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Volumn 69, Issue 3, 1997, Pages 1177-1184

The amyloid β-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells

Author keywords

Acetylcholinesterase; Alzheimer's disease; Amyloid protein; Cyclic AMP; Voltage dependent calcium channel

Indexed keywords

ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; DILTIAZEM; FORSKOLIN; NIFEDIPINE; PROTEIN KINASE; VERAPAMIL;

EID: 1842375103     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69031177.x     Document Type: Article
Times cited : (120)

References (72)
  • 1
    • 0028947093 scopus 로고
    • Pharmacology of memory: Cholinergic-glutamatergic interactions
    • Aigner T. G. (1995) Pharmacology of memory: cholinergic-glutamatergic interactions. Curr. Opin. Neurobiol. 5, 155-160.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 155-160
    • Aigner, T.G.1
  • 2
    • 0040613702 scopus 로고
    • Voltage activated calcium channels that must be phosphorylated to respond to membrane depolarisation
    • Armstrong D. and Ekert R. (1987) Voltage activated calcium channels that must be phosphorylated to respond to membrane depolarisation. Proc. Natl. Acad. Sci. USA 84, 2518-2522.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2518-2522
    • Armstrong, D.1    Ekert, R.2
  • 3
    • 0020545113 scopus 로고
    • Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: Selective loss of the intermediate (10S) form
    • Atack J. R., Perry E. K., Bonham J. R., Perry R. H., Tomlinson B. E., Blessed G., and Fairbairn A. (1983) Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: selective loss of the intermediate (10S) form. Neurosci. Lett. 40, 199-204.
    • (1983) Neurosci. Lett. , vol.40 , pp. 199-204
    • Atack, J.R.1    Perry, E.K.2    Bonham, J.R.3    Perry, R.H.4    Tomlinson, B.E.5    Blessed, G.6    Fairbairn, A.7
  • 4
    • 0024554076 scopus 로고
    • Classes of calcium channels in vertebrate cells
    • Bean B. P. (1989) Classes of calcium channels in vertebrate cells. Annu. Rev. Physiol. 51, 367-384.
    • (1989) Annu. Rev. Physiol. , vol.51 , pp. 367-384
    • Bean, B.P.1
  • 5
    • 0023899578 scopus 로고
    • Mechanism of cholinesterase inhibition in senile dementia of the Alzheimer's type: Clinical, pharmacological and therapeutic aspects
    • Becker R. E. and Giacobini E. (1988) Mechanism of cholinesterase inhibition in senile dementia of the Alzheimer's type: clinical, pharmacological and therapeutic aspects. Drug Dev. Res. 12, 163-195.
    • (1988) Drug Dev. Res. , vol.12 , pp. 163-195
    • Becker, R.E.1    Giacobini, E.2
  • 6
    • 0029360450 scopus 로고
    • Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice
    • Beeri R., Andres C., Lev-Lehman E., Timberg R., Huberman T., Shani M., and Soreq H. (1995) Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice. Curr. Biol. 5, 1063-1071.
    • (1995) Curr. Biol. , vol.5 , pp. 1063-1071
    • Beeri, R.1    Andres, C.2    Lev-Lehman, E.3    Timberg, R.4    Huberman, T.5    Shani, M.6    Soreq, H.7
  • 7
    • 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
  • 8
    • 0029553116 scopus 로고
    • Acetylcholine: A neurotransmitter for learning and memory?
    • Blokland A. (1995) Acetylcholine: a neurotransmitter for learning and memory? Brain Res. Rev. 21, 285-300.
    • (1995) Brain Res. Rev. , vol.21 , pp. 285-300
    • Blokland, A.1
  • 9
    • 0027180087 scopus 로고
    • Extracellular matrix components and amyloid in neuritic plaques of the Alzheimer's disease
    • Brandon E. and Inestrosa N. C. (1993) Extracellular matrix components and amyloid in neuritic plaques of the Alzheimer's disease. Gen. Pharmacol. 24, 1063-1068.
    • (1993) Gen. Pharmacol. , vol.24 , pp. 1063-1068
    • Brandon, E.1    Inestrosa, N.C.2
  • 11
    • 0025833592 scopus 로고
    • Calcium and ionophore A23187 stimulates deposition of extracellular matrix and acetylcholinesterase release in cultured myotubes
    • Bursztajn S., Schneider L. W., Jong Y.-J., and Berman S. A. (1991) Calcium and ionophore A23187 stimulates deposition of extracellular matrix and acetylcholinesterase release in cultured myotubes. Cell Tissue Res. 265, 95-103.
    • (1991) Cell Tissue Res. , vol.265 , pp. 95-103
    • Bursztajn, S.1    Schneider, L.W.2    Jong, Y.-J.3    Berman, S.A.4
  • 12
    • 0025815779 scopus 로고
    • Differentiation of a stem cell line toward a neuronal phenotype
    • Cheun J. E. and Yeh H. H. (1991) Differentiation of a stem cell line toward a neuronal phenotype. Int. J. Dev. Neurosci. 9, 391-404.
    • (1991) Int. J. Dev. Neurosci. , vol.9 , pp. 391-404
    • Cheun, J.E.1    Yeh, H.H.2
  • 13
    • 0030028223 scopus 로고    scopus 로고
    • Regulation of acetylcholinesterase expression during neuronal differentiation
    • Coleman B. A. and Taylor P. (1996) Regulation of acetylcholinesterase expression during neuronal differentiation. J. Biol. Chem. 271, 4410-4416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4410-4416
    • Coleman, B.A.1    Taylor, P.2
  • 14
    • 0028178530 scopus 로고
    • Amyloid β-peptide (AβP) potentiates a nimodipine-sensitive L-type barium conductance in N1E-115 neuroblastoma cells
    • Davidson R. M., Shajenko L., and Donta T. S. (1994) Amyloid β-peptide (AβP) potentiates a nimodipine-sensitive L-type barium conductance in N1E-115 neuroblastoma cells. Brain Res. 643, 324-327.
    • (1994) Brain Res. , vol.643 , pp. 324-327
    • Davidson, R.M.1    Shajenko, L.2    Donta, T.S.3
  • 15
    • 0011162190 scopus 로고
    • Selective loss of central cholinergic neurons in Alzheimer's disease
    • Davies P. and Maloney A. J. F. (1976) Selective loss of central cholinergic neurons in Alzheimer's disease. Lancet ii, 1403.
    • (1976) Lancet , vol.2 , pp. 1403
    • Davies, P.1    Maloney, A.J.F.2
  • 16
    • 0025362490 scopus 로고
    • Dihydropyridine receptor regulation of acetylcholinesterase
    • Decker M. M. and Berman H. A. (1990) Dihydropyridine receptor regulation of acetylcholinesterase. J. Biol. Chem. 265, 11796-11803.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11796-11803
    • Decker, M.M.1    Berman, H.A.2
  • 18
    • 0028247930 scopus 로고
    • Alzheimer's disease amyloid precursor protein ( AβPP): Proteolytic processing, secretases and βA4 amyloid production
    • Evin G., Beyreuther K., and Masters C. L. (1994) Alzheimer's disease amyloid precursor protein ( AβPP): proteolytic processing, secretases and βA4 amyloid production. Amyloid: Int. J. Exp. Clin. Invest. 1, 263-280.
    • (1994) Amyloid: Int. J. Exp. Clin. Invest. , vol.1 , pp. 263-280
    • Evin, G.1    Beyreuther, K.2    Masters, C.L.3
  • 19
    • 0022616905 scopus 로고
    • Distribution of the molecular forms of acetylcholinesterase in human brain: Alterations in dementia of the Alzheimer type
    • Fishman E. B., Siek G. C., MacCallum R. D., Bird E. D., Volicer L., and Marquis J. K. (1986) Distribution of the molecular forms of acetylcholinesterase in human brain: alterations in dementia of the Alzheimer type. Ann. Neurol. 19, 246-252.
    • (1986) Ann. Neurol. , vol.19 , pp. 246-252
    • Fishman, E.B.1    Siek, G.C.2    MacCallum, R.D.3    Bird, E.D.4    Volicer, L.5    Marquis, J.K.6
  • 20
    • 0027186334 scopus 로고
    • The cerebrospinal fluid soluble form of Alzheimer's amyloid β is complexed to sp40, 40 (ApoJ), an inhibitor of the complement membrane attack complex
    • Ghiso J., Matsubara E., Koudinov A., Wisneiwski T., and Frangione B. (1993) The cerebrospinal fluid soluble form of Alzheimer's amyloid β is complexed to sp40, 40 (ApoJ), an inhibitor of the complement membrane attack complex. Biochem. J. 293, 27-30.
    • (1993) Biochem. J. , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Wisneiwski, T.4    Frangione, B.5
  • 21
    • 0027198392 scopus 로고
    • Differential phosphorylation of two size forms of the neuronal class C L-type calcium channel alpha 1 subunit
    • Hell J. W., Yokoyama C. T., Wong S. T., Warner C., Snutch T. P., and Catterall W. A. (1993) Differential phosphorylation of two size forms of the neuronal class C L-type calcium channel alpha 1 subunit. J. Biol. Chem. 268, 19451-19457.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19451-19457
    • Hell, J.W.1    Yokoyama, C.T.2    Wong, S.T.3    Warner, C.4    Snutch, T.P.5    Catterall, W.A.6
  • 22
    • 0025734549 scopus 로고
    • Human and rodent sequence analogs of Alzheimer's amyloid βA4 share similar properties and can be solubilized in buffers of pH 7.4
    • Hilbich C., Kisters-Woike B., Reed J., Masters C. L., and Beyreuther K. (1991) Human and rodent sequence analogs of Alzheimer's amyloid βA4 share similar properties and can be solubilized in buffers of pH 7.4. Eur. J. Biochem. 201, 61-69.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 61-69
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 23
    • 0027362505 scopus 로고
    • Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during development in vivo
    • Houenou L. J., Sahuqué M. V., and Villageois A. P. (1993) Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during development in vivo. Cell. Mol. Neurobiol. 13, 217-232.
    • (1993) Cell. Mol. Neurobiol. , vol.13 , pp. 217-232
    • Houenou, L.J.1    Sahuqué, M.V.2    Villageois, A.P.3
  • 24
    • 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 N. C., Alvarez A., Perez C. A., Moreno R. D., Vicente M., Linker C., Casanueva O. I., Soto C., and 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    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 25
    • 0020326857 scopus 로고
    • Retinoic acid induces embryonal carcinoma cells to differentiate into neurons and glial cells
    • Jones-Villeneuve E. M. V., McBurney M. W., Rogers K. A., and Kalnins V. I. (1982) Retinoic acid induces embryonal carcinoma cells to differentiate into neurons and glial cells. J. Cell Biol. 94, 253-262.
    • (1982) J. Cell Biol. , vol.94 , pp. 253-262
    • Jones-Villeneuve, E.M.V.1    McBurney, M.W.2    Rogers, K.A.3    Kalnins, V.I.4
  • 26
    • 0026778186 scopus 로고
    • Amyloid β-protein fragment 25-35 causes activation of cytoplasmic calcium in neurons
    • Joseph R. and Han E. (1992) Amyloid β-protein fragment 25-35 causes activation of cytoplasmic calcium in neurons. Biochem. Biophys. Res. Commun. 184, 1441-1447.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1441-1447
    • Joseph, R.1    Han, E.2
  • 27
    • 0025905126 scopus 로고
    • Widespread amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders
    • Kalaria R. N., Galloway P. G., and Perry G. (1991) Widespread amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders. Neuropathol. Appl. Neurobiol. 17, 189-201.
    • (1991) Neuropathol. Appl. Neurobiol. , vol.17 , pp. 189-201
    • Kalaria, R.N.1    Galloway, P.G.2    Perry, G.3
  • 29
    • 0025125815 scopus 로고
    • Modulation of intracellular cyclic adenosine monophosphate levels and the differentiation response of human neuroblastoma cells
    • Lando M., Abemayor E., Verity A., and Sidell N. (1990) Modulation of intracellular cyclic adenosine monophosphate levels and the differentiation response of human neuroblastoma cells. Cancer Res. 50, 722-727.
    • (1990) Cancer Res. , vol.50 , pp. 722-727
    • Lando, M.1    Abemayor, E.2    Verity, A.3    Sidell, N.4
  • 31
    • 0028063039 scopus 로고
    • Regulation of acetylcholinesterase mRNA stability by calcium during differentiation from myoblasts to myotubes
    • Luo Z., Fuentes M.-E., and Taylor P. (1994) Regulation of acetylcholinesterase mRNA stability by calcium during differentiation from myoblasts to myotubes. J. Biol. Chem. 269, 27216-27223.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27216-27223
    • Luo, Z.1    Fuentes, M.-E.2    Taylor, P.3
  • 32
    • 0029931262 scopus 로고    scopus 로고
    • Acetylcholinesterase and nicotinic acetylcholine receptor expression diverge in muscular dysgenic mice lacking the L-type calcium channel
    • Luo D. Z., Pincon-Raymond M., and Taylor P. (1996) Acetylcholinesterase and nicotinic acetylcholine receptor expression diverge in muscular dysgenic mice lacking the L-type calcium channel. J. Neurochem. 67, 111-118.
    • (1996) J. Neurochem. , vol.67 , pp. 111-118
    • Luo, D.Z.1    Pincon-Raymond, M.2    Taylor, P.3
  • 33
    • 0028173205 scopus 로고
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature 372, 92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 35
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson M. P. and Goodman Y. (1995) Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res. 676, 219-224.
    • (1995) Brain Res. , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 36
    • 0030598110 scopus 로고    scopus 로고
    • Alzheimer's disease - Amyloid ox-tox transducers
    • Mattson M. P. and Rydel R. E. (1996) Alzheimer's disease - amyloid ox-tox transducers. Nature 382, 674-675.
    • (1996) Nature , vol.382 , pp. 674-675
    • Mattson, M.P.1    Rydel, R.E.2
  • 37
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilise 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 destabilise 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
  • 38
    • 0027297138 scopus 로고
    • Calcium-destabilising and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson M. P., Tomaselli K. J., and Rydel R. E. (1993) Calcium-destabilising 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.J.2    Rydel, R.E.3
  • 39
    • 0023836804 scopus 로고
    • Differentiation and maturation of embryonal carcinoma-derived neurons in cell culture
    • McBurney M. W., Reuhl K. R., Ally A. I., Nasipuri S., Bell J. C., and Craig J. (1988) Differentiation and maturation of embryonal carcinoma-derived neurons in cell culture. J. Neurosci. 8, 1063-1073.
    • (1988) J. Neurosci. , vol.8 , pp. 1063-1073
    • McBurney, M.W.1    Reuhl, K.R.2    Ally, A.I.3    Nasipuri, S.4    Bell, J.C.5    Craig, J.6
  • 40
    • 0021341974 scopus 로고
    • 2+ release in sarcoplasmic reticulum
    • 2+ release in sarcoplasmic reticulum. J. Biol. Chem. 259, 2365-2374.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2365-2374
    • Meissner, G.1
  • 41
    • 0026729258 scopus 로고
    • Maitotoxin-induced intracellular calcium rise in PC12 cells: Involvement of dihydropyridine-sensitive and ω-conotoxin-sensitive calcium channels and phosphoinositide breakdown
    • Meucci O., Grimaldi M., Scorziello A., Govoni S., Bergamaschi S., Yasumoto T., and Schettini G. (1992) Maitotoxin-induced intracellular calcium rise in PC12 cells: involvement of dihydropyridine-sensitive and ω-conotoxin-sensitive calcium channels and phosphoinositide breakdown. J. Neurochem. 59, 679-688.
    • (1992) J. Neurochem. , vol.59 , pp. 679-688
    • Meucci, O.1    Grimaldi, M.2    Scorziello, A.3    Govoni, S.4    Bergamaschi, S.5    Yasumoto, T.6    Schettini, G.7
  • 43
    • 0020317866 scopus 로고
    • Mechanism of calcium release from skeletal sarcoplasmic reticulum
    • Miyamoto H. and Racker E. J. (1982) Mechanism of calcium release from skeletal sarcoplasmic reticulum. Membr. Biol. 66, 193-201.
    • (1982) Membr. Biol. , vol.66 , pp. 193-201
    • Miyamoto, H.1    Racker, E.J.2
  • 44
    • 0027514286 scopus 로고
    • Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains
    • Morán M. A., Mufson E. J., and Gómez-Ramos P. (1993) Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains. Acta Neuropathol. 85, 362-369.
    • (1993) Acta Neuropathol. , vol.85 , pp. 362-369
    • Morán, M.A.1    Mufson, E.J.2    Gómez-Ramos, P.3
  • 45
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch R. M., Slack B. E., Wurtman R. J., and Growdon J. H. (1992) Release of Alzheimer amyloid precursor stimulated by activation of muscarinic acetylcholine receptors. Science 258, 304-307.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 46
    • 0029795254 scopus 로고    scopus 로고
    • Amyloid β-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain
    • Pederson W. A., Kloczewiak M. A., and Blusztajn J. K. (1996) Amyloid β-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain. Proc. Natl. Acad. Sci. USA 93, 8068-8071.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8068-8071
    • Pederson, W.A.1    Kloczewiak, M.A.2    Blusztajn, J.K.3
  • 47
    • 0028212976 scopus 로고
    • Regulation of the cloned L-type cardiac calcium channel by cyclic-AMP-dependent protein kinase
    • Perez-Reyes E., Yuan W., Wei X., and Bers D. M. (1994) Regulation of the cloned L-type cardiac calcium channel by cyclic-AMP-dependent protein kinase. FEBS Lett. 342, 119-123.
    • (1994) FEBS Lett. , vol.342 , pp. 119-123
    • Perez-Reyes, E.1    Yuan, W.2    Wei, X.3    Bers, D.M.4
  • 48
    • 0027402763 scopus 로고
    • Ryanodine induces maturation of embryonic acetylcholinesterase forms in cultured quail myotubules
    • Pessah I. N., Nieberg P. S., and Wilson B. W. (1993) Ryanodine induces maturation of embryonic acetylcholinesterase forms in cultured quail myotubules. Life Sci. 52, 1279-1285.
    • (1993) Life Sci. , vol.52 , pp. 1279-1285
    • Pessah, I.N.1    Nieberg, P.S.2    Wilson, B.W.3
  • 49
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli F., Castaño E., Glenner G. G., and Frangione B. (1988) Differences between vascular and plaque core amyloid in Alzheimer's disease. J. Neurochem. 51, 648-651.
    • (1988) J. Neurochem. , vol.51 , pp. 648-651
    • Prelli, F.1    Castaño, E.2    Glenner, G.G.3    Frangione, B.4
  • 50
    • 0029560730 scopus 로고
    • Thyroid hormones stabilise acetylcholinesterase mRNA in Neuro-2A cells that overexpress the β1 thyroid receptor
    • Puymirat J., Etongue-Mayer P., and Dussault J. H. (1995) Thyroid hormones stabilise acetylcholinesterase mRNA in Neuro-2A cells that overexpress the β1 thyroid receptor. J. Biol. Chem. 270, 30651-30656.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30651-30656
    • Puymirat, J.1    Etongue-Mayer, P.2    Dussault, J.H.3
  • 51
    • 0029022334 scopus 로고
    • Sites of selective cAMP-dependent phosphorylation of the L-type calcium channel alpha 1 subunit from intact rabbit skeletal muscle myotubes
    • Rotman E. I., Murphy B. J., and Catterall W. A. (1995) Sites of selective cAMP-dependent phosphorylation of the L-type calcium channel alpha 1 subunit from intact rabbit skeletal muscle myotubes. J. Biol. Chem. 270, 16371-16377.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16371-16377
    • Rotman, E.I.1    Murphy, B.J.2    Catterall, W.A.3
  • 52
    • 0022135418 scopus 로고
    • 2+ mediate changes in acetylcholinesterase and acetylcholine receptors caused by muscle contraction
    • 2+ mediate changes in acetylcholinesterase and acetylcholine receptors caused by muscle contraction. Proc. Natl. Acad. Sci. USA 82, 7121-7125.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7121-7125
    • Rubin, L.L.1
  • 53
    • 0002131730 scopus 로고
    • Cell culture methods and induction of differentiation of embryonal carcinoma cell lines
    • Robertson E. J., ed, IRL Press, Washington, D.C.
    • Rudnicki M. A. and McBurney M. W. (1987) Cell culture methods and induction of differentiation of embryonal carcinoma cell lines, in Teratocarcinomas and Embryonic Stem Cells: A Practical Approach (Robertson E. J., ed), pp. 19-50. IRL Press, Washington, D.C.
    • (1987) Teratocarcinomas and Embryonic Stem Cells: A Practical Approach , pp. 19-50
    • Rudnicki, M.A.1    McBurney, M.W.2
  • 54
    • 0027425580 scopus 로고
    • Voltage-dependent potentiation of the activity of cardiac L-type calcium channel alpha 1 subunits due to phosphorylation by cAMP-dependent protein kinase
    • Sculptoreanu A., Rotman E., Takahashi M., Scheuer T., and Catterall W. A. (1993) Voltage-dependent potentiation of the activity of cardiac L-type calcium channel alpha 1 subunits due to phosphorylation by cAMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA 90, 10135-10139.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10135-10139
    • Sculptoreanu, A.1    Rotman, E.2    Takahashi, M.3    Scheuer, T.4    Catterall, W.A.5
  • 55
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman M. S., Ragan C. I., and Iversen L. L. (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
  • 56
    • 0029897490 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • Small D. H., Michaelson S., and Sberna G. (1996) Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem. Int. 28, 453-483.
    • (1996) Neurochem. Int. , vol.28 , pp. 453-483
    • Small, D.H.1    Michaelson, S.2    Sberna, G.3
  • 58
    • 0024273721 scopus 로고
    • The presence of heparan sulfate proteoglycan in the neuritic plaques and congophilic angiopathy in Alzheimer's disease
    • Snow A. D., Mar H., Nochlin D., Kimata K., Kato M., Suzuki S., Hassel J., and Wight T. N. (1988) The presence of heparan sulfate proteoglycan in the neuritic plaques and congophilic angiopathy in Alzheimer's disease. Am. J. Pathol. 133, 456-463.
    • (1988) Am. J. Pathol. , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimata, K.4    Kato, M.5    Suzuki, S.6    Hassel, J.7    Wight, T.N.8
  • 59
    • 0022899577 scopus 로고
    • Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type
    • Summers W. K., Majovski L. V., Marsh G. M., Tachiki K., and Kling A. (1986) Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type. N. Engl. J. Med. 315, 1241-1245.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 1241-1245
    • Summers, W.K.1    Majovski, L.V.2    Marsh, G.M.3    Tachiki, K.4    Kling, A.5
  • 61
    • 0002052586 scopus 로고
    • The use of fluorescent indicators for measurements of cytosolic-free calcium concentration in cell populations and single cells
    • McCormack J. G. and Cobbold P. H., eds, IRL Press, Oxford, U.K.
    • Thomas A. P. and Delaville F. (1991) The use of fluorescent indicators for measurements of cytosolic-free calcium concentration in cell populations and single cells, in Cellular Calcium. A Practical Approach (McCormack J. G. and Cobbold P. H., eds), pp. 1-54. IRL Press, Oxford, U.K.
    • (1991) Cellular Calcium. A Practical Approach , pp. 1-54
    • Thomas, A.P.1    Delaville, F.2
  • 63
    • 0025000725 scopus 로고
    • Senile plaques: Staining for acetylcholinesterase and A4 protein: a comparative study in the hippocampus and entorhinal cortex
    • Ulrich J., Meier-Ruge W., Probst A., Meier E., and Ipsen S. (1990) Senile plaques: staining for acetylcholinesterase and A4 protein: a comparative study in the hippocampus and entorhinal cortex. Acta Neuropathol. 80, 624-628.
    • (1990) Acta Neuropathol. , vol.80 , pp. 624-628
    • Ulrich, J.1    Meier-Ruge, W.2    Probst, A.3    Meier, E.4    Ipsen, S.5
  • 64
    • 0030601311 scopus 로고    scopus 로고
    • cAMP effects on myogenic gene expression in rhabdomyosarcoma cells
    • Wasserman L. M., Newsham I., Huang H. J. S., and Cavenee W. K. (1996) cAMP effects on myogenic gene expression in rhabdomyosarcoma cells. Exp. Cell Res. 227, 55-62.
    • (1996) Exp. Cell Res. , vol.227 , pp. 55-62
    • Wasserman, L.M.1    Newsham, I.2    Huang, H.J.S.3    Cavenee, W.K.4
  • 65
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurons in culture
    • 2+ channel blockers attenuate β-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
  • 66
    • 0028981561 scopus 로고
    • Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade
    • Whitson J. S. and Appel S. H. (1995) Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade. Neurobiol. Aging 16, 5-10.
    • (1995) Neurobiol. Aging , vol.16 , pp. 5-10
    • Whitson, J.S.1    Appel, S.H.2
  • 67
    • 0029152729 scopus 로고
    • Essential role of neocortical acetylcholine in spatial memory
    • Winkler J., Suhr S. T., Gage F. H., Thal L. J., and Fisher L. J. (1995) Essential role of neocortical acetylcholine in spatial memory. Nature 375, 484-487.
    • (1995) Nature , vol.375 , pp. 484-487
    • Winkler, J.1    Suhr, S.T.2    Gage, F.H.3    Thal, L.J.4    Fisher, L.J.5
  • 68
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T. and Frangione B. (1992) Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci. Lett. 135, 235-238.
    • (1992) Neurosci. Lett. , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 69
    • 0026974904 scopus 로고
    • An endogenous membranebound protein inhibits the phosphorylation of the L-type calcium channel by the cAMP-dependent protein kinase
    • Woscholski R. and Marme D. (1992) An endogenous membranebound protein inhibits the phosphorylation of the L-type calcium channel by the cAMP-dependent protein kinase. Biochem. Biophys. Res. Commun. 186, 1588-1593.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1588-1593
    • Woscholski, R.1    Marme, D.2
  • 71
    • 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
  • 72
    • 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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