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Volumn 287, Issue 14, 2012, Pages 11174-11182

Synaptic released zinc promotes tau hyperphosphorylation by inhibition of Protein Phosphatase 2A (PP2A)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; BRAIN SLICES; EXCITATORY SYNAPSIS; EXTRACELLULAR; HIPPOCAMPAL SLICE; HYPERPHOSPHORYLATED; HYPERPHOSPHORYLATION; NEUROFIBRILLARY TANGLES; PRE-TREATMENT; PROTEIN PHOSPHATASE 2A; SYNAPTIC TERMINALS; ZINC CHELATOR;

EID: 84859506934     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.309070     Document Type: Article
Times cited : (120)

References (46)
  • 1
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • DOI 10.1038/nm0706-780, PII NM0706780
    • Mount, C., and Downton, C. (2006) Alzheimer disease: progress or profit? Nat. Med. 12, 780-784 (Pubitemid 44050066)
    • (2006) Nature Medicine , vol.12 , Issue.7 , pp. 780-784
    • Mount, C.1    Downton, C.2
  • 2
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., and Wisniewski, H. M. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 261, 6084-6089 (Pubitemid 17207447)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.13 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3
  • 3
    • 43249124363 scopus 로고    scopus 로고
    • Microtubule-associated protein tau in development, degeneration and protection of neurons
    • Wang, J. Z., and Liu, F. (2008) Microtubule-associated protein tau in development, degeneration and protection of neurons. Prog. Neurobiol. 85, 148-175
    • (2008) Prog. Neurobiol. , vol.85 , pp. 148-175
    • Wang, J.Z.1    Liu, F.2
  • 4
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • DOI 10.1016/0006-8993(89)91396-6
    • Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., and Wisniewski, H. M. (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 477, 90-99 (Pubitemid 19026942)
    • (1989) Brain Research , vol.477 , Issue.1-2 , pp. 90-99
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3    Budka, H.4    Jellinger, K.5    Wiche, G.6    Seitelberger, F.7    Grundke-Iqbal, I.8    Wisniewski, H.M.9
  • 5
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non- paired helical filament pool in Alzheimer disease
    • Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., and Grundke-Iqbal, I. (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24374-24384 (Pubitemid 23335430)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.-C.2    Shaikh, S.3    Del, A.C.A.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 7
    • 0022531202 scopus 로고
    • Seizures and myoclonus in patients with Alzheimer's disease
    • Hauser, W. A., Morris, M. L., Heston, L. L., and Anderson, V. E. (1986) Seizures and myoclonus in patients with Alzheimer disease. Neurology 36, 1226-1230 (Pubitemid 16047002)
    • (1986) Neurology , vol.36 , Issue.9 , pp. 1226-1230
    • Hauser, W.A.1    Morris, M.L.2    Heston, L.L.3    Anderson, V.E.4
  • 8
    • 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., and Jay, G. (1995) The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat. Genet. 9, 21-30
    • (1995) Nat. 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
  • 10
    • 65249093004 scopus 로고    scopus 로고
    • A role for synaptic zinc in activity-dependent Aβ oligomer formation and accumulation at excitatory synapses
    • Deshpande, A., Kawai, H., Metherate, R., Glabe, C. G., and Busciglio, J. (2009) A role for synaptic zinc in activity-dependent Aβ oligomer formation and accumulation at excitatory synapses. J. Neurosci. 29, 4004-4015
    • (2009) J. Neurosci. , vol.29 , pp. 4004-4015
    • Deshpande, A.1    Kawai, H.2    Metherate, R.3    Glabe, C.G.4    Busciglio, J.5
  • 11
    • 0025188014 scopus 로고
    • Labeling of the neurons of origin of zinc-containing pathways by intraperitoneal injections of sodium selenite
    • DOI 10.1016/0306-4522(90)90076-G
    • Slomianka, L., Danscher, G., and Frederickson, C. J. (1990) Labeling of the neurons of origin of zinc-containing pathways by intraperitoneal injections of sodium selenite. Neuroscience 38, 843-854 (Pubitemid 20383219)
    • (1990) Neuroscience , vol.38 , Issue.3 , pp. 843-854
    • Slomianka, L.1    Danscher, G.2    Frederickson, C.J.3
  • 12
    • 14844299775 scopus 로고    scopus 로고
    • Mechanism of zinc-induced phosphorylation of p70 S6 kinase and glycogen synthase kinase 3β in SH-SY5Y neuroblastoma cells
    • DOI 10.1111/j.1471-4159.2004.02948.x
    • An, W. L., Bjorkdahl, C., Liu, R., Cowburn, R. F., Winblad, B., and Pei, J. J. (2005) Mechanism of zinc-induced phosphorylation of p70 S6 kinase and glycogen synthase kinase 3β in SH-SY5Y neuroblastoma cells. J. Neurochem. 92, 1104-1115 (Pubitemid 40344301)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.5 , pp. 1104-1115
    • An, W.-L.1    Bjorkdahl, C.2    Liu, R.3    Cowburn, R.F.4    Winblad, B.5    Pei, J.-J.6
  • 13
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • Takashima, A. (2006) GSK-3 is essential in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 9, 309-317
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 309-317
    • Takashima, A.1
  • 15
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • DOI 10.1111/j.1460-9568.2005.04391.x
    • Liu, F., Grundke-Iqbal, I., Iqbal, K., and Gong, C. X. (2005) Contributions of protein phosphatases PP1, PP2A, PP2B, and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci. 22, 1942-1950 (Pubitemid 41579384)
    • (2005) European Journal of Neuroscience , vol.22 , Issue.8 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.-X.4
  • 16
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C. X., Singh, T. J., Grundke-Iqbal, I., and Iqbal, K. (1993) Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61, 921-927 (Pubitemid 23241228)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.3 , pp. 921-927
    • Gong, C.-X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 17
    • 24144440042 scopus 로고    scopus 로고
    • Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms
    • DOI 10.1111/j.1471-4159.2005.03270.x
    • Liu, R., Pei, J. J., Wang, X. C., Zhou, X. W., Tian, Q., Winblad, B., and Wang, J. Z. (2005) Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms. J. Neurochem. 94, 1225-1234 (Pubitemid 41232578)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.5 , pp. 1225-1234
    • Liu, R.1    Pei, J.-J.2    Wang, X.-C.3    Zhou, X.-W.4    Tian, Q.5    Winbladt, B.6    Wang, J.-Z.7
  • 18
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • DOI 10.1023/A:1012934207456
    • Frederickson, C. J., and Bush, A. I. (2001) Synaptically released zinc: physiological functions and pathological effects. Biometals 14, 353-366 (Pubitemid 34066638)
    • (2001) BioMetals , vol.14 , Issue.3-4 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 19
    • 38849084002 scopus 로고    scopus 로고
    • Presynaptic evidence for zinc release at the mossy fiber synapse of rat hippocampus
    • DOI 10.1002/jnr.21488
    • Ketterman, J. K., and Li, Y. V. (2008) Presynaptic evidence for zinc release at the mossy fiber synapse of rat hippocampus. J. Neurosci. Res. 86, 422-434 (Pubitemid 351196747)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.2 , pp. 422-434
    • Ketterman, J.K.1    Li, Y.V.2
  • 20
    • 71749113077 scopus 로고    scopus 로고
    • Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322
    • Mo, Z. Y., Zhu, Y. Z., Zhu, H. L., Fan, J. B., Chen, J., and Liang, Y. (2009) Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322. J. Biol. Chem. 284, 34648-34657
    • (2009) J. Biol. Chem. , vol.284 , pp. 34648-34657
    • Mo, Z.Y.1    Zhu, Y.Z.2    Zhu, H.L.3    Fan, J.B.4    Chen, J.5    Liang, Y.6
  • 22
    • 33845769476 scopus 로고    scopus 로고
    • Extracellular chelation of zinc does not affect hippocampal excitability and seizure-induced cell death in rats
    • DOI 10.1113/jphysiol.2006.121848
    • Lavoie, N., Peralta, M. R., 3rd, Chiasson, M., Lafortune, K., Pellegrini, L., Seress, L., and Tóth, K. (2007) Extracellular chelation of zinc does not affect hippocampal excitability and seizure-induced cell death in rats. J. Physiol. 578, 275-289 (Pubitemid 44971124)
    • (2007) Journal of Physiology , vol.578 , Issue.1 , pp. 275-289
    • Lavoie, N.1    Peralta III, M.R.2    Chiasson, M.3    Lafortune, K.4    Pellegrini, L.5    Seress, L.6    Toth, K.7
  • 23
    • 0035116275 scopus 로고    scopus 로고
    • Nuclear calcium signaling controls CREB-mediated gene expression triggered by synaptic activity
    • DOI 10.1038/85109
    • Hardingham, G. E., Arnold, F. J., and Bading, H. (2001) Nuclear calcium signaling controls CREB-mediated gene expression triggered by synaptic activity. Nat. Neurosci. 4, 261-267 (Pubitemid 32194873)
    • (2001) Nature Neuroscience , vol.4 , Issue.3 , pp. 261-267
    • Hardingham, G.E.1    Arnold, F.J.L.2    Bading, H.3
  • 24
    • 0035657358 scopus 로고    scopus 로고
    • 2+ from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation
    • Li, Y., Hough, C. J., Suh, S. W., Sarvey, J. M., and Frederickson, C. J. (2001) Rapid translocation of Zn(2+) from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation. J. Neurophysiol. 86, 2597-2604 (Pubitemid 34000617)
    • (2001) Journal of Neurophysiology , vol.86 , Issue.5 , pp. 2597-2604
    • Li, Y.1    Hough, C.J.2    Suh, S.W.3    Sarvey, J.M.4    Frederickson, C.J.5
  • 25
    • 0026447621 scopus 로고
    • Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development
    • Riederer, B. M. (1992) Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development. Histochem. J. 24, 783-790
    • (1992) Histochem. J. , vol.24 , pp. 783-790
    • Riederer, B.M.1
  • 26
    • 20144377557 scopus 로고    scopus 로고
    • The neurobiology of zinc in health and disease
    • DOI 10.1038/nrn1671
    • Frederickson, C. J., Koh, J. Y., and Bush, A. I. (2005) The neurobiology of zinc in health and disease. Nat. Rev. Neurosci. 6, 449-462 (Pubitemid 40774861)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.6 , pp. 449-462
    • Frederickson, C.J.1    Koh, J.-Y.2    Bush, A.I.3
  • 29
    • 0041672236 scopus 로고    scopus 로고
    • Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus
    • DOI 10.1093/cercor/13.8.823
    • Sindreu, C. B., Varoqui, H., Erickson, J. D., and Pérez-Clausell, J. (2003) Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus. Cereb. Cortex 13, 823-829 (Pubitemid 36917961)
    • (2003) Cerebral Cortex , vol.13 , Issue.8 , pp. 823-829
    • Sindreu, C.B.1    Varoqui, H.2    Erickson, J.D.3    Perez-Clausell, J.4
  • 30
    • 72449151659 scopus 로고    scopus 로고
    • Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit
    • Karakas, E., Simorowski, N., and Furukawa, H. (2009) Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. EMBO J. 28, 3910-3920
    • (2009) EMBO J. , vol.28 , pp. 3910-3920
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 31
    • 77953135668 scopus 로고    scopus 로고
    • Zinc differentially acts on components of long-term potentiation at hippocampal CA1 synapses
    • Takeda, A., Iwaki, H., Ando, M., Itagaki, K., Suzuki, M., and Oku, N. (2010) Zinc differentially acts on components of long-term potentiation at hippocampal CA1 synapses. Brain Res. 1323, 59-64
    • (2010) Brain Res. , vol.1323 , pp. 59-64
    • Takeda, A.1    Iwaki, H.2    Ando, M.3    Itagaki, K.4    Suzuki, M.5    Oku, N.6
  • 33
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: Possible relation to oxidative stress
    • DOI 10.1016/S0022-510X(96)00203-1, PII S0022510X96002031
    • Deibel, M. A., Ehmann, W. D., and Markesbery, W. R. (1996) Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J. Neurol. Sci. 143, 137-142 (Pubitemid 26402800)
    • (1996) Journal of the Neurological Sciences , vol.143 , Issue.1-2 , pp. 137-142
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 35
    • 27744545492 scopus 로고    scopus 로고
    • Alterations in zinc transporter protein-1 (ZnT-1) in the brain of subjects with mild cognitive impairment, early, and late-stage Alzheimer's disease
    • Lovell, M. A., Smith, J. L., Xiong, S., and Markesbery, W. R. (2005) Alterations in zinc transporter protein-1 (ZnT-1) in the brain of subjects with mild cognitive impairment, early, and late-stage Alzheimer's disease. Neurotox. Res. 7, 265-271
    • (2005) Neurotox. Res. , vol.7 , pp. 265-271
    • Lovell, M.A.1    Smith, J.L.2    Xiong, S.3    Markesbery, W.R.4
  • 36
    • 33747206832 scopus 로고    scopus 로고
    • Altered expression of zinc transporters-4 and -6 in mild cognitive impairment, early and late Alzheimer's disease brain
    • Smith, J. L., Xiong, S., Markesbery, W. R., and Lovell, M. A. (2006) Altered expression of zinc transporters-4 and -6 in mild cognitive impairment, early and late Alzheimer's disease brain. Neuroscience 140, 879-888
    • (2006) Neuroscience , vol.140 , pp. 879-888
    • Smith, J.L.1    Xiong, S.2    Markesbery, W.R.3    Lovell, M.A.4
  • 37
    • 76149093866 scopus 로고    scopus 로고
    • Cognitive loss in zinc transporter-3 knock-out mice: A phenocopy for the synaptic and memory deficits of Alzheimer's disease?
    • Adlard, P. A., Parncutt, J. M., Finkelstein, D. I., and Bush, A. I. (2010) Cognitive loss in zinc transporter-3 knock-out mice: a phenocopy for the synaptic and memory deficits of Alzheimer's disease? J. Neurosci. 30, 1631-1636
    • (2010) J. Neurosci. , vol.30 , pp. 1631-1636
    • Adlard, P.A.1    Parncutt, J.M.2    Finkelstein, D.I.3    Bush, A.I.4
  • 38
    • 70349292938 scopus 로고    scopus 로고
    • Zinc: The brain's dark horse
    • Bitanihirwe, B. K., and Cunningham, M. G. (2009) Zinc: the brain's dark horse. Synapse 63, 1029-1049
    • (2009) Synapse , vol.63 , pp. 1029-1049
    • Bitanihirwe, B.K.1    Cunningham, M.G.2
  • 39
    • 0025124693 scopus 로고
    • Zinc-containin neurons in hippocampus and related CNS structures
    • Frederickson, C. J., and Danscher, G. (1990) Zinc-containing neurons in hippocampus and related CNS structures. Prog. Brain Res. 83, 71-84 (Pubitemid 20205272)
    • (1990) Progress in Brain Research , vol.83 , pp. 71-84
    • Frederickson, C.J.1    Danscher, G.2
  • 41
    • 3242699005 scopus 로고    scopus 로고
    • Zinc release contributes to hypoglycemia-induced neuronal death
    • DOI 10.1016/j.nbd.2004.04.017, PII S0969996104001032
    • Suh, S. W., Garnier, P., Aoyama, K., Chen, Y., and Swanson, R. A. (2004) Zinc release contributes to hypoglycemia-induced neuronal death. Neurobiol. Dis. 16, 538-545 (Pubitemid 38942986)
    • (2004) Neurobiology of Disease , vol.16 , Issue.3 , pp. 538-545
    • Won, S.S.1    Garnier, P.2    Aoyama, K.3    Chen, Y.4    Swanson, R.A.5
  • 42
    • 0029777299 scopus 로고    scopus 로고
    • The role of zinc in selective neuronal death after transient global cerebral ischemia
    • Koh, J. Y., Suh, S. W., Gwag, B. J., He, Y. Y., Hsu, C. Y., and Choi, D. W. (1996) The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 272, 1013-1016 (Pubitemid 26259319)
    • (1996) Science , vol.272 , Issue.5264 , pp. 1013-1016
    • Koh, J.-Y.1    Suh, S.W.2    Gwag, B.J.3    He, Y.Y.4    Hsu, C.Y.5    Choi, D.W.6
  • 43
    • 80053627394 scopus 로고    scopus 로고
    • Zinc stimulates tau S214 phosphorylation by the activation of Raf/mitogen-activated protein kinase-kinase/extracellular signal-regulated kinase pathway
    • Kim, I., Park, E. J., Seo, J., Ko, S. J., Lee, J., and Kim, C. H. (2011) Zinc stimulates tau S214 phosphorylation by the activation of Raf/mitogen-activated protein kinase-kinase/extracellular signal-regulated kinase pathway. Neuroreport. 22, 839-844
    • (2011) Neuroreport. , vol.22 , pp. 839-844
    • Kim, I.1    Park, E.J.2    Seo, J.3    Ko, S.J.4    Lee, J.5    Kim, C.H.6
  • 44
    • 20444464441 scopus 로고    scopus 로고
    • Membrane depolarization induces the undulating phosphorylation/ dephosphorylation of glycogen synthase kinase 3β, and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells
    • DOI 10.1074/jbc.M413987200
    • Lee, Y. I., Seo, M., Kim, Y., Kim, S. Y., Kang, U. G., Kim, Y. S., and Juhnn, Y. S. (2005) Membrane depolarization induces the undulating phosphorylation/dephosphorylation of glycogen synthase kinase 3β, and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells. J. Biol. Chem. 280, 22044-22052 (Pubitemid 40827859)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22044-22052
    • Lee, Y.-I.1    Seo, M.2    Kim, Y.3    Kim, S.-Y.4    Kang, U.G.5    Kim, Y.-S.6    Juhnn, Y.-S.7
  • 45
    • 0019877124 scopus 로고
    • Phosphotyrosylprotein phosphatase. Specific inhibition by Zn
    • Brautigan, D. L., Bornstein, P., and Gallis, B. (1981) Phosphotyrosylprotein phosphatase. Specific inhibition by Zn. J. Biol. Chem. 256, 6519-6522
    • (1981) J. Biol. Chem. , vol.256 , pp. 6519-6522
    • Brautigan, D.L.1    Bornstein, P.2    Gallis, B.3
  • 46
    • 34249876632 scopus 로고    scopus 로고
    • Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40
    • DOI 10.1038/nsmb1254, PII NSMB1254
    • Chen, Y., Xu, Y., Bao, Q., Xing, Y., Li, Z., Lin, Z., Stock, J. B., Jeffrey, P. D., and Shi, Y. (2007) Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40. Nat. Struct. Mol. Biol. 14, 527-534 (Pubitemid 46871815)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.6 , pp. 527-534
    • Chen, Y.1    Xu, Y.2    Bao, Q.3    Xing, Y.4    Li, Z.5    Lin, Z.6    Stock, J.B.7    Jeffrey, P.D.8    Shi, Y.9


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