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Volumn 30, Issue 3, 2012, Pages 665-673

Pyruvate prevents the inhibition of the long-term potentiation induced by amyloid-β through protein phosphatase 2A inactivation

Author keywords

Amyloid oligomer; calmodulin dependent protein kinase 1; long term potentiation; protein phosphatase 2A; pyruvate; reactive oxygen species

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; FOSTRIECIN; LACTATE SODIUM; PHOSPHOPROTEIN PHOSPHATASE 2A; PYRUVATE SODIUM; REACTIVE OXYGEN METABOLITE;

EID: 84862867033     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2012-101869     Document Type: Article
Times cited : (21)

References (55)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 53-356
    • Hardy, J.1    Selkoe, D.J.2
  • 6
    • 33744471433 scopus 로고    scopus 로고
    • A beta immunotherapy: Lessons learned for potential treatment of Alzheimer's disease
    • Schenk DB, Seubert P, Grundman M, Black R (2005) A beta immunotherapy: Lessons learned for potential treatment of Alzheimer's disease. Neurodegener Dis 2, 255-260.
    • (2005) Neurodegener Dis , vol.2 , pp. 55-260
    • Schenk, D.B.1    Seubert, P.2    Grundman, M.3    Black, R.4
  • 7
    • 0028988308 scopus 로고
    • Increased phosphorylation of Ca2+/calmodulin-dependent kinase II and its endogenous substrates in the induction of long-term potentiation
    • Fukunaga K, Muller D, Miyamoto E (1995) Increased phosphorylation of Ca2+/calmodulin-dependent 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. 119-6124
    • Fukunaga, K.1    Muller, D.2    Miyamoto, E.3
  • 8
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaMK-II during long-term potentiation
    • Barria A, Muller D, Derkach V, Griffith LC, Soderling TR (1997) Regulatory phosphorylation of AMPA-type glutamate receptors by CaMK-II during long-term potentiation. Science 276, 2042-2045.
    • (1997) Science , vol.276 , pp. 042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 9
    • 34248401164 scopus 로고    scopus 로고
    • Reversal of synaptic memory by Ca2+/calmodulin-dependent kinase II inhibitor
    • Sanhueza M, McIntyre CC, Lisman JE (2007) Reversal of synaptic memory by Ca2+/calmodulin-dependent kinase II inhibitor. J Neurosci 27, 5190-5199.
    • (2007) J Neurosci , vol.27 , pp. 190-5199
    • Sanhueza, M.1    McIntyre, C.C.2    Lisman, J.E.3
  • 11
    • 14844315768 scopus 로고    scopus 로고
    • Amyliod-prevent activation of calcium/calmodulin dependent protein kinase II and AMPA receptor phosphorylation during hippocample long-term potentiation
    • Zhao DY, Watson JB, Xie CW (2004) Amyliod-prevent activation of calcium/calmodulin dependent protein kinase II and AMPA receptor phosphorylation during hippocample long-term potentiation. J Neurophysiol 2, 2853-2858.
    • (2004) J Neurophysiol , vol.2 , pp. 853-2858
    • Zhao, D.Y.1    Watson, J.B.2    Xie, C.W.3
  • 12
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling
    • Janssens V, Goris J (2001) Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling. Biochem J 353, 417-439.
    • (2001) Biochem J , vol.353 , pp. 17-439
    • Janssens, V.1    Goris, J.2
  • 14
    • 57049156456 scopus 로고    scopus 로고
    • Oxidative impairment of hippocampal long-term potentiation involves activation of protein phospahatase 2A and is prevented by ketone bodies
    • Maalouf M, Rho JM (2008) Oxidative impairment of hippocampal long-term potentiation involves activation of protein phospahatase 2A and is prevented by ketone bodies. J Neurosci Res 86, 322-330.
    • (2008) J Neurosci Res , vol.86 , pp. 22-330
    • Maalouf, M.1    Rho, J.M.2
  • 16
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Matton MP (2004) Pathways towards and away from Alzheimer's disease. Nature 430, 631-639.
    • (2004) Nature , vol.430 , pp. 31-639
    • Matton, M.P.1
  • 18
    • 0032229327 scopus 로고    scopus 로고
    • Reactive oxygen species mediate cellular damage in Alzheimer's disease
    • Perry G, Castellani RJ, Hirai K, Smith MA (1998) Reactive oxygen species mediate cellular damage in Alzheimer's disease. J Alzheimers Dis 1, 45-55.
    • (1998) J Alzheimers Dis , vol.1 , pp. 5-55
    • Perry, G.1    Castellani, R.J.2    Hirai, K.3    Smith, M.A.4
  • 19
    • 0034516988 scopus 로고    scopus 로고
    • Toward a comprehensive theory for Alzheimer's disease Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of betaprotein
    • Selkoe DJ (2000) Toward a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of betaprotein. Ann NY Acad Sci 924, 17-25.
    • (2000) Ann NY Acad Sci , vol.924 , pp. 7-25
    • Selkoe, D.J.1
  • 22
    • 0030703154 scopus 로고    scopus 로고
    • Pyruvate protects neurons against hydrogen peroxide-induced toxicity
    • Desagher S, Glowinski J, Premont J (1997) Pyruvate protects neurons against hydrogen peroxide-induced toxicity. J Neurosci 17, 9060-9067.
    • (1997) J Neurosci , vol.17 , pp. 060-9067
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 23
    • 0038167009 scopus 로고    scopus 로고
    • Pyruvate protection against-amyloid-induced neuronal death: Role of mitochondrial redox state
    • Alvarez G, Ramos M, Ruiz F, Satŕustegui J, Boǵonez E (2003) Pyruvate protection against-amyloid-induced neuronal death: Role of mitochondrial redox state. J Neurosci Res 73, 260-269.
    • (2003) J Neurosci Res , vol.73 , pp. 60-269
    • Alvarez, G.1    Ramos, M.2    Ruiz, F.3    Satŕustegui, J.4    Boǵonez, E.5
  • 24
    • 35448984525 scopus 로고    scopus 로고
    • Different effects of monocarboxylates on neuronal survival and-amyloid toxicity
    • Wang XN, Takata T, Sakurai T, Yokono K (2007) Different effects of monocarboxylates on neuronal survival and-amyloid toxicity. Eur J Neurosci 26, 2142-2150.
    • (2007) Eur J Neurosci , vol.26 , pp. 142-2150
    • Wang, X.N.1    Takata, T.2    Sakurai, T.3    Yokono, K.4
  • 25
    • 77957810913 scopus 로고    scopus 로고
    • Amyloid-neurotoxicity restricts glucose window for neuronal survival in rat hippocampal slice cultures
    • Wang X, Song X, Takata T, Miichi Y, Yokono K, Sakurai T (2010) Amyloid-neurotoxicity restricts glucose window for neuronal survival in rat hippocampal slice cultures. Exp Gerontol 45, 904-908.
    • (2010) Exp Gerontol , vol.45 , pp. 04-908
    • Wang, X.1    Song, X.2    Takata, T.3    Miichi, Y.4    Yokono, K.5    Sakurai, T.6
  • 26
    • 0025805120 scopus 로고
    • A simple method for organotypic cultures of nervous tissue
    • Stoppini L, Buchs PA, Muller D (1991) A simple method for organotypic cultures of nervous tissue. J Neurosci Methods 37, 173-182.
    • (1991) J Neurosci Methods , vol.37 , pp. 73-182
    • Stoppini, L.1    Buchs, P.A.2    Muller, D.3
  • 27
    • 30644475475 scopus 로고    scopus 로고
    • Soluble-Amyloid1?40 induces NMDA-dependert degradation of postsynaptic density-95 at glutamatergic synapses
    • Roselli F, Tirard M, Lu J, Hutzler P, Lamberti P, Livrea P, Morabito M, Almeida OFX (2005) Soluble-Amyloid1?40 induces NMDA-dependert degradation of postsynaptic density-95 at glutamatergic synapses. J Neurosci 25, 11061-11070.
    • (2005) J Neurosci , vol.25 , pp. 1061-11070
    • Roselli, F.1    Tirard, M.2    Lu, J.3    Hutzler, P.4    Lamberti, P.5    Livrea, P.6    Morabito, M.7    Almeida, O.F.X.8
  • 28
    • 0016208056 scopus 로고
    • Recovery of neuronal activity and highenergy compound level after complete and prolonged brain ischemia
    • Okada Y (1974) Recovery of neuronal activity and highenergy compound level after complete and prolonged brain ischemia. Brain Res 72, 346-349.
    • (1974) Brain Res , vol.72 , pp. 46-349
    • Okada, Y.1
  • 29
    • 0033118508 scopus 로고    scopus 로고
    • Adenylyl cyclase activation modulates activity-dependent changes in synaptic strength and Ca2+/calmodulin-dependent kinase II autophosphorylation
    • Makhinson M, Chotiner JK, Watson JB, O'Dell TJ (1999) Adenylyl cyclase activation modulates activity-dependent changes in synaptic strength and Ca2+/calmodulin-dependent kinase II autophosphorylation. J Neurosci 19, 2500-2510.
    • (1999) J Neurosci , vol.19 , pp. 500-2510
    • Makhinson, M.1    Chotiner, J.K.2    Watson, J.B.3    O'dell, T.J.4
  • 30
    • 0035895957 scopus 로고    scopus 로고
    • The neuroprotective effects of phytoestrogens on amyloid-protein-induced toxicity are mediated by abrogating the activation of caspase cascade in rat cortical neurons
    • Wang CN, Chi CW, Lin YL, Chen CF, Shiao YJ (2001) The neuroprotective effects of phytoestrogens on amyloid-protein-induced toxicity are mediated by abrogating the activation of caspase cascade in rat cortical neurons. J Biol Chem 276, 5287-5295.
    • (2001) J Biol Chem , vol.276 , pp. 287-5295
    • Wang, C.N.1    Chi, C.W.2    Lin, Y.L.3    Chen, C.F.4    Shiao, Y.J.5
  • 32
    • 0036354603 scopus 로고    scopus 로고
    • Alzheimer amyloid beta-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus
    • Chen QS, Wei WZ, Shimahara T, Xie CW (2002) Alzheimer amyloid beta-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus. Neurobiol Learn Mem 77, 354-371.
    • (2002) Neurobiol Learn Mem , vol.77 , pp. 54-371
    • Chen, Q.S.1    Wei, W.Z.2    Shimahara, T.3    Xie, C.W.4
  • 33
    • 0035407298 scopus 로고    scopus 로고
    • Roles of serine/threonine phosphatases in hippocampal synaptic plasticity
    • Winder DG, Sweatt JD (2001) Roles of serine/threonine phosphatases in hippocampal synaptic plasticity. Nat Rev Neurosci 2, 461-474.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 61-474
    • Winder, D.G.1    Sweatt, J.D.2
  • 35
    • 73949133583 scopus 로고    scopus 로고
    • GluN2B subunit-containing NMDA receptor antagonists prevent A-mediated synaptic plasticity disruption in vivo
    • Hu NM, Klyubin I, Anwyl R, Rowan MJ (2009) GluN2B subunit-containing NMDA receptor antagonists prevent A-mediated synaptic plasticity disruption in vivo. Proc Natl Acad Sci U S A 106, 20504-20509.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 0504-20509
    • Hu, N.M.1    Klyubin, I.2    Anwyl, R.3    Rowan, M.J.4
  • 36
    • 0022929859 scopus 로고
    • Reversible generation of a Ca2+-dependent from of Ca2+ (calmodulin)-dependent protein kinase II by an autophosphorylation mechanism
    • Schworer CM, Colbran RJ, Soderling TR (1986) Reversible generation of a Ca2+-dependent from of Ca2+ (calmodulin)-dependent protein kinase II by an autophosphorylation mechanism. J Biol Chem 261, 8581-8584.
    • (1986) J Biol Chem , vol.261 , pp. 581-8584
    • Schworer, C.M.1    Colbran, R.J.2    Soderling, T.R.3
  • 37
    • 0030946102 scopus 로고    scopus 로고
    • Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
    • Strack S, Choi S, Lovinger DM, Colbran RJ (1997) Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density. J Biol Chem 272, 13467-13470.
    • (1997) J Biol Chem , vol.272 , pp. 3467-13470
    • Strack, S.1    Choi, S.2    Lovinger, D.M.3    Colbran, R.J.4
  • 38
    • 0022444426 scopus 로고
    • Autophosphorylation reversibly regulated the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II
    • Lai Y, nairn AC, Greengard P (1986) Autophosphorylation reversibly regulated the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II. Proc Natl Acad Sci U S A 83, 4253-4257.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 253-4257
    • Lai, Y.1    Nairn, A.C.2    Greengard, P.3
  • 39
    • 0023226506 scopus 로고
    • Inactivation and reactivation of the multifunctional calmodulin-dependent protein kinase from brain by autophosphorylation and dephosphorylation: Involvement of protein phosphatases fron brain
    • SaitohY,Yamamoto H, FukubagaK,MatsukadoY, Miyamoto E (1987) Inactivation and reactivation of the multifunctional calmodulin-dependent protein kinase from brain by autophosphorylation and dephosphorylation: Involvement of protein phosphatases fron brain. J Neurochem 49, 1286-1292.
    • (1987) J Neurochem , vol.49 , pp. 286-1292
    • Saitoh, Y.1    Yamamoto, H.2    Fukubaga, K.3    Matsukado, Y.4    Miyamoto, E.5
  • 40
    • 0024073790 scopus 로고
    • Sequences of auphosphorylation sites in neural type II CaM kinase that control Ca2+-dependent activity
    • Miller SG, Patton BL, Kennedy MB (1988) Sequences of auphosphorylation sites in neural type II CaM kinase that control Ca2+-dependent activity. Neuron 1, 593-604.
    • (1988) Neuron , vol.1 , pp. 93-604
    • Miller, S.G.1    Patton, B.L.2    Kennedy, M.B.3
  • 41
    • 0027339550 scopus 로고
    • Dephosphorylation of autophosphorylated Ca2+/calmodulindependent kinase II by protein phosphatase 2C
    • Fukunaga K, Kobayashi T, Tamura S, Miyamoto E (1993) Dephosphorylation of autophosphorylated Ca2+/calmodulindependent kinase II by protein phosphatase 2C. J Biol Chem 268, 133-137.
    • (1993) J Biol Chem , vol.268 , pp. 33-137
    • Fukunaga, K.1    Kobayashi, T.2    Tamura, S.3    Miyamoto, E.4
  • 42
    • 0029076397 scopus 로고
    • Nonenzymatically glycated tau in Alzhheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • Yan SD, Yan SF, Chen X, Fu J, Chen M, Kuppusamy P, Smith MA, Perry G, Godman GC, Nawroth P, et al. (1995) Nonenzymatically glycated tau in Alzhheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nat Med 1, 693-699.
    • (1995) Nat Med , vol.1 , pp. 93-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10
  • 44
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • MottonMP(1997) Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 77, 1081-1082.
    • (1997) Physiol Rev , vol.77 , pp. 1081-1082
    • Motton, M.P.1
  • 47
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M, Yu Z-X, Ferrans VJ, Irani K, Finkel T (1995) Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270, 296-299.
    • (1995) Science , vol.270 , pp. 96-299
    • Sundaresan, M.1    Yu, Z.-X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 48
    • 0032100603 scopus 로고    scopus 로고
    • Redox signaling and the emerging therapeutic potential of thiol antioxidants
    • Sen CK (1998) Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem Pharmacol 55, 1747-1758.
    • (1998) Biochem Pharmacol , vol.55 , pp. 747-1758
    • Sen, C.K.1
  • 49
    • 0033568661 scopus 로고    scopus 로고
    • Repression of gene expression by oxidative stress
    • Morel Y, Barouki R (1999) Repression of gene expression by oxidative stress. Biochem J 342, 481-496.
    • (1999) Biochem J , vol.342 , pp. 81-496
    • Morel, Y.1    Barouki, R.2
  • 50
    • 0030664790 scopus 로고    scopus 로고
    • Biphasic effect of hyfrogen peroxide on field potentials in rat hippocampal slices
    • Katsuki H, Nakanishi C, Saito H, Matsuki N (1997) Biphasic effect of hyfrogen peroxide on field potentials in rat hippocampal slices. Eur J Pharmacol 337, 213-218.
    • (1997) Eur J Pharmacol , vol.337 , pp. 13-218
    • Katsuki, H.1    Nakanishi, C.2    Saito, H.3    Matsuki, N.4
  • 51
    • 3643050864 scopus 로고    scopus 로고
    • Changes in membrane and synaptic properties of thalamocortical circuitry caused by hydrogen peroxide
    • Frantseva MV, Velazquez JLP, Carlen PL (1998) Changes in membrane and synaptic properties of thalamocortical circuitry caused by hydrogen peroxide. J Neurophysiol 80, 1317-1326.
    • (1998) J Neurophysiol , vol.80 , pp. 317-1326
    • Frantseva, M.V.1    Velazquez, J.L.P.2    Carlen, P.L.3
  • 52
    • 0036785151 scopus 로고    scopus 로고
    • Role of reactive oxygen species in hippocampal long-term potentiation: Contributory or inhibitory?
    • Knapp LT, Klann E (2002) Role of reactive oxygen species in hippocampal long-term potentiation: Contributory or inhibitory? J Neurosci Res 70, 1-7.
    • (2002) J Neurosci Res , vol.70 , pp. 1-7
    • Knapp, L.T.1    Klann, E.2
  • 53
    • 8444227821 scopus 로고    scopus 로고
    • Reactive oxygen species and synaptic plasticity in the aging hippocampus
    • Serrano F, KlannE(2004) Reactive oxygen species and synaptic plasticity in the aging hippocampus. Aging Res Rev 3, 431-443.
    • (2004) Aging Res Rev , vol.3 , pp. 431-443
    • Serrano, F.1    Klann, E.2
  • 54
    • 0033121096 scopus 로고    scopus 로고
    • Modulation of protein kinases and protein phosphatases by reactive oxygen species: Implication for hippocampal synaptic plasticity
    • Klann E, Thiel E (1999) Modulation of protein kinases and protein phosphatases by reactive oxygen species: Implication for hippocampal synaptic plasticity. Prog Neuropsychophamacol Biol Psychiatry 23, 359-376.
    • (1999) Prog Neuropsychophamacol Biol Psychiatry , vol.23 , pp. 59-376
    • Klann, E.1    Thiel, E.2
  • 55
    • 76749138927 scopus 로고    scopus 로고
    • Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration
    • Hsu MJ, Sheu JR, Lin CH, Shen MY, Hsu CY (2010) Mitochondrial mechanisms in amyloid beta peptide-induced cerebrovascular degeneration. Biochim Biophys Acta 3, 290-296.
    • (2010) Biochim Biophys Acta , vol.3 , pp. 90-296
    • Hsu, M.J.1    Sheu, J.R.2    Lin, C.H.3    Shen, M.Y.4    Hsu, C.Y.5


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