메뉴 건너뛰기




Volumn 127, Issue 3, 2004, Pages 649-658

Phosphorylation of tau at THR212 and SER214 in human neuronal and glial cultures: The role of AKT

Author keywords

AD; Akt; Akt protein kinase B; Alzheimer's disease; AT100; c Akt; constitutively active Akt; day in vitro; DIV; glycogen synthase kinase; glycogen synthase kinase 3 ; GSK3; human astrocytes; human neurons; IGF 1; okadaic acid; protein kinase A

Indexed keywords

OKADAIC ACID; PHOSPHOTRANSFERASE; PROTEIN KINASE B; TAU PROTEIN;

EID: 3342936441     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2004.05.036     Document Type: Article
Times cited : (35)

References (51)
  • 1
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B: Comparison with MAPKAP kinase-1 and p70 s6 kinase
    • Alessi D.R., Caudwell F.B., Andjelkovic M., Hemmings B.A., Cohen P. Molecular basis for the substrate specificity of protein kinase B Comparison with MAPKAP kinase-1 and p70 s6 kinase. FEBS Lett. 399:1996;333-338
    • (1996) FEBS Lett , vol.399 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    Andjelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 2
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • Billingsley M.L., Kincaid R.L. Regulated phosphorylation and dephosphorylation of tau protein Effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J. 323:1997;577-591
    • (1997) Biochem J , vol.323 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 3
    • 0027198565 scopus 로고
    • The balance between tau protein's microtubule growth and nucleation activities: Implications for the formation of axonal microtubules
    • Brandt R., Lee G. The balance between tau protein's microtubule growth and nucleation activities Implications for the formation of axonal microtubules. J Neurochem. 61:1993;997-1005
    • (1993) J Neurochem , vol.61 , pp. 997-1005
    • Brandt, R.1    Lee, G.2
  • 5
    • 0033587742 scopus 로고    scopus 로고
    • Lithium activates the serine/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons
    • Chalecka-Franaszek E., Chuang D.M. Lithium activates the serine/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons. Proc Natl Acad Sci USA. 96:1999;8745-8750
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8745-8750
    • Chalecka-Franaszek, E.1    Chuang, D.M.2
  • 6
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland D.W., Hwo S.Y., Kirschner M.W. Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J Mol Biol. 116:1977;227-247
    • (1977) J Mol Biol , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 7
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., 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.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 8
    • 0037415737 scopus 로고    scopus 로고
    • Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex
    • Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H. Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex. EMBO J. 22:2003;494-501
    • (2003) EMBO J , vol.22 , pp. 494-501
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Yeo, M.4    Good, V.M.5    Thompson, V.6    Dale, T.C.7    Pearl, L.H.8
  • 9
    • 0037051935 scopus 로고    scopus 로고
    • Modelling Alzheimer's specific abnormal tau phosphorylation independently of GSK3beta and PKA activities
    • Delobel P., Flament S., Hamdane M., Delacourte A., Vilain J.P., Buee L. Modelling Alzheimer's specific abnormal tau phosphorylation independently of GSK3beta and PKA activities. FEBS Lett. 516:2002;151-155
    • (2002) FEBS Lett , vol.516 , pp. 151-155
    • Delobel, P.1    Flament, S.2    Hamdane, M.3    Delacourte, A.4    Vilain, J.P.5    Buee, L.6
  • 11
    • 0042734922 scopus 로고    scopus 로고
    • Akt is a molecular target for signal transduction therapy in brain ischemic insult
    • Fukunaga K., Kawano T. Akt is a molecular target for signal transduction therapy in brain ischemic insult. J Pharmacol Sci. 92:2003;317-327
    • (2003) J Pharmacol Sci , vol.92 , pp. 317-327
    • Fukunaga, K.1    Kawano, T.2
  • 12
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling
    • Grimes C.A., 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
  • 13
    • 0030750558 scopus 로고    scopus 로고
    • Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites
    • Hoffmann R., Lee V.M.Y., Leight S., Varga I., Otvos L. Jr. Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry. 36:1997;8114-8124
    • (1997) Biochemistry , vol.36 , pp. 8114-8124
    • Hoffmann, R.1    Lee, V.M.Y.2    Leight, S.3    Varga, I.4    Otvos Jr., L.5
  • 14
    • 0030748390 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons
    • Hong M., Lee V.M. Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons. J Biol Chem. 272:1997;19547-19553
    • (1997) J Biol Chem , vol.272 , pp. 19547-19553
    • Hong, M.1    Lee, V.M.2
  • 15
    • 0036311771 scopus 로고    scopus 로고
    • The aging brain: Changes in the neuronal/insulin receptor signal transduction cascade trigger late-onset sporadic alzheimer disease (SAD): A mini-review
    • Hoyer S. The aging brain Changes in the neuronal/insulin receptor signal transduction cascade trigger late-onset sporadic alzheimer disease (SAD): a mini-review. J Neural Transm. 109:2002;991-1002
    • (2002) J Neural Transm , vol.109 , pp. 991-1002
    • Hoyer, S.1
  • 17
    • 0031827311 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor stimulates neurite outgrowth in a calretinin-enriched neuronal culture system
    • Iwasaki K., Isaacs K.R., Jacobowitz D.M. Brain-derived neurotrophic factor stimulates neurite outgrowth in a calretinin-enriched neuronal culture system. Int J Dev Neurosci. 16:1998;135-145
    • (1998) Int J Dev Neurosci , vol.16 , pp. 135-145
    • Iwasaki, K.1    Isaacs, K.R.2    Jacobowitz, D.M.3
  • 20
    • 0033612919 scopus 로고    scopus 로고
    • Sequence of neurodegeneration and accumulation of phosphorylated tau in cultured neurons after okadaic acid treatment
    • Kim D., Su J., Cotman C.W. Sequence of neurodegeneration and accumulation of phosphorylated tau in cultured neurons after okadaic acid treatment. Brain Res. 839:1999;253-262
    • (1999) Brain Res , vol.839 , pp. 253-262
    • Kim, D.1    Su, J.2    Cotman, C.W.3
  • 21
    • 10744223843 scopus 로고    scopus 로고
    • Epigallocatechin gallate protects nerve growth factor differentiated PC12 cells from oxidative-radical-stress-induced apoptosis through its effect on phosphoinositide 3-kinase/Akt and glycogen synthase kinase-3
    • Koh S.H., Kim S.H., Kwon H., Park Y., Kim K.S., Song C.W., Kim J., Kim M.H., Yu H.J., Henkel J.S., Jung H.K. Epigallocatechin gallate protects nerve growth factor differentiated PC12 cells from oxidative-radical-stress-induced apoptosis through its effect on phosphoinositide 3-kinase/Akt and glycogen synthase kinase-3. Brain Res Mol Brain Res. 118:2003;72-81
    • (2003) Brain Res Mol Brain Res , vol.118 , pp. 72-81
    • Koh, S.H.1    Kim, S.H.2    Kwon, H.3    Park, Y.4    Kim, K.S.5    Song, C.W.6    Kim, J.7    Kim, M.H.8    Yu, H.J.9    Henkel, J.S.10    Jung, H.K.11
  • 23
    • 0242409714 scopus 로고    scopus 로고
    • Akt/PKB Kinase phosphorylates separately Thr212 and Ser214 of tau protein in vitro
    • Ksiezak-Reding H., Pyo H.K., Feinstein B., Pasinetti G.M. Akt/PKB Kinase phosphorylates separately Thr212 and Ser214 of tau protein in vitro. Biochim Biophys Acta. 1639:2003;159-168
    • (2003) Biochim Biophys Acta , vol.1639 , pp. 159-168
    • Ksiezak-Reding, H.1    Pyo, H.K.2    Feinstein, B.3    Pasinetti, G.M.4
  • 24
    • 0035877156 scopus 로고    scopus 로고
    • Expression, purification, characterization and homology modeling of active Akt/PKB, a key enzyme involved in cell survival signaling
    • Kumar C.C., Diao R., Yin Z., Liu Y., Samatar A.A., Madison V., Xiao L. Expression, purification, characterization and homology modeling of active Akt/PKB, a key enzyme involved in cell survival signaling. Biochim Biophys Acta. 1526:2001;257-268
    • (2001) Biochim Biophys Acta , vol.1526 , pp. 257-268
    • Kumar, C.C.1    Diao, R.2    Yin, Z.3    Liu, Y.4    Samatar, A.A.5    Madison, V.6    Xiao, L.7
  • 25
    • 0026484937 scopus 로고
    • Characterization of primary human fetal dissociated central nervous system cultures with an emphasis on microglia
    • Lee S.C., Liu W., Brosnan C.F., Dickson D.W. Characterization of primary human fetal dissociated central nervous system cultures with an emphasis on microglia. Lab Invest. 67:1992;465-476
    • (1992) Lab Invest , vol.67 , pp. 465-476
    • Lee, S.C.1    Liu, W.2    Brosnan, C.F.3    Dickson, D.W.4
  • 26
    • 0038982381 scopus 로고    scopus 로고
    • Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau
    • Leger J., Kempf M., Lee G., Brandt R. Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau. J Biol Chem. 272:1997;8441-8446
    • (1997) J Biol Chem , vol.272 , pp. 8441-8446
    • Leger, J.1    Kempf, M.2    Lee, G.3    Brandt, R.4
  • 27
    • 85047697574 scopus 로고    scopus 로고
    • A novel conditional Akt 'survival switch' reversibly protects cells from apoptosis
    • Li B., Desai S.A., MacCorkle-Chosnek R.A., Fan L., Spencer D.M. A novel conditional Akt 'survival switch' reversibly protects cells from apoptosis. Gene Ther. 9:2002;233-244
    • (2002) Gene Ther , vol.9 , pp. 233-244
    • Li, B.1    Desai, S.A.2    MacCorkle-Chosnek, R.A.3    Fan, L.4    Spencer, D.M.5
  • 28
    • 0032500861 scopus 로고    scopus 로고
    • Alzheimer-specific epitope of AT100 in transfected cell lines with tau: Toward an efficient cell model of tau abnormal phosphorylation
    • Mailliot C., Bussiere T., Caillet-Boudin M.L., Delacourte A., Buee L. Alzheimer-specific epitope of AT100 in transfected cell lines with tau Toward an efficient cell model of tau abnormal phosphorylation. Neurosci Lett. 255:1998;13-16
    • (1998) Neurosci Lett , vol.255 , pp. 13-16
    • Mailliot, C.1    Bussiere, T.2    Caillet-Boudin, M.L.3    Delacourte, A.4    Buee, L.5
  • 29
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow E.M., Stamer K., Vogel R., Thies E., Mandelkow E. Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging. 24:2003;1079-1085
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 30
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E.S., Shin R.W., Billingsley M.L., Van deVoorde A., O'Connor M., Trojanowski J.Q., Lee V.M. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron. 13:1994;989-1002
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    Van Devoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 31
    • 0037192820 scopus 로고    scopus 로고
    • Differential signaling of cyclic AMP: Opposing effects of exchange protein directly activated by cyclic AMP and cAMP-dependent protein kinase on protein kinase b activation
    • Mei F.C., Qiao J., Tsygankova O.M., Meinkoth J.L., Quilliam L.A., Cheng X. Differential signaling of cyclic AMP Opposing effects of exchange protein directly activated by cyclic AMP and cAMP-dependent protein kinase on protein kinase b activation. J Biol Chem. 277:2002;11497-11504
    • (2002) J Biol Chem , vol.277 , pp. 11497-11504
    • Mei, F.C.1    Qiao, J.2    Tsygankova, O.M.3    Meinkoth, J.L.4    Quilliam, L.A.5    Cheng, X.6
  • 32
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • Millward T.A., Zolnierowicz S., Hemmings B.A. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci. 24:1999;186-191
    • (1999) Trends Biochem Sci , vol.24 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 36
    • 0024320852 scopus 로고
    • Development of N-methyl-D-aspartate excitotoxicity in cultured hippocampal neurons
    • Peterson C., Neal J.H., Cotman C.W. Development of N-methyl-D-aspartate excitotoxicity in cultured hippocampal neurons. Brain Res Dev Brain Res. 48:1989;187-195
    • (1989) Brain Res Dev Brain Res , vol.48 , pp. 187-195
    • Peterson, C.1    Neal, J.H.2    Cotman, C.W.3
  • 37
    • 0036154215 scopus 로고    scopus 로고
    • Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes
    • Resjo S., Goransson O., Harndahl L., Zolnierowicz S., Manganiello V., Degerman E. Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal. 14:2002;231-238
    • (2002) Cell Signal , vol.14 , pp. 231-238
    • Resjo, S.1    Goransson, O.2    Harndahl, L.3    Zolnierowicz, S.4    Manganiello, V.5    Degerman, E.6
  • 38
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-jun n-terminal kinase and p38, and glycogen synthase kinase-3beta
    • Reynolds C.H., Betts J.C., Blackstock W.P., Nebreda A.R., Anderton B.H. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry Differences in vitro between the mitogen-activated protein kinases ERK2, c-jun n-terminal kinase and p38, and glycogen synthase kinase-3beta. J Neurochem. 74:2000;1587-1595
    • (2000) J Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Anderton, B.H.5
  • 40
    • 0035955512 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase 3beta in intact mammalian cells influences the stability of microtubules
    • Sang H., Lu Z., Li Y., Ru B., Wang W., Chen J. Phosphorylation of tau by glycogen synthase kinase 3beta in intact mammalian cells influences the stability of microtubules. Neurosci Lett. 312:2001;141-144
    • (2001) Neurosci Lett , vol.312 , pp. 141-144
    • Sang, H.1    Lu, Z.2    Li, Y.3    Ru, B.4    Wang, W.5    Chen, J.6
  • 41
    • 0042733215 scopus 로고    scopus 로고
    • Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells
    • Sasaki K., Sato M., Umezawa Y. Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells. J Biol Chem. 278:2003;30945-30951
    • (2003) J Biol Chem , vol.278 , pp. 30945-30951
    • Sasaki, K.1    Sato, M.2    Umezawa, Y.3
  • 42
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A., Biernat J., von Bergen M., Mandelkow E., Mandelkow E.M. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry. 38:1999;3549-3558
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 44
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K., Vogel R., Thies E., Mandelkow E., Mandelkow E.M. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol. 156:2002;1051-1063
    • (2002) J Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 45
    • 0036759157 scopus 로고    scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • Stein T.D., Johnson J.A. Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways. J Neurosci. 22:2002;7380-7388
    • (2002) J Neurosci , vol.22 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 46
    • 0035884914 scopus 로고    scopus 로고
    • Hyperosmotic stress-induced apoptosis and tau phosphorylation in human neuroblastoma cells
    • Stoothoff W.H., Johnson G.V. Hyperosmotic stress-induced apoptosis and tau phosphorylation in human neuroblastoma cells. J Neurosci Res. 65:2001;573-582
    • (2001) J Neurosci Res , vol.65 , pp. 573-582
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 47
    • 0036323020 scopus 로고    scopus 로고
    • The role of tau in Alzheimer's disease
    • Trojanowski J.Q., Lee V.M. The role of tau in Alzheimer's disease. Med Clin North Am. 86:2002;615-627
    • (2002) Med Clin North Am , vol.86 , pp. 615-627
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 48
    • 0032864021 scopus 로고    scopus 로고
    • Depolarization and neurotrophins converge on the phosphatidylinositol 3-kinase-Akt pathway to synergistically regulate neuronal survival
    • Vaillant A.R., Mazzoni I., Tudan C., Boudreau M., Kaplan D.R., Miller F.D. Depolarization and neurotrophins converge on the phosphatidylinositol 3-kinase-Akt pathway to synergistically regulate neuronal survival. J Cell Biol. 146:1999;955-966
    • (1999) J Cell Biol , vol.146 , pp. 955-966
    • Vaillant, A.R.1    Mazzoni, I.2    Tudan, C.3    Boudreau, M.4    Kaplan, D.R.5    Miller, F.D.6
  • 50
    • 0034518163 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) a neuroprotective trophic factor acting via the Akt kinase pathway
    • Zheng W.-H., Kar S., Dore S., Quirion R. Insulin-like growth factor-1 (IGF-1) A neuroprotective trophic factor acting via the Akt kinase pathway. J Neural Transm Suppl. 60:2000;262-272
    • (2000) J Neural Transm Suppl , vol.60 , pp. 262-272
    • Zheng, W.-H.1    Kar, S.2    Dore, S.3    Quirion, R.4
  • 51
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase a at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhofer Q., Biernat J., Mandelkow E.M., Illenberger S., Godemann R., Mandelkow E. Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical- filament-like conformation. Eur J Biochem. 252:1998;542-552
    • (1998) Eur J Biochem , vol.252 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.