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Volumn 106, Issue 3, 2008, Pages 1092-1103

CaM kinase II and protein kinase C activations mediate enhancement of long-term potentiation by nefiracetam in the rat hippocampal CA1 region

Author keywords

Alzheimer's disease; Calcium calmodulin dependent protein kinase II; Long term potentiation; N methyl D aspartate acid; Nefiracetam; Protein kinase C

Indexed keywords

AMPA RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEFIRACETAM; NICOTINIC RECEPTOR; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN KINASE C ALPHA; SYNAPTOPHYSIN;

EID: 48249090845     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05440.x     Document Type: Article
Times cited : (33)

References (47)
  • 1
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptor by CaM-KII during long-term potentiation
    • Barria A., Muller D., Derkach V., Griffith L. C. Soderling T. R. (1997) Regulatory phosphorylation of AMPA-type glutamate receptor by CaM-KII during long-term potentiation. Science 276, 2042 2045.
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 3
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss T. V. Collingridge G. L. (1993) A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31 39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 4
    • 0032588030 scopus 로고    scopus 로고
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • 2+/calmodulin- kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionate type glutamate receptors. Proc. Natl Acad. Sci. USA 96, 3269 3274.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 5
    • 0026631288 scopus 로고
    • Milacemide; A placebo-controlled study in senile dementia of the Alzheimer type
    • Dysken M. W., Mendels J. LeWitt P. (1992) Milacemide; a placebo-controlled study in senile dementia of the Alzheimer type. Am. J. Geriatr. Psychiatry 40, 503 506.
    • (1992) Am. J. Geriatr. Psychiatry , vol.40 , pp. 503-506
    • Dysken, M.W.1    Mendels, J.2    Lewitt, P.3
  • 6
    • 0036173960 scopus 로고    scopus 로고
    • Antagonistic effects of dopaminergic signaling and ethanol on protein kinase A-mediated phosphorylation of DARPP-32 and the NR1 subunit of the NMDA receptor
    • Edwards S., Simmons D. L., Galindo D. G., Doherty J. M., Scott A. M., Hughes P. D. Wilcox R. E. (2002) Antagonistic effects of dopaminergic signaling and ethanol on protein kinase A-mediated phosphorylation of DARPP-32 and the NR1 subunit of the NMDA receptor. Alcoholism 26, 173 180.
    • (2002) Alcoholism , vol.26 , pp. 173-180
    • Edwards, S.1    Simmons, D.L.2    Galindo, D.G.3    Doherty, J.M.4    Scott, A.M.5    Hughes, P.D.6    Wilcox, R.E.7
  • 7
    • 0027203084 scopus 로고
    • Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons
    • Fley U., Huang Y. Y. Kandel E. R. (1993) Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science 260, 1661 1664.
    • (1993) Science , vol.260 , pp. 1661-1664
    • Fley, U.1    Huang, Y.Y.2    Kandel, E.R.3
  • 8
    • 0034282008 scopus 로고    scopus 로고
    • A working model of CaM Kinase II activity in hippocampal long-term potentiation and memory
    • Fukunaga K. Miyamoto E. (2000) A working model of CaM Kinase II activity in hippocampal long-term potentiation and memory. Neurosci. Res. 38, 3 17.
    • (2000) Neurosci. Res. , vol.38 , pp. 3-17
    • Fukunaga, K.1    Miyamoto, E.2
  • 9
    • 0023819387 scopus 로고
    • 2+/calmodulin-dependent protein kinase II in rat brain and various tissues
    • 2+/calmodulin-dependent protein kinase II in rat brain and various tissues. J. Neurochem. 51, 1070 1078.
    • (1988) J. Neurochem. , vol.51 , pp. 1070-1078
    • Fukunaga, K.1    Goto, S.2    Miyamoto, E.3
  • 10
    • 0026613087 scopus 로고
    • 2+/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured rat hippocampal neurons
    • 2+/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured rat hippocampal neurons. J. Biol. Chem. 267, 22527 22533.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22527-22533
    • Fukunaga, K.1    Soderling, T.R.2    Miyamoto, E.3
  • 12
    • 0028988308 scopus 로고
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long term potentiation
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long term potentiation. J. Biol. Chem. 270, 6119 6124.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6119-6124
    • Fukunaga, K.1    Muller, D.2    Miyamoto, E.3
  • 13
    • 0034082560 scopus 로고    scopus 로고
    • Cholinesterase inhibitor therapy stabilizes symptoms of Alzheimer's disease
    • Giacobini E. (2000) Cholinesterase inhibitor therapy stabilizes symptoms of Alzheimer's disease. Alzheimer Dis. Assoc. Disorders 14 (Suppl. 1 S3 S10.
    • (2000) Alzheimer Dis. Assoc. Disorders , vol.14 , Issue.1
    • Giacobini, E.1
  • 15
    • 0024849434 scopus 로고
    • Milacemide, a glycine prodrug, enhances performance of learning tasks in normal and amnestic reodents
    • Hanndelmann G. E., Nevins M. E., Mueller L. L., Arnolde S. M. Cordi A. A. (1989) Milacemide, a glycine prodrug, enhances performance of learning tasks in normal and amnestic reodents. Pharmacol. Biochem. Behav. 34, 823 828.
    • (1989) Pharmacol. Biochem. Behav. , vol.34 , pp. 823-828
    • Hanndelmann, G.E.1    Nevins, M.E.2    Mueller, L.L.3    Arnolde, S.M.4    Cordi, A.A.5
  • 16
    • 0028846262 scopus 로고
    • Isozyme specific changes in the expression of protein kinase C isozyme (alpha-zeta) genes in the hippocampus of rats induced by kindling epileptogenesis
    • Kamphuis W., Hendriksen E. Lopes da Silva F. H. (1995) Isozyme specific changes in the expression of protein kinase C isozyme (alpha-zeta) genes in the hippocampus of rats induced by kindling epileptogenesis. Brain Res. 702, 94 100.
    • (1995) Brain Res. , vol.702 , pp. 94-100
    • Kamphuis, W.1    Hendriksen, E.2    Lopes Da Silva, F.H.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioral memory
    • Lisman J., Schulman H. Cline H. (2002) The molecular basis of CaMKII function in synaptic and behavioral memory. Nat. Rev. Neurosci. 3, 175 190.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 19
    • 0033216276 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II and mitogen-activated protein kinase activation in hippocampal long-term potentiation
    • 2+/calmodulin-dependent protein kinase II and mitogen-activated protein kinase activation in hippocampal long-term potentiation. J. Neurosci. 19, 8292 8299.
    • (1999) J. Neurosci. , vol.19 , pp. 8292-8299
    • Liu, J.1    Fukunaga, K.2    Yamamoto, H.3    Nishi, K.4    Miyamoto, E.5
  • 20
    • 0028880861 scopus 로고
    • Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo P. M., Hjelmstad G. O., Mukherji S., Soderling T. R., Malenka R. C. Nicoll R. A. (1995) Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc. Natl Acad. Sci. USA 92, 11175 11179.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11175-11179
    • Lledo, P.M.1    Hjelmstad, G.O.2    Mukherji, S.3    Soderling, T.R.4    Malenka, R.C.5    Nicoll, R.A.6
  • 21
    • 0023633194 scopus 로고
    • Protein kinase C inhibitors eliminate hippocampal long-term potentiation
    • Lovinger D. M., Wong K. L., Murakami K. Routtenberg A. (1987) Protein kinase C inhibitors eliminate hippocampal long-term potentiation. Brain Res. 436, 177 183.
    • (1987) Brain Res. , vol.436 , pp. 177-183
    • Lovinger, D.M.1    Wong, K.L.2    Murakami, K.3    Routtenberg, A.4
  • 22
    • 0025286701 scopus 로고
    • The nature and causes of hippocampal long-term potentiation
    • Lynch G., Kessler M., Arai A. Larson J. (1990) The nature and causes of hippocampal long-term potentiation. Prog. Brain Res. 83, 233 250.
    • (1990) Prog. Brain Res. , vol.83 , pp. 233-250
    • Lynch, G.1    Kessler, M.2    Arai, A.3    Larson, J.4
  • 23
    • 0034732104 scopus 로고    scopus 로고
    • Allosteric modulation of nicotinic acetylcholine receptors as a treatment strategy for Alzheimer's disease
    • Maelicke A. Albuquerque E. X. (2000) Allosteric modulation of nicotinic acetylcholine receptors as a treatment strategy for Alzheimer's disease. Eur. J. Pharmacol. 393, 165 170.
    • (2000) Eur. J. Pharmacol. , vol.393 , pp. 165-170
    • Maelicke, A.1    Albuquerque, E.X.2
  • 25
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation - A decade of progress?
    • Malenka R. C. Nicoll R. A. (1999) Long-term potentiation - a decade of progress? Science 285, 1870 1874.
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 26
    • 0031435496 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II
    • Mammen A. L., Kameyama K., Roche K. W. Huganir R. L. (1997) Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J. Biol. Chem. 272, 32528 32533.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32528-32533
    • Mammen, A.L.1    Kameyama, K.2    Roche, K.W.3    Huganir, R.L.4
  • 27
    • 0141742496 scopus 로고    scopus 로고
    • Potentiation of N-methyl-D-aspartate-induced currents by the nootropic drug nefiracetam in rat cortical neurons
    • Moriguchi S., Marszalec W., Zhao X., Yeh J. Z. Narahashi T. (2003) Potentiation of N-methyl-D-aspartate-induced currents by the nootropic drug nefiracetam in rat cortical neurons. J. Pharmacol. Exp. Ther. 307, 160 167.
    • (2003) J. Pharmacol. Exp. Ther. , vol.307 , pp. 160-167
    • Moriguchi, S.1    Marszalec, W.2    Zhao, X.3    Yeh, J.Z.4    Narahashi, T.5
  • 28
    • 4243072971 scopus 로고    scopus 로고
    • Mechanism of action of galantamine on N-methyl-D-aspartate receptors in rat cortical neurons
    • Moriguchi S., Marszalec W., Zhao X., Yeh J. Z. Narahashi T. (2004) Mechanism of action of galantamine on N-methyl-D-aspartate receptors in rat cortical neurons. J. Pharmacol. Exp. Ther. 310, 933 942.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 933-942
    • Moriguchi, S.1    Marszalec, W.2    Zhao, X.3    Yeh, J.Z.4    Narahashi, T.5
  • 29
    • 33846407216 scopus 로고    scopus 로고
    • Nefiracetam potentiates N-methyl-D-aspartate (NMDA) receptor function via protein kinase C activation and reduces magnesium block of NMDA receptor
    • Moriguchi S., Shioda N., Maejima H., Zhao X., Marszalec W., Yeh J. Z., Fukunaga K. Narahashi T. (2007) Nefiracetam potentiates N-methyl-D-aspartate (NMDA) receptor function via protein kinase C activation and reduces magnesium block of NMDA receptor. Mol. Pharmacol. 71, 580 587.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 580-587
    • Moriguchi, S.1    Shioda, N.2    Maejima, H.3    Zhao, X.4    Marszalec, W.5    Yeh, J.Z.6    Fukunaga, K.7    Narahashi, T.8
  • 30
    • 0027984961 scopus 로고
    • Ameliorating effects of nefiracetam (DM-9384) on brain dysfunction
    • Nabeshima T. (1994) Ameliorating effects of nefiracetam (DM-9384) on brain dysfunction. Drugs Today 30, 357 379.
    • (1994) Drugs Today , vol.30 , pp. 357-379
    • Nabeshima, T.1
  • 31
    • 0028207467 scopus 로고
    • Effects of nefiracetam on drug-induced impairment of latent learning in mice in a water finding task
    • Nabeshima T., Nakayama S., Ichihara K., Yamada K., Shiotani T. Hasegawa T. (1994) Effects of nefiracetam on drug-induced impairment of latent learning in mice in a water finding task. Eur. J. Pharmacol. 255, 57 65.
    • (1994) Eur. J. Pharmacol. , vol.255 , pp. 57-65
    • Nabeshima, T.1    Nakayama, S.2    Ichihara, K.3    Yamada, K.4    Shiotani, T.5    Hasegawa, T.6
  • 32
    • 0033134776 scopus 로고    scopus 로고
    • A 'long-term-potentiation-like' facilitation of hippocampal synaptic transmission induced by the nootropic nefiracetam
    • Nishizaki T., Matsuoka T., Nomura T., Matsuyama S., Watabe S., Shiotani T. Yoshii M. (1999) A 'long-term-potentiation-like' facilitation of hippocampal synaptic transmission induced by the nootropic nefiracetam. Brain Res. 826, 281 288.
    • (1999) Brain Res. , vol.826 , pp. 281-288
    • Nishizaki, T.1    Matsuoka, T.2    Nomura, T.3    Matsuyama, S.4    Watabe, S.5    Shiotani, T.6    Yoshii, M.7
  • 33
    • 0032898479 scopus 로고    scopus 로고
    • Phosphorylation of myristoylated alanine-rich protein kinase C substrate by mitogen-activated protein kinase in cultured rat hippocampal neurons following stimulation of glutamate receptors
    • Ohmitsu M., Fukunaga K., Yamamoto H. Miyamoto E. (1999) Phosphorylation of myristoylated alanine-rich protein kinase C substrate by mitogen-activated protein kinase in cultured rat hippocampal neurons following stimulation of glutamate receptors. J. Biol. Chem. 274, 408 417.
    • (1999) J. Biol. Chem. , vol.274 , pp. 408-417
    • Ohmitsu, M.1    Fukunaga, K.2    Yamamoto, H.3    Miyamoto, E.4
  • 34
    • 0030175899 scopus 로고    scopus 로고
    • Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
    • Roche K. W., O'Brien R. J., Mammen A. L., Bernhardt J. Huganir R. L. (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16, 1179 1188.
    • (1996) Neuron , vol.16 , pp. 1179-1188
    • Roche, K.W.1    O'Brien, R.J.2    Mammen, A.L.3    Bernhardt, J.4    Huganir, R.L.5
  • 35
    • 0036232874 scopus 로고    scopus 로고
    • The nicotinic allosteric potentiating ligand galantamine facilitates synaptic transmission in the mammalian central nervous system
    • Santos M. D., Alkondon M., Pereira E. F., Aracava Y., Eisenberg H. M., Maelicke A. Albuquerque E. X. (2002) The nicotinic allosteric potentiating ligand galantamine facilitates synaptic transmission in the mammalian central nervous system. Mol. Pharmacol. 61, 1222 1234.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1222-1234
    • Santos, M.D.1    Alkondon, M.2    Pereira, E.F.3    Aracava, Y.4    Eisenberg, H.M.5    Maelicke, A.6    Albuquerque, E.X.7
  • 36
    • 0030023684 scopus 로고    scopus 로고
    • Agonist responses of neuronal nicotinic acetylcholine receptors are potentiated by a novel class of allosterically acting ligands
    • Schrattenholz A., Pereira E. F. R., Roth U., Weber K. H., Albuquerque E. X. Maelicke A. (1996) Agonist responses of neuronal nicotinic acetylcholine receptors are potentiated by a novel class of allosterically acting ligands. Mol. Pharmacol. 49, 1 6.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1-6
    • Schrattenholz, A.1    Pereira, E.F.R.2    Roth, U.3    Weber, K.H.4    Albuquerque, E.X.5    Maelicke, A.6
  • 39
    • 0031807666 scopus 로고    scopus 로고
    • Protein kinase C expression and activity after global incomplete cerebral ischemia in dogs
    • Sieber F. E., Traystman R. J., Brown P. R. Martin L. J. (1998) Protein kinase C expression and activity after global incomplete cerebral ischemia in dogs. Stroke 29, 1445 1452.
    • (1998) Stroke , vol.29 , pp. 1445-1452
    • Sieber, F.E.1    Traystman, R.J.2    Brown, P.R.3    Martin, L.J.4
  • 40
    • 0034142054 scopus 로고    scopus 로고
    • Postsynaptic protein phosphorylation and LTP
    • Soderling T. R. Derkach V. A. (2000) Postsynaptic protein phosphorylation and LTP. Trends Neurosci. 23, 75 80.
    • (2000) Trends Neurosci. , vol.23 , pp. 75-80
    • Soderling, T.R.1    Derkach, V.A.2
  • 41
    • 0027209184 scopus 로고
    • Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain
    • Tingley W. G., Roche K. W., Thompson A. K. Huganir R. L. (1993) Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364, 70 73.
    • (1993) Nature , vol.364 , pp. 70-73
    • Tingley, W.G.1    Roche, K.W.2    Thompson, A.K.3    Huganir, R.L.4
  • 42
    • 0031040615 scopus 로고    scopus 로고
    • Characterization of protein kinase a and protein kinase C phosphorylation of the N-methyl-D-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies
    • Tingley W. G., Ehlers M. D., Kameyama K., Doherty C., Ptak J. B., Riley C. T. Huganir R. L. (1997) Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-D-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies. J. Biol. Chem. 272, 5157 5166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5157-5166
    • Tingley, W.G.1    Ehlers, M.D.2    Kameyama, K.3    Doherty, C.4    Ptak, J.B.5    Riley, C.T.6    Huganir, R.L.7
  • 43
    • 0038721940 scopus 로고    scopus 로고
    • NMDA and beta-1 adrenergic receptors differently signal phosphorylation of glutamate receptor type 1 in area CA1 of hippocampus
    • Vanhoose A. M. Winder D. G. (2003) NMDA and beta-1 adrenergic receptors differently signal phosphorylation of glutamate receptor type 1 in area CA1 of hippocampus. J. Neurosci. 23, 5827 5834.
    • (2003) J. Neurosci. , vol.23 , pp. 5827-5834
    • Vanhoose, A.M.1    Winder, D.G.2
  • 44
    • 0028921951 scopus 로고
    • Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site
    • Wafford K. A., Kathoria M., Bain C. J., Marshall G., Le Bourdelles B., Kemp J. A. Whiting P. J. (1995) Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site. Mol. Pharmacol. 47, 374 380.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 374-380
    • Wafford, K.A.1    Kathoria, M.2    Bain, C.J.3    Marshall, G.4    Le Bourdelles, B.5    Kemp, J.A.6    Whiting, P.J.7
  • 45
    • 0141920783 scopus 로고    scopus 로고
    • New aspects of neurotransmitter release and exocytosis: Dynamic and differential regulation of synapsin I phosphorylation by acute neuronal excitation in vivo
    • Yamagata Y. (2003) New aspects of neurotransmitter release and exocytosis: dynamic and differential regulation of synapsin I phosphorylation by acute neuronal excitation in vivo. J. Pharmacol. Sci. 93, 22 29.
    • (2003) J. Pharmacol. Sci. , vol.93 , pp. 22-29
    • Yamagata, Y.1
  • 46
    • 0031081046 scopus 로고    scopus 로고
    • Cellular mechanism of underlying cognition-enhancing actions of nefiracetam (DM-9384)
    • Yoshii M., Watabe S., Sakurai T. Shiotani T. (1997) Cellular mechanism of underlying cognition-enhancing actions of nefiracetam (DM-9384). Behav. Brain Res. 83, 185 188.
    • (1997) Behav. Brain Res. , vol.83 , pp. 185-188
    • Yoshii, M.1    Watabe, S.2    Sakurai, T.3    Shiotani, T.4
  • 47
    • 0035057505 scopus 로고    scopus 로고
    • Nootropic drug modulation of neuronal nicotinic acethylcholine receptors in rat cortical neurons
    • Zhao X., Kuryatov A., Lindstorm J. M., Yeh J. Z. Narahashi T. (2001) Nootropic drug modulation of neuronal nicotinic acethylcholine receptors in rat cortical neurons. Mol. Pharmacol. 59, 674 683.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 674-683
    • Zhao, X.1    Kuryatov, A.2    Lindstorm, J.M.3    Yeh, J.Z.4    Narahashi, T.5


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