메뉴 건너뛰기




Volumn 9, Issue 3, 1997, Pages 220-234

Selective phosphorylation of adult tau isoforms in mature hippocampal neurons exposed to fibrillar aβ

Author keywords

[No Author keywords available]

Indexed keywords

TAU PROTEIN;

EID: 0030879686     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1006/mcne.1997.0615     Document Type: Article
Times cited : (176)

References (54)
  • 1
    • 0027533173 scopus 로고
    • Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein
    • Arioki M., Tsukamoto M., Ishiguro K., Kato R., Sato, Imahori K., Uchita T. Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein. J. Neurochem. 60:1993;461-468.
    • (1993) J. Neurochem. , vol.60 , pp. 461-468
    • Arioki, M.1    Tsukamoto, M.2    Ishiguro, K.3    Kato, R.4    Sato5    Imahori, K.6    Uchita, T.7
  • 2
    • 0027757042 scopus 로고
    • Abnormal Alzheimer's like phosphorylation of tau protein by cyclin-dependent cdk2 and cdk5
    • Bauman K., Mandelkow E-M., Biernat J., Piwnica-Worms H., Mandelkow E. Abnormal Alzheimer's like phosphorylation of tau protein by cyclin-dependent cdk2 and cdk5. FEBS Lett. 36:1993;417-424.
    • (1993) FEBS Lett. , vol.36 , pp. 417-424
    • Bauman, K.1    Mandelkow, E-M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 3
    • 0017277818 scopus 로고
    • Assay of protein in the presence of interfering material
    • Bensadaun A., Weinstein R. Assay of protein in the presence of interfering material. Anal. Biochem. 70:1976;241-250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadaun, A.1    Weinstein, R.2
  • 4
    • 0000854861 scopus 로고
    • Growth of a rat neuroblastoma cell line in serum-free supplemented media
    • Bottenstein J. E., Sato G. H. Growth of a rat neuroblastoma cell line in serum-free supplemented media. Proc. Natl. Acad. Sci. USA. 76:1979;514-517.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 514-517
    • Bottenstein, J.E.1    Sato, G.H.2
  • 5
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser 396 in Alzheimer's disease recapitulates development and contributes to reduce microtubule binding
    • Bramblett G. T., Goedert M., Jakes R., Merrick S. E., Trojanowski J. Q., Lee V. M.-Y. Abnormal tau phosphorylation at Ser 396 in Alzheimer's disease recapitulates development and contributes to reduce 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.-Y.6
  • 6
    • 0027429479 scopus 로고
    • Developmental changes in τ phosphorylation: Foetal τ is transiently phosphorylated in a manner similar to paired helical filament τ characteristic of Alzheimer's disease
    • Brion J. P., Smith C., Couck A. M., Gallo J. M., Anderton B. H. Developmental changes in τ phosphorylation: Foetal τ is transiently phosphorylated in a manner similar to paired helical filament τ characteristic of Alzheimer's disease. J. Neurochem. 61:1993;2071-2080.
    • (1993) J. Neurochem. , vol.61 , pp. 2071-2080
    • Brion, J.P.1    Smith, C.2    Couck, A.M.3    Gallo, J.M.4    Anderton, B.H.5
  • 7
    • 0028986916 scopus 로고
    • β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B. A. β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 14:1995;879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 8
    • 0025098891 scopus 로고
    • Inhibition of neuronal polarity by tau antisense oligonucleotides in primary cerebellar neurones
    • Caceres A., Kosik K. S. Inhibition of neuronal polarity by tau antisense oligonucleotides in primary cerebellar neurones. Nature. 343:1990;461-463.
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 9
    • 0029022960 scopus 로고
    • Impairment of axonal development and of synaptogenesis in hippocampal neurons of synapsin I-deficient mice
    • Chin L., Li L., Ferreira A., Kosik K. S., Greengard P. Impairment of axonal development and of synaptogenesis in hippocampal neurons of synapsin I-deficient mice. Proc. Natl. Acad. Sci. USA. 92:1995;9230-9234.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9230-9234
    • Chin, L.1    Li, L.2    Ferreira, A.3    Kosik, K.S.4    Greengard, P.5
  • 12
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti C. G., Sullivan C. A., Banker G. A. The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8:1988;1454-1468.
    • (1988) J. Neurosci. , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 13
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H., Kirschner M. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1992;1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.4
  • 15
    • 0028840004 scopus 로고
    • Inactivation of glycogen synthase kinase-3 by epidermal growth factor is mediated by mitogen-activated protein kinase/p90 ribosomal protein S6 kinase signaling pathway in NIH/3T3 cells
    • Eldar-Finkelman H., Seger R., Vandenheede J. R., Krebs E. G. Inactivation of glycogen synthase kinase-3 by epidermal growth factor is mediated by mitogen-activated protein kinase/p90 ribosomal protein S6 kinase signaling pathway in NIH/3T3 cells. J. Biol. Chem. 270:1995;987-990.
    • (1995) J. Biol. Chem. , vol.270 , pp. 987-990
    • Eldar-Finkelman, H.1    Seger, R.2    Vandenheede, J.R.3    Krebs, E.G.4
  • 16
    • 0024433060 scopus 로고
    • Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: Evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP-2 and tau
    • Ferreira A., Busciglio J., Caceres A. Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP-2 and tau. Dev. Brain Res. 49:1989;215-228.
    • (1989) Dev. Brain Res. , vol.49 , pp. 215-228
    • Ferreira, A.1    Busciglio, J.2    Caceres, A.3
  • 17
    • 0029046477 scopus 로고
    • Suppression of synapsin II inhibits the formation and maintenance of synapses in hippocampal culture
    • Ferreira A., Han H.-Q., Greengard P., Kosik K. S. Suppression of synapsin II inhibits the formation and maintenance of synapses in hippocampal culture. Proc. Natl. Acad. Sci. USA. 92:1995;9225-9229.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9225-9229
    • Ferreira, A.1    Han, H.-Q.2    Greengard, P.3    Kosik, K.S.4
  • 18
    • 0026001491 scopus 로고
    • The distribution of synapsin I and synaptophysin in hippocampal neurons in culture
    • Fletcher T. L., Cameron P., DeCamilli P., Banker G. The distribution of synapsin I and synaptophysin in hippocampal neurons in culture. J. Neurosci. 11:1991;1617-1626.
    • (1991) J. Neurosci. , vol.11 , pp. 1617-1626
    • Fletcher, T.L.1    Cameron, P.2    Decamilli, P.3    Banker, G.4
  • 19
    • 0029070173 scopus 로고
    • Differential effects of amyloid peptides β-(1-40) and β-(25-35) injections into the rat nucleus basalis
    • Giovanelli L., Casamenti F., Scali C., Bartolini L., Pepeu G. Differential effects of amyloid peptides β-(1-40) and β-(25-35) injections into the rat nucleus basalis. Neuroscience. 66:1995;781-792.
    • (1995) Neuroscience , vol.66 , pp. 781-792
    • Giovanelli, L.1    Casamenti, F.2    Scali, C.3    Bartolini, L.4    Pepeu, G.5
  • 20
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillatine M. G., Jakes R., Rutherford D., 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    Spillatine, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 21
    • 0026784416 scopus 로고
    • P42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A
    • Goedert M., Cohen E. S., Jakes R., Cohen P. p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A. FEBS Lett. 312:1992;95-99.
    • (1992) FEBS Lett. , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 23
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M., Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9:1990;4225-4230.
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 25
    • 0028179001 scopus 로고
    • Secreted beta-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation
    • Greenberg S. M., Koo E. H., Selkoe D. J., Qui W. Q., Kosik K. S. Secreted beta-amyloid precursor protein stimulates mitogen-activated protein kinase and enhances tau phosphorylation. Proc. Natl. Acad. Sci. USA. 91:1994;7104-7108.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7104-7108
    • Greenberg, S.M.1    Koo, E.H.2    Selkoe, D.J.3    Qui, W.Q.4    Kosik, K.S.5
  • 26
    • 0026487365 scopus 로고
    • Glycogen synthase kinase 3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal colocalization of the kinase
    • Hanger D. P., Hughes K., Woodgett J. R., Brion J. P., Anderton B. H. Glycogen synthase kinase 3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal colocalization of the kinase. Neurosci. Lett. 147:1992;58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 28
    • 3142628959 scopus 로고
    • A quantitative dot immunobinding assay for proteins using nitrocellulose membrane filters
    • Jan R., Schiebler W., Greengard P. A quantitative dot immunobinding assay for proteins using nitrocellulose membrane filters. Proc. Natl. Acad. Sci. USA. 81:1984;1684-1687.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1684-1687
    • Jan, R.1    Schiebler, W.2    Greengard, P.3
  • 30
    • 0027426029 scopus 로고
    • A cdc-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubules
    • Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahori K., Uchita T. A cdc-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubules. FEBS Lett. 335:1993;171-175.
    • (1993) FEBS Lett. , vol.335 , pp. 171-175
    • Kobayashi, S.1    Ishiguro, K.2    Omori, A.3    Takamatsu, M.4    Arioka, M.5    Imahori, K.6    Uchita, T.7
  • 31
    • 8044224425 scopus 로고
    • Experimental models of neurofibrillary disease
    • C. Marotta. Minneapolis: Minnesota Press
    • Kosik K. S., Selkoe D. J. Experimental models of neurofibrillary disease. Marotta C. Neurofilaments. 1983;Minnesota Press, Minneapolis.
    • (1983) Neurofilaments
    • Kosik, K.S.1    Selkoe, D.J.2
  • 32
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik K. S., Orecchio L., Binder L. I., Trojanowski J., Lee V., Lee G. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron. 1:1988;817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.2    Binder, L.I.3    Trojanowski, J.4    Lee, V.5    Lee, G.6
  • 33
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik K. S., Orecchio L., Bakalis S., Neve R. Developmentally regulated expression of specific tau sequences. Neuron. 2:1989;1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.2    Bakalis, S.3    Neve, R.4
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of the bacteriophage T4
    • Laemmli U. K. Cleavage of structural protein during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0026694067 scopus 로고
    • Implication of brain cdc2 and MAP kinases in the phosphorylation of tau proteins in Alzheimer's disease
    • Ledesma M. D., Correas L., Avila J., Diaz-Nido J. Implication of brain cdc2 and MAP kinases in the phosphorylation of tau proteins in Alzheimer's disease. FEBS Lett. 308:1992;218-224.
    • (1992) FEBS Lett. , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, L.2    Avila, J.3    Diaz-Nido, J.4
  • 36
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G., Cowan N., Kirschner M. The primary structure and heterogeneity of tau protein from mouse brain. Science. 239:1988;285-288.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 37
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and it is inhibited by Congo red
    • Lorenzo A., Yankner B. A. β-Amyloid neurotoxicity requires fibril formation and it is inhibited by Congo red. Proc. Natl. Acad. Sci. USA. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 40
    • 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. Y. 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.Y.7
  • 41
  • 42
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau, and chromosomal localization of the genes for tau and microtubule associated protein 2
    • Neve R. L., Haris P., Kosik K. S., Kurnit D. M., Donlon T. A. Identification of cDNA clones for the human microtubule-associated protein tau, and chromosomal localization of the genes for tau and microtubule associated protein 2. Mol. Brain Res. 1:1986;271-280.
    • (1986) Mol. Brain Res. , vol.1 , pp. 271-280
    • Neve, R.L.1    Haris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 43
    • 0027421625 scopus 로고
    • Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments
    • Paudel H. K., Lew J., Zenobia A., Wang J. H. Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments. J. Biol. Chem. 268:1993;23512-23518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23512-23518
    • Paudel, H.K.1    Lew, J.2    Zenobia, A.3    Wang, J.H.4
  • 44
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike C. J., Walencewicz-Wasserman A. J., Kosmoski, Cribbs D. H., Glabe C. G., Cotman C. W. Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity. J. Neurochem. 64:1995;253-265.
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 45
    • 0028879127 scopus 로고
    • Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells
    • Smith C. J., Anderton B. H., Davies D., Gallo J. M. Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells. FEBS Lett. 375:1995;243-248.
    • (1995) FEBS Lett. , vol.375 , pp. 243-248
    • Smith, C.J.1    Anderton, B.H.2    Davies, D.3    Gallo, J.M.4
  • 46
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • Sturgill T. W., Ray L. B., Erikson E., Maller J. L. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature. 334:1988;715-719.
    • (1988) Nature , vol.334 , pp. 715-719
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 47
    • 0028177965 scopus 로고
    • The α-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro
    • Sutherland C., Cohen P. The α-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro. FEBS Lett. 338:1994;37-42.
    • (1994) FEBS Lett. , vol.338 , pp. 37-42
    • Sutherland, C.1    Cohen, P.2
  • 48
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3β by phosphorylation: New kinase connections in insulin and growth factor signalling
    • Sutherland C., Leighton I. A., Cohen P. Inactivation of glycogen synthase kinase-3β by phosphorylation: New kinase connections in insulin and growth factor signalling. Biochem. J. 296:1993;15-19.
    • (1993) Biochem. J. , vol.296 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 50
    • 0022468128 scopus 로고
    • Clonal analysis of oligodendrocyte development in culture: Evidence for a developmental clock that counts cell divisions
    • Temple S., Raff M. C. Clonal analysis of oligodendrocyte development in culture: Evidence for a developmental clock that counts cell divisions. Cell. 44:1986;773-779.
    • (1986) Cell , vol.44 , pp. 773-779
    • Temple, S.1    Raff, M.C.2
  • 51
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelein T., Gordon J. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4354-4356.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4354-4356
    • Towbin, H.1    Staehelein, T.2    Gordon, J.3
  • 53
    • 0024990330 scopus 로고
    • Nerotrophic and neurotoxic effects of amyloid β-protein: Reversal by tachykinin neuropeptides
    • Yanker B. A., Duffy L. K., Kirschner D. A. Nerotrophic and neurotoxic effects of amyloid β-protein: Reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yanker, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 54
    • 0027930019 scopus 로고
    • Use of a synthetic peptide as a selective substrate for glycogen synthase kinase 3
    • Wang Q. M., Roach P., Fiol C. J. Use of a synthetic peptide as a selective substrate for glycogen synthase kinase 3. Anal. Biochem. 220:1994;397-402.
    • (1994) Anal. Biochem. , vol.220 , pp. 397-402
    • Wang, Q.M.1    Roach, P.2    Fiol, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.