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Volumn 5, Issue 2, 1998, Pages 81-88

Enhancement of outward potassium current may participate in β-amyloid peptide-induced cortical neuronal death

Author keywords

Alzheimer's disease; Apoptosis; Calcium; Delayed rectifier; Ion channel; TEA

Indexed keywords

4 AMINOPYRIDINE; AMYLOID BETA PROTEIN; CALCIUM CHANNEL; CALCIUM CHANNEL BLOCKING AGENT; CHARYBDOTOXIN; GADOLINIUM; NIFEDIPINE; POTASSIUM CHANNEL BLOCKING AGENT; TETRYLAMMONIUM;

EID: 0004491134     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1006/nbdi.1998.0186     Document Type: Article
Times cited : (184)

References (51)
  • 2
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., Rojas, E., & Pollard, H. B. (1993) Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. USA 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 3
    • 0344136514 scopus 로고
    • Tyrosine kinase inhibitors induce neuronal apoptosis, but attenuate NMDA-mediated neurotoxicity in cortical cell cultures
    • Behrens, M. M., Gwag, B. J., Koh, J., & Choi, D. W. (1995) Tyrosine kinase inhibitors induce neuronal apoptosis, but attenuate NMDA-mediated neurotoxicity in cortical cell cultures. Soc. Neurosci. Abs. 21, 1585.
    • (1995) Soc. Neurosci. Abs. , vol.21 , pp. 1585
    • Behrens, M.M.1    Gwag, B.J.2    Koh, J.3    Choi, D.W.4
  • 8
    • 0026482631 scopus 로고
    • Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium
    • Franklin, J. L., & Johnson, E. M., Jr. (1992) Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium. TINS 15, 501-508.
    • (1992) TINS , vol.15 , pp. 501-508
    • Franklin, J.L.1    Johnson E.M., Jr.2
  • 9
    • 0029923244 scopus 로고    scopus 로고
    • Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein
    • Fraser, S. P., Suh, Y-H., Chong, Y. H., & Djamgoz, M. B. A. (1996) Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein. J. Neurochem. 66, 2034-2040.
    • (1996) J. Neurochem. , vol.66 , pp. 2034-2040
    • Fraser, S.P.1    Suh, Y.-H.2    Chong, Y.H.3    Djamgoz, M.B.A.4
  • 10
    • 0031014448 scopus 로고    scopus 로고
    • Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments
    • Fraser, S. P., Suh, Y-H., & Djamgoz, M. B. A. (1997) Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments. TINS 20, 67-72.
    • (1997) TINS , vol.20 , pp. 67-72
    • Fraser, S.P.1    Suh, Y.-H.2    Djamgoz, M.B.A.3
  • 11
    • 0028037404 scopus 로고
    • Amyloid beta protein-induced irreversible current in rat cortical neurones
    • Furukawa, K., Abe, Y., & Akaike, N. (1994) Amyloid beta protein-induced irreversible current in rat cortical neurones. Neuroreport 5, 2016-2018.
    • (1994) Neuroreport , vol.5 , pp. 2016-2018
    • Furukawa, K.1    Abe, Y.2    Akaike, N.3
  • 12
    • 0030068094 scopus 로고    scopus 로고
    • + channels and suppression of neuronal activity by secreted β-amyloid-precursor protein
    • + channels and suppression of neuronal activity by secreted β-amyloid-precursor protein. Nature 379, 74-78.
    • (1996) Nature , vol.379 , pp. 74-78
    • Furukawa, K.1    Barger, S.W.2    Blalock, E.M.3    Mattson, M.P.4
  • 13
    • 0023244774 scopus 로고
    • The role of depolarization in the survival and differentiation of cerebellar granule cells in culture
    • Gallo, V., Kingsbury, A., Balazs, R., & Jorgensen, O. S. (1987) The role of depolarization in the survival and differentiation of cerebellar granule cells in culture. J. Neurosci. 7, 2203-2213.
    • (1987) J. Neurosci. , vol.7 , pp. 2203-2213
    • Gallo, V.1    Kingsbury, A.2    Balazs, R.3    Jorgensen, O.S.4
  • 14
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., & Higgins, G. A. (1992) Alzheimer's disease: The amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 15
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. (1995) Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 16
    • 0014089361 scopus 로고
    • The selective inhibition of delayed potassium currents in nerve by tetraethylammonium ion
    • Hille, B. (1967) The selective inhibition of delayed potassium currents in nerve by tetraethylammonium ion. J. Gen. Physiol. 50, 1287-1302.
    • (1967) J. Gen. Physiol. , vol.50 , pp. 1287-1302
    • Hille, B.1
  • 17
    • 0030695214 scopus 로고    scopus 로고
    • Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation
    • Holmes, T. C., Berman, K., Swartz, J. E., Dagan, D., & Levitan, I. B. (1997) Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation. J. Neurosci. 17, 8964-8974.
    • (1997) J. Neurosci. , vol.17 , pp. 8964-8974
    • Holmes, T.C.1    Berman, K.2    Swartz, J.E.3    Dagan, D.4    Levitan, I.B.5
  • 20
    • 0028019105 scopus 로고
    • Possible role of neuronal apoptosis in Alzheimer's disease
    • Johnson, E. M., Jr. (1994) Possible role of neuronal apoptosis in Alzheimer's disease. Neurobiol. Aging 15, S187-S189.
    • (1994) Neurobiol. Aging , vol.15
    • Johnson E.M., Jr.1
  • 21
    • 0026584043 scopus 로고
    • A "calcium set-point hypothesis" of neuronal dependence on neurotrophic factor
    • Johnson, E. M., Jr., Koike, T., & Franklin, J. (1992) A "calcium set-point hypothesis" of neuronal dependence on neurotrophic factor. Exp. Neurol. 115, 163-166.
    • (1992) Exp. Neurol. , vol.115 , pp. 163-166
    • Johnson E.M., Jr.1    Koike, T.2    Franklin, J.3
  • 22
    • 0030608841 scopus 로고    scopus 로고
    • +-ATPase activity, glucose transport, and glutamate transport induced by amyloid β-peptide and iron
    • +-ATPase activity, glucose transport, and glutamate transport induced by amyloid β-peptide and iron. J. Neurosci. Res. 50, 522-530.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 522-530
    • Keller, J.N.1    Germeyer, A.2    Begley, J.G.3    Mattson, M.P.4
  • 23
    • 0027360460 scopus 로고
    • Protein tyrosine phosphorylation is mandatory for CD40-mediated rescue of germinal center B cells from apoptosis
    • Knox, K. A., & Gordon, J. (1993) Protein tyrosine phosphorylation is mandatory for CD40-mediated rescue of germinal center B cells from apoptosis. Eur. J. Immunol. 23, 2578-2584.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2578-2584
    • Knox, K.A.1    Gordon, J.2
  • 24
    • 0023221068 scopus 로고
    • Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay
    • Koh, J. Y., & Choi, D. W. (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
  • 26
    • 0026646328 scopus 로고
    • In vivo neurotoxicity of beta amyloid β(1-40) and the β(25-35) fragment
    • Kowall, N. W., McKee, A. C., Yankner, B. A., & Beal, M. F. (1992) In vivo neurotoxicity of beta amyloid β(1-40) and the β(25-35) fragment. Neurobiol. Aging 13, 537-542.
    • (1992) Neurobiol. Aging , vol.13 , pp. 537-542
    • Kowall, N.W.1    McKee, A.C.2    Yankner, B.A.3    Beal, M.F.4
  • 27
    • 0028981717 scopus 로고
    • The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla, F. M., Tinkle, B. T., Bieberich, C. J., Haudenschild, C. C., & Jay, G. (1995) The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nature Genet. 9, 21-30.
    • (1995) Nature Genet. , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 28
    • 0026602899 scopus 로고
    • A group of potassium-channel blockers-acetylcholine releasers: New potentials for Alzheimer's disease? A review
    • Lavretsky, E. P., & Jarvik, L. F. (1992) A group of potassium-channel blockers-acetylcholine releasers: New potentials for Alzheimer's disease? A review. J. Clin. Psychopharmacol. 12, 110-118.
    • (1992) J. Clin. Psychopharmacol. , vol.12 , pp. 110-118
    • Lavretsky, E.P.1    Jarvik, L.F.2
  • 29
    • 0029001091 scopus 로고
    • Neuronal membrane conductance activated by amyloid β peptide: Importance of peptide conformation
    • Li, W. Y., Czilli, D. L., & Simmons, L. K. (1995) Neuronal membrane conductance activated by amyloid β peptide: Importance of peptide conformation. Brain Res. 682, 207-211.
    • (1995) Brain Res. , vol.682 , pp. 207-211
    • Li, W.Y.1    Czilli, D.L.2    Simmons, L.K.3
  • 31
    • 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., & 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
  • 33
    • 0015483326 scopus 로고
    • +-current components of a molluscan neurone
    • +-current components of a molluscan neurone. Pflüger's Arch. 336, 87-100.
    • (1972) Pflüger's Arch. , vol.336 , pp. 87-100
    • Neher, E.1    Lux, H.D.2
  • 34
    • 0027453525 scopus 로고
    • Tyrosine kinase(s) regulate apoptosis and bcl-2 expression in a growth factor-dependent cell line
    • Otani, H., Erdos, M., & Leonard, W. J. (1993) Tyrosine kinase(s) regulate apoptosis and bcl-2 expression in a growth factor-dependent cell line. J. Biol. Chem. 268, 22733-22736.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22733-22736
    • Otani, H.1    Erdos, M.2    Leonard, W.J.3
  • 35
    • 0028175838 scopus 로고
    • Interleukin-1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity
    • Perregaux, D., & Gabel, C. A. (1994) Interleukin-1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity. J. Biol. Chem. 269, 15195-15203.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15195-15203
    • Perregaux, D.1    Gabel, C.A.2
  • 36
    • 0029790234 scopus 로고    scopus 로고
    • Attenuation of β-amyloid neurotoxicity in vitro by potassium-induced depolarization
    • Pike, C. J., Balázs, R., & Cotman, C. W. (1996) Attenuation of β-amyloid neurotoxicity in vitro by potassium-induced depolarization. J. Neurochem. 67, 1774-1777.
    • (1996) J. Neurochem. , vol.67 , pp. 1774-1777
    • Pike, C.J.1    Balázs, R.2    Cotman, C.W.3
  • 37
    • 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., & 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
  • 38
    • 0001884447 scopus 로고
    • Cytotoxicity in murine neocortical cell culture
    • C. A. Tyson & J. M. Frazier, Eds., Academic Press, San Diego
    • Rose, K., Goldberg, M. P., & Choi, D. W. (1993) Cytotoxicity in murine neocortical cell culture. In: Methods in Toxicology (C. A. Tyson & J. M. Frazier, Eds.), pp. 46-60. Academic Press, San Diego.
    • (1993) Methods in Toxicology , pp. 46-60
    • Rose, K.1    Goldberg, M.P.2    Choi, D.W.3
  • 39
    • 0026782205 scopus 로고
    • Voltage-dependent block of fast chloride channels from rat cortical neurons by external tetraethylammonium ion
    • Sanchez, D. Y., & Blatz, A. L. (1992) Voltage-dependent block of fast chloride channels from rat cortical neurons by external tetraethylammonium ion. J. Gen. Physiol. 100, 217-231.
    • (1992) J. Gen. Physiol. , vol.100 , pp. 217-231
    • Sanchez, D.Y.1    Blatz, A.L.2
  • 40
    • 0027166738 scopus 로고
    • Amyloid β peptides act directly on single neurons
    • Simmons, M. A., & Schneider, C. R. (1993) Amyloid β peptides act directly on single neurons. Neurosci. Lett. 150, 133-136.
    • (1993) Neurosci. Lett. , vol.150 , pp. 133-136
    • Simmons, M.A.1    Schneider, C.R.2
  • 42
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su, J. H., Anderson, A. J., Cummings, B. J., & Cotman, C. W. (1994) Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 5, 2529-2533.
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 43
    • 0026494972 scopus 로고
    • Epidermal growth factor and basic fibroblast growth factor suppress the spontaneous onset of apoptosis in cultured rat ovarian granulosa cells and follicles by a tyrosine kinase-dependent mechanism
    • Tilly, J. L., Billig, H., Kowalski, K. I., & Hsueh, A. J. (1992) Epidermal growth factor and basic fibroblast growth factor suppress the spontaneous onset of apoptosis in cultured rat ovarian granulosa cells and follicles by a tyrosine kinase-dependent mechanism. Mol. Endocrinol. 6, 1942-1950.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1942-1950
    • Tilly, J.L.1    Billig, H.2    Kowalski, K.I.3    Hsueh, A.J.4
  • 44
    • 0028989337 scopus 로고
    • Potassium-inhibited processing of IL-1β in human monocytes
    • Walev, I., Reske, K., Palmer, M., Valeva, A., & Bhakdi, S. (1995) Potassium-inhibited processing of IL-1β in human monocytes. EMBO J. 14, 1607-1614.
    • (1995) EMBO J. , vol.14 , pp. 1607-1614
    • Walev, I.1    Reske, K.2    Palmer, M.3    Valeva, A.4    Bhakdi, S.5
  • 45
    • 0028171547 scopus 로고
    • Ultrastructural analysis of β-amyloid-induced apoptosis in cultured hippocampal neurons
    • Watt, J. A., Pike, C. J., Walencewicz-Wasserman, A. J., & Cotman, C. W. (1994) Ultrastructural analysis of β-amyloid-induced apoptosis in cultured hippocampal neurons. Brain Res. 661, 147-156.
    • (1994) Brain Res. , vol.661 , pp. 147-156
    • Watt, J.A.1    Pike, C.J.2    Walencewicz-Wasserman, A.J.3    Cotman, C.W.4
  • 46
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate beta-amyloid peptide toxicity to cortical neurons in culture
    • 2+ channel blockers attenuate beta-amyloid peptide toxicity to cortical neurons in culture. J. Neurochem. 62, 372-375.
    • (1994) J. Neurochem. , vol.62 , pp. 372-375
    • Weiss, J.H.1    Pike, C.J.2    Cotman, C.W.3
  • 48
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides. Science 250, 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 51
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M., & Horvitz, H. R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzyme. Cell 75, 641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5


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