LANSBURY, JR. 1993. The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implication for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 18
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of α-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • MARCINKIEWICZ, M. & N.G. SEIDAH. Coordinated expression of α-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain. J. Neurochem. 75: 2133-2143.
    • J. Neurochem. , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 19
    • 0032776320 scopus 로고    scopus 로고
    • Diversity in protein recognition by PTB domains
    • FORMAN-KAY, J.D. & T. PAWSON. 1999. Diversity in protein recognition by PTB domains. Curr. Opin. Struct. Biol. 9: 690-695.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 690-695
    • Forman-Kay, J.D.1    Pawson, T.2
  • 20
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • BORG, J.P., J. OOI, E. LEVY & B. MARGOLIS. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16: 6229-6241.
    • Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 21
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • HOWELL, B.W., L.M. LANIER, R. FRANK, et al. 1999. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19: 5179-5188.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3
  • 22
    • 0030894021 scopus 로고    scopus 로고
    • Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins
    • ZAMBRANO, N., J.D. BUXBAUM, G. MINOPOLI, et al. 1997. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins. J. Biol. Chem. 272: 6399-6405.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6399-6405
    • Zambrano, N.1    Buxbaum, J.D.2    Minopoli, G.3
  • 23
    • 0035118308 scopus 로고    scopus 로고
    • Identification of amino-terminally and phosphotyrosine modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain
    • RUSSO, C., S. SALIS, V. DOLCINI, et al. 2001. Identification of amino-terminally and phosphotyrosine modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain. Neurobiol. Disease 8: 173-180.
    • (2001) Neurobiol. Disease , vol.8 , pp. 173-180
    • Russo, C.1    Salis, S.2    Dolcini, V.3
  • 24
    • 0035827587 scopus 로고    scopus 로고
    • The α-amyloid precursor protein APP is tyrosine phosphorilated in cells expressing a constitutively active form of the Abl protoncogene
    • ZAMBRANO, N., P. BRUNI, O. MINOPOLI, et al. 2001. The α-amyloid precursor protein APP is tyrosine phosphorilated in cells expressing a constitutively active form of the Abl protoncogene. J. Biol. Chem. 276: 19787-19792.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19787-19792
    • Zambrano, N.1    Bruni, P.2    Minopoli, O.3
  • 25
    • 10144263284 scopus 로고    scopus 로고
    • The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein
    • TIENARI, P.J., B. DE STROOPER, E. IKONEN, et al. 1996. The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein. EMBO J. 15: 5218-5229.
    • (1996) EMBO J. , vol.15 , pp. 5218-5229
    • Tienari, P.J.1    De Strooper, B.2    Ikonen, E.3
  • 26
    • 0029057814 scopus 로고
    • Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • YANG, A.J., M. KNAUER, D.A. BURDICK & C. GLABE. 1995. Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J. Biol. Chem. 270: 14786-14792.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 27
    • 0032213730 scopus 로고    scopus 로고
    • Emerging roles for SH2/PTB-containing Shc adaptor proteins in the developing mammalian brain
    • CATTANEO, E. & P.G. PELICCI. 1998. Emerging roles for SH2/PTB-containing Shc adaptor proteins in the developing mammalian brain. Trends Neurosci. 21: 476-481.
    • (1998) Trends Neurosci. , vol.21 , pp. 476-481
    • Cattaneo, E.1    Pelicci, P.G.2
  • 28
    • 0029731182 scopus 로고    scopus 로고
    • Characterization of the phosphotyrosine-binding domain of the Drosophila Shcprotein
    • LI, S.C., K.M. LAI, G.D. GISH, et al. 1996. Characterization of the phosphotyrosine-binding domain of the Drosophila Shcprotein. J. Biol. Chem. 271: 31855-31862.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31855-31862
    • Li, S.C.1    Lai, K.M.2    Gish, G.D.3
  • 29
    • 0028276575 scopus 로고
    • Extracellular signal regulated kinases. Localization of protein and mRNA in the human hippocampal formation in Alzheimer's disease
    • HYMAN, B.T., T.E. ELVHAGE & J. REITER. 1994. Extracellular signal regulated kinases. Localization of protein and mRNA in the human hippocampal formation in Alzheimer's disease. Am. J. Pathol. 144: 565-572.
    • (1994) Am. J. Pathol. , vol.144 , pp. 565-572
    • Hyman, B.T.1    Elvhage, T.E.2    Reiter, J.3
  • 30
    • 0034612175 scopus 로고    scopus 로고
    • Neuroinflammation Working Group. 2000. Neurobiol. Aging 21: 383-421.
    • (2000) Neurobiol. Aging , vol.21 , pp. 383-421
  • 31
    • 0028027214 scopus 로고
    • Thrombin receptor activation induces secretion and nonamyloidogenic processing of amyloid beta-protein precursor
    • DAVIS-SALINAS, J., S.M. SAPORITO-IRWIN, F.M. DONOVAN, et al. 1994. Thrombin receptor activation induces secretion and nonamyloidogenic processing of amyloid beta-protein precursor. J. Biol. Chem. 269: 22623-22627.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22623-22627
    • Davis-Salinas, J.1    Saporito-Irwin, S.M.2    Donovan, F.M.3
  • 32
    • 0033347395 scopus 로고    scopus 로고
    • Pertussis toxin-sensitive and -insensitive thrombin stimulation of shcphosphorylation and mitogenesis are mediated through distinct pathways
    • RICKETTS, W.A., J.H. BROWN & J.M. OLEFSKY. 1999. Pertussis toxin-sensitive and -insensitive thrombin stimulation of shcphosphorylation and mitogenesis are mediated through distinct pathways. Mol. Endocrinol. 13: 1988-2001.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1988-2001
    • Ricketts, W.A.1    Brown, J.H.2    Olefsky, J.M.3
  • 33
    • 0034284153 scopus 로고    scopus 로고
    • Serine proteases and brain damage - Is there a link?
    • GINGRICH, M.B. & S.F. TRAYNELIS. 2000. Serine proteases and brain damage - Is there a link? Trends Neurosci. 23: 399-407.
    • (2000) Trends Neurosci. , vol.23 , pp. 399-407
    • Gingrich, M.B.1    Traynelis, S.F.2
  • 34
    • 0028864592 scopus 로고
    • Thrombin activates mitogen-activated protein kinase in primary astrocyte cultures
    • BHAT, N.R., P. ZHANG & E. HOGAN. 1995. Thrombin activates mitogen-activated protein kinase in primary astrocyte cultures. J. Cell. Physiol. 165: 417-424.
    • (1995) J. Cell. Physiol. , vol.165 , pp. 417-424
    • Bhat, N.R.1    Zhang, P.2    Hogan, E.3
  • 35
    • 0026454599 scopus 로고
    • Thrombin accumulation in brains of patients with Alzheimer's disease
    • AKIYAMA, H., K. IKEDA, H. KONDO & P.L. MCGEER. 1992. Thrombin accumulation in brains of patients with Alzheimer's disease. Neurosci. Lett. 146: 152-154.
    • (1992) Neurosci. Lett. , vol.146 , pp. 152-154
    • Akiyama, H.1    Ikeda, K.2    Kondo, H.3    McGeer, P.L.4
  • 36
    • 0034161592 scopus 로고    scopus 로고
    • Protease-activated receptors: Sentries for inflammation?
    • COCKS, T.M. & J.D. MOFFATT. 2000. Protease-activated receptors: sentries for inflammation? Trends Pharmacol. Sci. 21: 103-108.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 103-108
    • Cocks, T.M.1    Moffatt, J.D.2
  • 37
    • 0030829885 scopus 로고    scopus 로고
    • The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system
    • TURGEON, V. & L.J. HOUENOU. 1997. The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system. Brain Res. Brain Res. Rev. 25: 85-95.
    • (1997) Brain Res. Brain Res. Rev. , vol.25 , pp. 85-95
    • Turgeon, V.1    Houenou, L.J.2
  • 38
    • 0034001547 scopus 로고    scopus 로고
    • Thrombin inhibitor ameliorates secondary damage in rat brain injury: Suppression of inflammatory cells and vimentin-positive astrocytes
    • KUBO, Y., M. SUZUKI, A. KUDO, et al. 2000. Thrombin inhibitor ameliorates secondary damage in rat brain injury: suppression of inflammatory cells and vimentin-positive astrocytes. J. Neurotrauma 17: 163-172.
    • (2000) J. Neurotrauma , vol.17 , pp. 163-172
    • Kubo, Y.1    Suzuki, M.2    Kudo, A.3
  • 39
    • 0028935717 scopus 로고
    • Ligand-dependent G protein coupling function of amyloid transmembrane precursor
    • T. OKAMOTO, S. TAKEDA, Y. MURAYAMA, et al. 1995. Ligand-dependent G protein coupling function of amyloid transmembrane precursor. J. Biol. Chem. 270: 4205-4208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4205-4208
    • Okamoto, T.1    Takeda, S.2    Murayama, Y.3
  • 40
    • 0034672421 scopus 로고    scopus 로고
    • Alzheimer's disease: A dysfunction of the amyloid precursor protein
    • NEVE, R.L., D.L. MCPHIE & Y. CHEN. 2000. Alzheimer's disease: a dysfunction of the amyloid precursor protein. Brain Res. 886: 54-66.
    • (2000) Brain Res. , vol.886 , pp. 54-66
    • Neve, R.L.1    McPhie, D.L.2    Chen, Y.3


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