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Volumn 580, Issue 10, 2006, Pages 2503-2511

The involvement of glycogen synthase kinase-3 and protein phosphatase-2A in lactacystin-induced tau accumulation

Author keywords

Glycogen synthase kinase 3; Hyperphosphorylation; Proteasome; Protein phosphatase 2A; Tau

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3; LACTACYSTIN; LITHIUM CHLORIDE; PACLITAXEL; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEASOME; SERINE; TAU PROTEIN;

EID: 33646083672     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.03.073     Document Type: Article
Times cited : (28)

References (50)
  • 5
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • Ferrer I., Gomez-Isla T., Puig B., Freixes M., Ribe E., Dalfo E., and Avila J. Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies. Curr. Alzheimer Res. 2 (2005) 3-18
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3    Freixes, M.4    Ribe, E.5    Dalfo, E.6    Avila, J.7
  • 7
    • 0036769791 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase in Alzheimer's disease
    • Tian Q., and Wang J. Role of serine/threonine protein phosphatase in Alzheimer's disease. Neurosignals 11 (2002) 262-269
    • (2002) Neurosignals , vol.11 , pp. 262-269
    • Tian, Q.1    Wang, J.2
  • 10
    • 0036942289 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway
    • Cardozo C., and Michaud C. Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway. Arch. Biochem. Biophys. 408 (2002) 103-110
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 103-110
    • Cardozo, C.1    Michaud, C.2
  • 12
    • 15244345543 scopus 로고    scopus 로고
    • Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons
    • Brown M.R., Bondada V., Keller J.N., Thorpe J., and Geddes J.W. Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons. J. Alzheimer's Dis. 7 (2005) 15-24
    • (2005) J. Alzheimer's Dis. , vol.7 , pp. 15-24
    • Brown, M.R.1    Bondada, V.2    Keller, J.N.3    Thorpe, J.4    Geddes, J.W.5
  • 13
    • 33646078288 scopus 로고    scopus 로고
    • Zhang, Y.J., Xu, Y.F., Liu, Y.H., Yin, J., Li, H.L., Wang, Q., and Wang, J.Z. Peroxynitrite induces Alzheimer-like tau modifications and accumulation in rat brain and its underlying mechanisms, FASEB J. (in press).
  • 14
    • 10944273982 scopus 로고    scopus 로고
    • Phosphorylated tau and the neurodegenerative foldopathies
    • Kosik K.S., and Shimura H. Phosphorylated tau and the neurodegenerative foldopathies. Biochim. Biophys. Acta 1739 (2005) 298-310
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 298-310
    • Kosik, K.S.1    Shimura, H.2
  • 15
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J.N., Hanni K.B., and Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75 (2000) 436-439
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 17
    • 0037383052 scopus 로고    scopus 로고
    • Relationship between beta-amyloid degradation and the 26S proteasome in neural cells
    • Lopez Salon M., Pasquini L., Besio Moreno M., Pasquini J.M., and Soto E. Relationship between beta-amyloid degradation and the 26S proteasome in neural cells. Exp. Neurol. 180 (2003) 131-143
    • (2003) Exp. Neurol. , vol.180 , pp. 131-143
    • Lopez Salon, M.1    Pasquini, L.2    Besio Moreno, M.3    Pasquini, J.M.4    Soto, E.5
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett G.T., Goedert M., Jakes R., Merrick S.E., Trojanowski J.Q., and Lee V.M. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10 (1993) 1089-1099
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 20
    • 0030813929 scopus 로고    scopus 로고
    • Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons
    • Merrick S.E., Trojanowski J.Q., and Lee V.M. Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons. J. Neurosci. 17 (1997) 5726-5737
    • (1997) J. Neurosci. , vol.17 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 21
    • 0346434153 scopus 로고    scopus 로고
    • Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory
    • Liu S.J., Zhang A.H., Li H.L., Wang Q., Deng H.M., Netzer W.J., Xu H.X., and Wang J.Z. Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J. Neurochem. 87 (2003) 1333-1344
    • (2003) J. Neurochem. , vol.87 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3    Wang, Q.4    Deng, H.M.5    Netzer, W.J.6    Xu, H.X.7    Wang, J.Z.8
  • 22
    • 0032540459 scopus 로고    scopus 로고
    • The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases
    • Tanaka T., Zhong J., Iqbal K., Trenkner E., and Grundke-Iqbal I. The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 426 (1998) 248-254
    • (1998) FEBS Lett. , vol.426 , pp. 248-254
    • Tanaka, T.1    Zhong, J.2    Iqbal, K.3    Trenkner, E.4    Grundke-Iqbal, I.5
  • 23
    • 0034598963 scopus 로고    scopus 로고
    • Inactivation of glycogen synthase kinase-3 by protein kinase C delta: implications for regulation of tau phosphorylation
    • Tsujio I., Tanaka T., Kudo T., Nishikawa T., Shinozaki K., Grundke-Iqbal I., Iqbal K., and Takeda M. Inactivation of glycogen synthase kinase-3 by protein kinase C delta: implications for regulation of tau phosphorylation. FEBS Lett. 469 (2000) 111-117
    • (2000) FEBS Lett. , vol.469 , pp. 111-117
    • Tsujio, I.1    Tanaka, T.2    Kudo, T.3    Nishikawa, T.4    Shinozaki, K.5    Grundke-Iqbal, I.6    Iqbal, K.7    Takeda, M.8
  • 24
    • 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
  • 25
    • 0028172239 scopus 로고
    • The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases
    • Mawal-Dewan M., Henley J., Van de Voorde A., Trojanowski J.Q., and Lee V.M. The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269 (1994) 30981-30987
    • (1994) J. Biol. Chem. , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van de Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 26
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: on protein death and cell life
    • Ciechancver A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17 (1998) 7151-7160
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechancver, A.1
  • 27
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • de Vrij F.M., Fischer D.F., van Leeuwen F.W., and Hol E.M. Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog. Neurobiol. 74 (2004) 249-270
    • (2004) Prog. Neurobiol. , vol.74 , pp. 249-270
    • de Vrij, F.M.1    Fischer, D.F.2    van Leeuwen, F.W.3    Hol, E.M.4
  • 28
    • 22144460186 scopus 로고    scopus 로고
    • Proteinaceous intracellular inclusions in neurodegenerative disorders
    • Dziewulska D., and Rafalowska J. Proteinaceous intracellular inclusions in neurodegenerative disorders. Folia Neuropathol. 43 (2005) 51-63
    • (2005) Folia Neuropathol. , vol.43 , pp. 51-63
    • Dziewulska, D.1    Rafalowska, J.2
  • 29
    • 0030962262 scopus 로고    scopus 로고
    • p53-dependent induction of apoptosis by proteasome inhibitors
    • Lopes U.G., Erhardt P., Yao R., and Cooper G.M. p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem. 272 (1997) 12893-12896
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 30
    • 0034651104 scopus 로고    scopus 로고
    • Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis
    • Canu N., Barbato C., Ciotti M.T., Serafino A., Dus L., and Calissano P. Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis. J. Neurosci. 20 (2000) 589-599
    • (2000) J. Neurosci. , vol.20 , pp. 589-599
    • Canu, N.1    Barbato, C.2    Ciotti, M.T.3    Serafino, A.4    Dus, L.5    Calissano, P.6
  • 31
    • 0342393043 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells
    • Pasquini L.A., Besio M., Adamo A.M., Pasquini J.M., and Soto E.F. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells. J. Neurosci. Res. 59 (2000) 601-611
    • (2000) J. Neurosci. Res. , vol.59 , pp. 601-611
    • Pasquini, L.A.1    Besio, M.2    Adamo, A.M.3    Pasquini, J.M.4    Soto, E.F.5
  • 33
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H., Schwartz D., Gygi S.P., and Kosik K.S. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279 (2004) 4869-4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 35
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes
    • Jope R.S. Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol. Sci. 24 (2003) 441-443
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 36
    • 0035900678 scopus 로고    scopus 로고
    • Inhibition of 20 S and 26 S proteasome activity by lithium chloride
    • Rice A.M., and Sartorelli A.C. Inhibition of 20 S and 26 S proteasome activity by lithium chloride. J. Biol. Chem. 276 (2001) 42722-42727
    • (2001) J. Biol. Chem. , vol.276 , pp. 42722-42727
    • Rice, A.M.1    Sartorelli, A.C.2
  • 37
    • 27844479156 scopus 로고    scopus 로고
    • A positive feedback loop between glycogen synthase kinase 3β and protein phosphatase 1 after stimulation of NR2B NMDA receptors in forebrain neurons
    • Szatmari E., Habas A., Yang P., Zheng J.J., Hagg T., and Hetman M. A positive feedback loop between glycogen synthase kinase 3β and protein phosphatase 1 after stimulation of NR2B NMDA receptors in forebrain neurons. J. Biol. Chem. 280 (2005) 37526-37535
    • (2005) J. Biol. Chem. , vol.280 , pp. 37526-37535
    • Szatmari, E.1    Habas, A.2    Yang, P.3    Zheng, J.J.4    Hagg, T.5    Hetman, M.6
  • 38
    • 16244398685 scopus 로고    scopus 로고
    • MAP kinase protects G protein-coupled receptor kinase 2 from proteasomal degradation
    • Theilade J., Hansen J.L., Haunso S., and Sheikh S.P. MAP kinase protects G protein-coupled receptor kinase 2 from proteasomal degradation. Biochem. Biophys. Res. Commun. 330 (2005) 685-689
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 685-689
    • Theilade, J.1    Hansen, J.L.2    Haunso, S.3    Sheikh, S.P.4
  • 39
    • 24744444714 scopus 로고    scopus 로고
    • A crucial role for GRK2 in regulation of endothelial cell nitric oxide synthase function in portal hypertension
    • Liu S., Premont R.T., Kontos C.D., Zhu S., and Rockey D.C. A crucial role for GRK2 in regulation of endothelial cell nitric oxide synthase function in portal hypertension. Nat. Med. 11 (2005) 952-958
    • (2005) Nat. Med. , vol.11 , pp. 952-958
    • Liu, S.1    Premont, R.T.2    Kontos, C.D.3    Zhu, S.4    Rockey, D.C.5
  • 40
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A.E., Alessi D.R., Cohen P., Andjelkovich M., and Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (1995) 785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 41
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • Oliver C.J., and Shenolikar S. Physiologic importance of protein phosphatase inhibitors. Front Biosci. 3 (1998) 961-972
    • (1998) Front Biosci. , vol.3 , pp. 961-972
    • Oliver, C.J.1    Shenolikar, S.2
  • 42
    • 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
  • 43
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable inhibitor protein phosphatase 2A from bovine kidney
    • Li M., Guo H., and Damuni Z. Purification and characterization of two potent heat-stable inhibitor protein phosphatase 2A from bovine kidney. Biochemistry 34 (1995) 1988-1996
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 44
    • 0034680902 scopus 로고    scopus 로고
    • Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain
    • Bennecib M., Gong C.X., Grundke-Iqbal I., and Iqbal K. Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain. FEBS Lett. 485 (2000) 87-93
    • (2000) FEBS Lett. , vol.485 , pp. 87-93
    • Bennecib, M.1    Gong, C.X.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 45
    • 0042679509 scopus 로고    scopus 로고
    • Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease
    • Pei J.J., Gong C.X., An W.L., Winblad B., Cowburn R.F., Grundke-Iqbal I., and Iqbal K. Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease. Am. J. Pathol. 163 (2003) 845-858
    • (2003) Am. J. Pathol. , vol.163 , pp. 845-858
    • Pei, J.J.1    Gong, C.X.2    An, W.L.3    Winblad, B.4    Cowburn, R.F.5    Grundke-Iqbal, I.6    Iqbal, K.7
  • 46
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • Kins S., Kurosinski P., Nitsch R.M., and Gotz J. Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am. J. Pathol. 163 (2003) 833-843
    • (2003) Am. J. Pathol. , vol.163 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Gotz, J.4
  • 47
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 48
    • 0012810697 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway of intracellular proteolysis
    • Doherty F.J., Dawson S., and Mayer R.J. The ubiquitin-proteasome pathway of intracellular proteolysis. Essays Biochem. 38 (2002) 51-63
    • (2002) Essays Biochem. , vol.38 , pp. 51-63
    • Doherty, F.J.1    Dawson, S.2    Mayer, R.J.3
  • 49
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R., Grune T., and Davies K.J. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol. Life Sci. 58 (2001) 1442-1450
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.3
  • 50
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., and Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65 (1996) 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3


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