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Volumn 1252, Issue , 2009, Pages 66-75

Inhibition of glycogen synthase kinase-3β downregulates total tau proteins in cultured neurons and its reversal by the blockade of protein phosphatase-2A

Author keywords

Alzheimer's disease; Glycogen synthase kinase 3 ; Lithium; Protein phosphatase 2A; Protein phosphatase 2B; Tau

Indexed keywords

CALCINEURIN; CYCLIN DEPENDENT KINASE 5; GLYCOGEN SYNTHASE KINASE 3BETA; LITHIUM; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; ROSCOVITINE; TACROLIMUS; TAU PROTEIN;

EID: 58349114277     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2008.11.057     Document Type: Article
Times cited : (51)

References (51)
  • 3
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K., Mandelkow E.M., Biernat J., Piwnica-Worms H., and Mandelkow E. Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett. 336 (1993) 417-424
    • (1993) FEBS Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 5
    • 44849144122 scopus 로고    scopus 로고
    • I1PP2A affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A
    • Chen S., Li B., Grundke-Iqbal I., and Iqbal K. I1PP2A affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A. J. Biol. Chem. 283 (2008) 10513-10521
    • (2008) J. Biol. Chem. , vol.283 , pp. 10513-10521
    • Chen, S.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 6
    • 34248222543 scopus 로고    scopus 로고
    • Pharmacologic reductions of total tau levels; implications for the role of microtubule dynamics in regulating tau expression
    • Dickey C.A., Ash P., Klosak N., Lee W.C., Petrucelli L., Hutton M., and Eckman C.B. Pharmacologic reductions of total tau levels; implications for the role of microtubule dynamics in regulating tau expression. Mol. Neurodegener. 1 (2006) 6
    • (2006) Mol. Neurodegener. , vol.1 , pp. 6
    • Dickey, C.A.1    Ash, P.2    Klosak, N.3    Lee, W.C.4    Petrucelli, L.5    Hutton, M.6    Eckman, C.B.7
  • 7
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • Embi N., Rylatt D.B., and Cohen P. Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107 (1980) 519-527
    • (1980) Eur. J. Biochem. , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 8
    • 0034329543 scopus 로고    scopus 로고
    • Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants
    • Flaherty D.B., Soria J.P., Tomasiewicz H.G., and Wood J.G. Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants. J. Neurosci. Res. 62 (2000) 463-472
    • (2000) J. Neurosci. Res. , vol.62 , pp. 463-472
    • Flaherty, D.B.1    Soria, J.P.2    Tomasiewicz, H.G.3    Wood, J.G.4
  • 9
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M.G., Jakes R., Rutherford D., and Crowther R.A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3 (1989) 519-526
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 10
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong C.X., Singh T.J., Grundke-Iqbal I., and Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61 (1993) 921-927
    • (1993) J. Neurochem. , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 11
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling
    • Grimes C.A., and Jope R.S. The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling. Prog. Neurobiol. 65 (2001) 391-426
    • (2001) Prog. Neurobiol. , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 12
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • Hooper C., Killick R., and Lovestone S. The GSK3 hypothesis of Alzheimer's disease. J. Neurochem. 104 (2008) 1433-1439
    • (2008) J. Neurochem. , vol.104 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 13
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami S., Harada A., and Hirokawa N. Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice. Neurosci. Lett. 279 (2000) 129-132
    • (2000) Neurosci. Lett. , vol.279 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 14
    • 0036170771 scopus 로고    scopus 로고
    • Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta
    • Ivaska J., Nissinen L., Immonen N., Eriksson J.E., Kahari V.M., and Heino J. Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta. Mol. Cell. Biol. 22 (2002) 1352-1359
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1352-1359
    • Ivaska, J.1    Nissinen, L.2    Immonen, N.3    Eriksson, J.E.4    Kahari, V.M.5    Heino, J.6
  • 15
    • 0032947795 scopus 로고    scopus 로고
    • Anti-bipolar therapy: mechanism of action of lithium
    • Jope R.S. Anti-bipolar therapy: mechanism of action of lithium. Mol. Psychiatry 4 (1999) 117-128
    • (1999) Mol. Psychiatry , vol.4 , pp. 117-128
    • Jope, R.S.1
  • 16
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins S., Crameri A., Evans D.R., Hemmings B.A., Nitsch R.M., and Gotz J. Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276 (2001) 38193-38200
    • (2001) J. Biol. Chem. , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Gotz, J.6
  • 17
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein P.S., and Melton D.A. A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 8455-8459
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 18
    • 0036103182 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection
    • Li X., Bijur G.N., and Jope R.S. Glycogen synthase kinase-3beta, mood stabilizers, and neuroprotection. Bipolar Disord. 4 (2002) 137-144
    • (2002) Bipolar Disord. , vol.4 , pp. 137-144
    • Li, X.1    Bijur, G.N.2    Jope, R.S.3
  • 19
    • 47849120642 scopus 로고    scopus 로고
    • decrease of protein phosphatase 2a and its association with accumulation and hyperphosphorylation of tau in down syndrome
    • Liang Z., Liu F., Iqbal K., Grundke-Iqbal I., Wegiel J., and Gong C.X. decrease of protein phosphatase 2a and its association with accumulation and hyperphosphorylation of tau in down syndrome. J. Alzheimer's Dis. 13 (2008) 295-302
    • (2008) J. Alzheimer's Dis. , vol.13 , pp. 295-302
    • Liang, Z.1    Liu, F.2    Iqbal, K.3    Grundke-Iqbal, I.4    Wegiel, J.5    Gong, C.X.6
  • 20
    • 34548568958 scopus 로고    scopus 로고
    • GSK-3beta acts downstream of PP2A and the PI 3-kinase-Akt pathway, and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis
    • Lin C.F., Chen C.L., Chiang C.W., Jan M.S., Huang W.C., and Lin Y.S. GSK-3beta acts downstream of PP2A and the PI 3-kinase-Akt pathway, and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis. J. Cell. Sci. 120 (2007) 2935-2943
    • (2007) J. Cell. Sci. , vol.120 , pp. 2935-2943
    • Lin, C.F.1    Chen, C.L.2    Chiang, C.W.3    Jan, M.S.4    Huang, W.C.5    Lin, Y.S.6
  • 21
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • Liu F., Grundke-Iqbal I., Iqbal K., and Gong C.X. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci. 22 (2005) 1942-1950
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 22
    • 47049089041 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase-3 inhibits protein phosphatase-2A and the underlying mechanisms
    • Liu G.P., Zhang Y., Yao X.Q., Zhang C.E., Fang J., Wang Q., and Wang J.Z. Activation of glycogen synthase kinase-3 inhibits protein phosphatase-2A and the underlying mechanisms. Neurobiol. Aging 29 9 (2007) 1348-1358
    • (2007) Neurobiol. Aging , vol.29 , Issue.9 , pp. 1348-1358
    • Liu, G.P.1    Zhang, Y.2    Yao, X.Q.3    Zhang, C.E.4    Fang, J.5    Wang, Q.6    Wang, J.Z.7
  • 23
    • 24144440042 scopus 로고    scopus 로고
    • Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms
    • Liu R., Pei J.J., Wang X.C., Zhou X.W., Tian Q., Winblad B., and Wang J.Z. Acute anoxia induces tau dephosphorylation in rat brain slices and its possible underlying mechanisms. J. Neurochem. 94 (2005) 1225-1234
    • (2005) J. Neurochem. , vol.94 , pp. 1225-1234
    • Liu, R.1    Pei, J.J.2    Wang, X.C.3    Zhou, X.W.4    Tian, Q.5    Winblad, B.6    Wang, J.Z.7
  • 25
    • 34247865533 scopus 로고    scopus 로고
    • A chaperone-dependent GSK3beta transitional intermediate mediates activation-loop autophosphorylation
    • Lochhead P.A., Kinstrie R., Sibbet G., Rawjee T., Morrice N., and Cleghon V. A chaperone-dependent GSK3beta transitional intermediate mediates activation-loop autophosphorylation. Mol. Cell 24 (2006) 627-633
    • (2006) Mol. Cell , vol.24 , pp. 627-633
    • Lochhead, P.A.1    Kinstrie, R.2    Sibbet, G.3    Rawjee, T.4    Morrice, N.5    Cleghon, V.6
  • 26
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer's disease
    • Maeda S., Sahara N., Saito Y., Murayama S., Ikai A., and Takashima A. Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer's disease. Neurosci. Res. 54 (2006) 197-201
    • (2006) Neurosci. Res. , vol.54 , pp. 197-201
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, S.4    Ikai, A.5    Takashima, A.6
  • 27
    • 0031037714 scopus 로고    scopus 로고
    • Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5
    • Meijer L., Borgne A., Mulner O., Chong J.P., Blow J.J., Inagaki N., Inagaki M., Delcros J.G., and Moulinoux J.P. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5. Eur. J. Biochem. 243 (1997) 527-536
    • (1997) Eur. J. Biochem. , vol.243 , pp. 527-536
    • Meijer, L.1    Borgne, A.2    Mulner, O.3    Chong, J.P.4    Blow, J.J.5    Inagaki, N.6    Inagaki, M.7    Delcros, J.G.8    Moulinoux, J.P.9
  • 29
    • 38049170722 scopus 로고    scopus 로고
    • Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2A- and glycogen synthase kinase-3 -dependent phosphorylation of Tau
    • Meske V., Albert F., and Ohm T.G. Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2A- and glycogen synthase kinase-3 -dependent phosphorylation of Tau. J. Biol. Chem. 283 (2008) 100-109
    • (2008) J. Biol. Chem. , vol.283 , pp. 100-109
    • Meske, V.1    Albert, F.2    Ohm, T.G.3
  • 32
    • 0032577899 scopus 로고    scopus 로고
    • WNT-1 and HGF regulate GSK3 beta activity and beta-catenin signaling in mammary epithelial cells
    • Papkoff J., and Aikawa M. WNT-1 and HGF regulate GSK3 beta activity and beta-catenin signaling in mammary epithelial cells. Biochem. Biophys. Res. Commun. 247 (1998) 851-858
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 851-858
    • Papkoff, J.1    Aikawa, M.2
  • 33
    • 0035823496 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse
    • Planel E., Yasutake K., Fujita S.C., and Ishiguro K. Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse. J. Biol. Chem. 276 (2001) 34298-34306
    • (2001) J. Biol. Chem. , vol.276 , pp. 34298-34306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 34
    • 11144227267 scopus 로고    scopus 로고
    • Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis
    • Rametti A., Esclaire F., Yardin C., and Terro F. Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis. J. Biol. Chem. 279 (2004) 54518-54528
    • (2004) J. Biol. Chem. , vol.279 , pp. 54518-54528
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3    Terro, F.4
  • 35
    • 40849095832 scopus 로고    scopus 로고
    • Lithium down-regulates tau in cultured cortical neurons: a possible mechanism of neuroprotection
    • Rametti A., Esclaire F., Yardin C., Cogne N., and Terro F. Lithium down-regulates tau in cultured cortical neurons: a possible mechanism of neuroprotection. Neurosci. Lett. 434 (2008) 93-98
    • (2008) Neurosci. Lett. , vol.434 , pp. 93-98
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3    Cogne, N.4    Terro, F.5
  • 39
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A
    • Seeling J.M., Miller J.R., Gil R., Moon R.T., White R., and Virshup D.M. Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science 283 (1999) 2089-2091
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 41
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation
    • Stambolic V., and Woodgett J.R. Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem. J. 303 Pt 3 (1994) 701-704
    • (1994) Biochem. J. , vol.303 , Issue.PART 3 , pp. 701-704
    • Stambolic, V.1    Woodgett, J.R.2
  • 43
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H., Grundke-Iqbal I., and Iqbal K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am. J. Pathol. 166 (2005) 1761-1771
    • (2005) Am. J. Pathol. , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 45
    • 0037390480 scopus 로고    scopus 로고
    • Lithium, but not valproate, induces the serine/threonine phosphatase activity of protein phosphatase 2A in the rat brain, without affecting its expression
    • Tsuji S., Morinobu S., Tanaka K., Kawano K., and Yamawaki S. Lithium, but not valproate, induces the serine/threonine phosphatase activity of protein phosphatase 2A in the rat brain, without affecting its expression. J. Neural Transm. 110 (2003) 413-425
    • (2003) J. Neural Transm. , vol.110 , pp. 413-425
    • Tsuji, S.1    Morinobu, S.2    Tanaka, K.3    Kawano, K.4    Yamawaki, S.5
  • 46
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V., Schuck T., Trojanowski J.Q., and Lee V.M. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp. Neurol. 168 (2001) 402-412
    • (2001) Exp. Neurol. , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 47
    • 34548190489 scopus 로고    scopus 로고
    • An aluminum-based rat model for Alzheimer's disease exhibits oxidative damage, inhibition of PP2A activity, hyperphosphorylated tau, and granulovacuolar degeneration
    • Walton J.R. An aluminum-based rat model for Alzheimer's disease exhibits oxidative damage, inhibition of PP2A activity, hyperphosphorylated tau, and granulovacuolar degeneration. J. Inorg. Biochem. 101 (2007) 1275-1284
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1275-1284
    • Walton, J.R.1
  • 48
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
    • Wang J.Z., Gong C.X., Zaidi T., Grundke-Iqbal I., and Iqbal K. Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem. 270 (1995) 4854-4860
    • (1995) J. Biol. Chem. , vol.270 , pp. 4854-4860
    • Wang, J.Z.1    Gong, C.X.2    Zaidi, T.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 49
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang Q.M., Fiol C.J., DePaoli-Roach A.A., and Roach P.J. Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J. Biol. Chem. 269 (1994) 14566-14574
    • (1994) J. Biol. Chem. , vol.269 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    DePaoli-Roach, A.A.3    Roach, P.J.4
  • 50
    • 14944347390 scopus 로고    scopus 로고
    • Inactivation of GSK-3beta in okadaic acid-induced neurodegeneration: relevance to Alzheimer's disease
    • Yoon S.Y., Choi J.E., Huh J.W., Hwang O., Nam Hong H., and Kim D. Inactivation of GSK-3beta in okadaic acid-induced neurodegeneration: relevance to Alzheimer's disease. NeuroReport 16 (2005) 223-227
    • (2005) NeuroReport , vol.16 , pp. 223-227
    • Yoon, S.Y.1    Choi, J.E.2    Huh, J.W.3    Hwang, O.4    Nam Hong, H.5    Kim, D.6


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