메뉴 건너뛰기




Volumn 850, Issue 1-2, 1999, Pages 207-216

Free PKC catalytic subunits (PKM) phosphorylate tau via a pathway distinct from that utilized by intact PKC

Author keywords

Alzheimer's disease; Calpain; MAP kinase; Paired helical filaments; Protein kinase C; Protein kinase M phosphorylation; Signal transduction; Tau

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CALCIMYCIN; DIACYLGLYCEROL; MITOGEN ACTIVATED PROTEIN KINASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; TAU PROTEIN;

EID: 0032733910     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)02146-0     Document Type: Article
Times cited : (23)

References (79)
  • 1
    • 0030985157 scopus 로고    scopus 로고
    • Acute rise in the concentration of free cytoplasmic calcium leads to dephosphorylation of the microtubule-associated protein tau
    • Adamec E., Mercken M., Beermann M.L., Didier M., Nixon R.A. Acute rise in the concentration of free cytoplasmic calcium leads to dephosphorylation of the microtubule-associated protein tau. Brain Res. 757:1997;93-101.
    • (1997) Brain Res. , vol.757 , pp. 93-101
    • Adamec, E.1    Mercken, M.2    Beermann, M.L.3    Didier, M.4    Nixon, R.A.5
  • 2
    • 0027764538 scopus 로고
    • Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: Possible role of protein kinase M
    • Al Z., Cohen C.M. Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: possible role of protein kinase M. Biochem. J. 296:1993;675-683.
    • (1993) Biochem. J. , vol.296 , pp. 675-683
    • Al, Z.1    Cohen, C.M.2
  • 4
    • 0001454672 scopus 로고    scopus 로고
    • The calpain hypothesis of neurodegeneration: Evidence for a common cytotoxic pathway
    • Bartus R.T. The calpain hypothesis of neurodegeneration: evidence for a common cytotoxic pathway. Neuroscientist. 3:1997;314-327.
    • (1997) Neuroscientist , vol.3 , pp. 314-327
    • Bartus, R.T.1
  • 5
    • 0030793593 scopus 로고    scopus 로고
    • Phosphorylation events mediated by protein kinase Cα and ε participate in the regulation of tau steady-state levels and generation of certain "alzheimer-like" phospho-epitopes
    • Boyce J.J., Shea T.B. Phosphorylation events mediated by protein kinase Cα and ε participate in the regulation of tau steady-state levels and generation of certain "Alzheimer-like" phospho-epitopes. Int. J. Dev. Neurosci. 15:1997;295-307.
    • (1997) Int. J. Dev. Neurosci. , vol.15 , pp. 295-307
    • Boyce, J.J.1    Shea, T.B.2
  • 6
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at ser-396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Brambett 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 reduced microtubule binding. Neuron. 10:1993;1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Brambett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 7
    • 0032540311 scopus 로고    scopus 로고
    • Developmental regulation and PKC dependence of Alzheimer's-type tau phosphorylations in cultured fetal rat hippocampal neurons
    • Combs C.K., Coleman P.D., O'Banion M.K. Developmental regulation and PKC dependence of Alzheimer's-type tau phosphorylations in cultured fetal rat hippocampal neurons. Dev. Brain Res. 107:1998;143-158.
    • (1998) Dev. Brain Res. , vol.107 , pp. 143-158
    • Combs, C.K.1    Coleman, P.D.2    O'Banion, M.K.3
  • 8
    • 0030050166 scopus 로고    scopus 로고
    • Phorbol ester enhances phosphorylated tau protein immunoreactivity in neuronal cultures
    • (1996 Jan. 26)
    • Couratier P., Lesort M., Condamines O., Mourton-Gilles C., Delacourte A., Hugon J. Phorbol ester enhances phosphorylated tau protein immunoreactivity in neuronal cultures. Neurosci Lett. 203(3):1996;155-158. (1996 Jan. 26).
    • (1996) Neurosci Lett. , vol.203 , Issue.3 , pp. 155-158
    • Couratier, P.1    Lesort, M.2    Condamines, O.3    Mourton-Gilles, C.4    Delacourte, A.5    Hugon, J.6
  • 9
    • 0028973143 scopus 로고
    • Hyperphosphorylation of tau and filopodial retraction following microinjection of protein kinase C catalytic subunits
    • Cressman C.M., Shea T.B. Hyperphosphorylation of tau and filopodial retraction following microinjection of protein kinase C catalytic subunits. J. Neurosci. Res. 42:1995;648-656.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 648-656
    • Cressman, C.M.1    Shea, T.B.2
  • 10
    • 0029097539 scopus 로고
    • Alteration in tau antigenicity and electrophoretic migration by PKCa under cell-free conditions
    • Cressman C.M., Mercken M.M., Shea T.B. Alteration in tau antigenicity and electrophoretic migration by PKCa under cell-free conditions. Neurosci. Res. Commun. 17:1995;61-64.
    • (1995) Neurosci. Res. Commun. , vol.17 , pp. 61-64
    • Cressman, C.M.1    Mercken, M.M.2    Shea, T.B.3
  • 11
    • 0029049028 scopus 로고
    • Proteolysis of protein kinase C: MM, μm-requiring calpains have different abilities to generate, and degrade, the free catalytic subunit, protein kinase M
    • Cressman C.M., Mohan P.S., Nixon R.A., Shea T.B. Proteolysis of protein kinase C: mM, μM-requiring calpains have different abilities to generate, and degrade, the free catalytic subunit, protein kinase M. FEBS Lett. 367:1995;223-227.
    • (1995) FEBS Lett. , vol.367 , pp. 223-227
    • Cressman, C.M.1    Mohan, P.S.2    Nixon, R.A.3    Shea, T.B.4
  • 12
    • 0031576378 scopus 로고    scopus 로고
    • Selective activation by bryostatin demonstrates unique roles for PKCe in neurite extension and tau phosphorylation
    • Ekinci F.J., Shea T.B. Selective activation by bryostatin demonstrates unique roles for PKCe in neurite extension and tau phosphorylation. Int. J. Dev. Neurosci. 15:1997;867-874.
    • (1997) Int. J. Dev. Neurosci. , vol.15 , pp. 867-874
    • Ekinci, F.J.1    Shea, T.B.2
  • 13
    • 0032972004 scopus 로고    scopus 로고
    • Hyperactivation of mitogen-activated protein kinase increases phospho-tau immunoreactivity within human neuroblastoma: Additive and synergistic influence of alteration of additional kinase activities
    • Ekinci F.J., Shea T.B. Hyperactivation of mitogen-activated protein kinase increases phospho-tau immunoreactivity within human neuroblastoma: Additive and synergistic influence of alteration of additional kinase activities. Cell. Mol. Neurobiol. 19:1999;249-260.
    • (1999) Cell. Mol. Neurobiol. , vol.19 , pp. 249-260
    • Ekinci, F.J.1    Shea, T.B.2
  • 14
    • 0025285212 scopus 로고
    • A specific inhibitor of protein kinase C induces differentiation of neuroblastoma cells
    • Felipo V., Minana M.-D., Grisola S. A specific inhibitor of protein kinase C induces differentiation of neuroblastoma cells. J. Biol. Chem. 265:1990;9599-9601.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9599-9601
    • Felipo, V.1    Minana, M.-D.2    Grisola, S.3
  • 15
    • 0029072567 scopus 로고
    • Modulation of the phosphorylation state of tau in situ: The roles of calcium and cyclic AMP
    • Fleming L.M., Johnson G.V. Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP. Biochem. J. 309:1995;41-47.
    • (1995) Biochem. J. , vol.309 , pp. 41-47
    • Fleming, L.M.1    Johnson, G.V.2
  • 16
    • 0029564859 scopus 로고
    • Constitutively active MAP kinase kinase (MEK1) stimulates SAP kinase and c-Jun transcriptional activity in U937 human leukemic cells
    • Franklin, Kraft A.S. Constitutively active MAP kinase kinase (MEK1) stimulates SAP kinase and c-Jun transcriptional activity in U937 human leukemic cells. Oncogene. 11:1995;2365-2374.
    • (1995) Oncogene , vol.11 , pp. 2365-2374
    • Franklin1    Kraft, A.S.2
  • 19
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases
    • Goedert M., Hasegawa M., Jakes R., Lawler S., Cuenda A., Cohen P. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett. 409:1997;57-62.
    • (1997) FEBS Lett. , vol.409 , pp. 57-62
    • Goedert, M.1    Hasegawa, M.2    Jakes, R.3    Lawler, S.4    Cuenda, A.5    Cohen, P.6
  • 20
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localization 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 localization 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
  • 21
    • 0025218078 scopus 로고
    • Protein kinase C during differentiation of human promyelocytic leukemia cell line, HL-60
    • Hashimoto K., Kishimoto A., Aihara H., Yasuda I., Mikawa K., Nishizuka Y. Protein kinase C during differentiation of human promyelocytic leukemia cell line, HL-60. FEBS Lett. 263:1990;31-34.
    • (1990) FEBS Lett. , vol.263 , pp. 31-34
    • Hashimoto, K.1    Kishimoto, A.2    Aihara, H.3    Yasuda, I.4    Mikawa, K.5    Nishizuka, Y.6
  • 22
    • 0024440305 scopus 로고
    • Protein kinase C activation and down-regulation in relation to phorbol ester-induced differentiation of SH-SY-5Y human neuroblastoma
    • Heikkila J.E., Akerlind G., Akerman K.E.O. Protein kinase C activation and down-regulation in relation to phorbol ester-induced differentiation of SH-SY-5Y human neuroblastoma. J. Cell. Physiol. 140:1991;593-600.
    • (1991) J. Cell. Physiol. , vol.140 , pp. 593-600
    • Heikkila, J.E.1    Akerlind, G.2    Akerman, K.E.O.3
  • 23
    • 0031018774 scopus 로고    scopus 로고
    • Okadaic acid induces hyperphosphorylation of tau independently of mitogen-activated protein kinase activation
    • Ho D.T., Shayan H., Murphy T.H. Okadaic acid induces hyperphosphorylation of tau independently of mitogen-activated protein kinase activation. J. Neurochem. 68:1997;106-111.
    • (1997) J. Neurochem. , vol.68 , pp. 106-111
    • Ho, D.T.1    Shayan, H.2    Murphy, T.H.3
  • 24
    • 0030748390 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons
    • Hong M., Lee V.M.-Y. 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.-Y.2
  • 25
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • Hong M., Chen D.C., Klein P.S., Lee V.M. Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J. Biol. Chem. 272:1997;25326-25332.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25326-25332
    • Hong, M.1    Chen, D.C.2    Klein, P.S.3    Lee, V.M.4
  • 26
    • 0017716047 scopus 로고
    • Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues: II. Proenzyme and its activation by calcium-dependent protease from rat brain
    • Inoue M., Kishimoto A., Takai Y., Nishizuka Y. Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues: II. Proenzyme and its activation by calcium-dependent protease from rat brain. J. Biol. Chem. 252:1977;7610-7616.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7610-7616
    • Inoue, M.1    Kishimoto, A.2    Takai, Y.3    Nishizuka, Y.4
  • 27
    • 0032951956 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of recombinant tau by the paired-helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase
    • Jicha G.A., O'Donnell A., Weaver C., Angeletti R., Davies P. Hierarchical phosphorylation of recombinant tau by the paired-helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase. J. Neurochem. 72:1999;214-224.
    • (1999) J. Neurochem. , vol.72 , pp. 214-224
    • Jicha, G.A.1    O'Donnell, A.2    Weaver, C.3    Angeletti, R.4    Davies, P.5
  • 28
    • 0021111512 scopus 로고
    • Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease
    • Kishimoto A., Kajikawa N., Shiota M., Nishizuka Y. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J. Biol. Chem. 258:1983;1156-1164.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1156-1164
    • Kishimoto, A.1    Kajikawa, N.2    Shiota, M.3    Nishizuka, Y.4
  • 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 kinase associated with microtubules
    • Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahora K., Uchida T. A cdc-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed 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    Imahora, K.6    Uchida, T.7
  • 31
    • 0025110182 scopus 로고
    • β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage
    • Koh J.-Y., Yang L.L., Cotman C.W. β-amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage. Brain Res. 533:1990;315-320.
    • (1990) Brain Res. , vol.533 , pp. 315-320
    • Koh, J.-Y.1    Yang, L.L.2    Cotman, C.W.3
  • 32
    • 0029608729 scopus 로고
    • Phospholipids inhibit proteolysis of protein kinase C alpha by mM calcium-requiring calpain
    • Lang D., Beermann M.L., Hauser G., Cressman C.M., Shea T.B. Phospholipids inhibit proteolysis of protein kinase C alpha by mM calcium-requiring calpain. Neurochem. Res. 20:1995;1361-1364.
    • (1995) Neurochem. Res. , vol.20 , pp. 1361-1364
    • Lang, D.1    Beermann, M.L.2    Hauser, G.3    Cressman, C.M.4    Shea, T.B.5
  • 33
    • 0029115567 scopus 로고
    • A role for amplified protein kinase C activity in the pathogenesis of amyotrophic lateral sclerosis
    • Lanius R.A., Paddon H.B., Mezei M., Wagey R., Krieger C., Pelech S.L., Shaw C.A. A role for amplified protein kinase C activity in the pathogenesis of amyotrophic lateral sclerosis. J. Neurochem. 65:1995;927-930.
    • (1995) J. Neurochem. , vol.65 , pp. 927-930
    • Lanius, R.A.1    Paddon, H.B.2    Mezei, M.3    Wagey, R.4    Krieger, C.5    Pelech, S.L.6    Shaw, C.A.7
  • 35
    • 0026509489 scopus 로고
    • Distinct mechanisms of differentiation of SH-SY-5Y neuroblastoma cells by protein kinase C activators and inhibitors
    • Leli U., Cataldo A.M., Shea T.B., Nixon R.A., Hauser G. Distinct mechanisms of differentiation of SH-SY-5Y neuroblastoma cells by protein kinase C activators and inhibitors. J. Neurochem. 58:1992;1191-1198.
    • (1992) J. Neurochem. , vol.58 , pp. 1191-1198
    • Leli, U.1    Cataldo, A.M.2    Shea, T.B.3    Nixon, R.A.4    Hauser, G.5
  • 36
    • 0026531691 scopus 로고
    • Intracellular delivery of protein kinase C-α Or -ε isoform-specific antibodies promotes acquisition of a morphologically differentiated phenotype in neuroblastoma cells
    • Leli U., Parker P.J., Shea T.B. Intracellular delivery of protein kinase C-α or -ε isoform-specific antibodies promotes acquisition of a morphologically differentiated phenotype in neuroblastoma cells. FEBS Lett. 297:1992;91-94.
    • (1992) FEBS Lett. , vol.297 , pp. 91-94
    • Leli, U.1    Parker, P.J.2    Shea, T.B.3
  • 38
    • 0027335781 scopus 로고
    • P44mpk MAP kinase induces Alzheimer type alterations in tau function and in primary hippocampal neurons
    • Lu Q., Soria J.P., Wood J.G. p44mpk MAP kinase induces Alzheimer type alterations in tau function and in primary hippocampal neurons. J. Neurosci. Res. 35:1993;439-444.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 439-444
    • Lu, Q.1    Soria, J.P.2    Wood, J.G.3
  • 40
    • 0025811402 scopus 로고
    • Evidence for the involvement of protein kinase C in neurodegenerative changes in cultured human cortical neurons
    • Mattson M.P. Evidence for the involvement of protein kinase C in neurodegenerative changes in cultured human cortical neurons. Exp. Neurol. 16:1991;95-103.
    • (1991) Exp. Neurol. , vol.16 , pp. 95-103
    • Mattson, M.P.1
  • 42
    • 0024446059 scopus 로고
    • Inhibition of protein kinase C induces differentiation of neuroblastoma cells
    • Minana M.-D., Felipo V., Grisolia S. Inhibition of protein kinase C induces differentiation of neuroblastoma cells. FEBS Lett. 87:1989;184-186.
    • (1989) FEBS Lett. , vol.87 , pp. 184-186
    • Minana, M.-D.1    Felipo, V.2    Grisolia, S.3
  • 43
    • 0031567583 scopus 로고
    • Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons
    • Munoz-Montano J.R., Moreno F.J., Avila J., Diaz-Nido J. Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons. FEBS Lett. 411:1995;183-188.
    • (1995) FEBS Lett. , vol.411 , pp. 183-188
    • Munoz-Montano, J.R.1    Moreno, F.J.2    Avila, J.3    Diaz-Nido, J.4
  • 44
    • 0023117172 scopus 로고
    • Proteolytic activation of protein kinase C: A physiological reaction?
    • Murray A.W., Fournier A., Hardy S.J. Proteolytic activation of protein kinase C: a physiological reaction? TIBS. 12:1987;53-54.
    • (1987) TIBS , vol.12 , pp. 53-54
    • Murray, A.W.1    Fournier, A.2    Hardy, S.J.3
  • 46
    • 0028129138 scopus 로고
    • Compromised mitochondrial function results in dephosphorylation of tau through a calcium-dependent process in rat brain cerebral cortical slices
    • Norman S.G., Johnson G.V. Compromised mitochondrial function results in dephosphorylation of tau through a calcium-dependent process in rat brain cerebral cortical slices. Neurochem. Res. 19:1994;1151-1158.
    • (1994) Neurochem. Res. , vol.19 , pp. 1151-1158
    • Norman, S.G.1    Johnson, G.V.2
  • 47
    • 0025828072 scopus 로고
    • Morphology of neurites from N18TG2 cell induced by protein kinase inhibitor H-7 and by cAMP
    • Ono K., Katayama N., Yamagata Y., Tokunaga A., Tsuda M. Morphology of neurites from N18TG2 cell induced by protein kinase inhibitor H-7 and by cAMP. Brain Res. Bull. 26:1991;605-612.
    • (1991) Brain Res. Bull. , vol.26 , pp. 605-612
    • Ono, K.1    Katayama, N.2    Yamagata, Y.3    Tokunaga, A.4    Tsuda, M.5
  • 48
    • 0027471767 scopus 로고
    • Neurite outgrowth from N18TG2 neuroblastoma induced by H-7, a protein kinase inhibitor, in the presence of colchicine
    • Ono K., Tokunaga A., Tsuda M. Neurite outgrowth from N18TG2 neuroblastoma induced by H-7, a protein kinase inhibitor, in the presence of colchicine. Brain Res. Bull. 31:1993;209-215.
    • (1993) Brain Res. Bull. , vol.31 , pp. 209-215
    • Ono, K.1    Tokunaga, A.2    Tsuda, M.3
  • 49
    • 0029034774 scopus 로고
    • Inhibition of MAP kinase kinase blocks the differentiation of PC-12 cells induced by nerve growth factor
    • Pang L., Sawada T., Decker S.J., Saltiel A.R. Inhibition of MAP kinase kinase blocks the differentiation of PC-12 cells induced by nerve growth factor. J. Biol. Chem. 270:1995;13585-13588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13585-13588
    • Pang, L.1    Sawada, T.2    Decker, S.J.3    Saltiel, A.R.4
  • 50
    • 0024995709 scopus 로고
    • The specific inhibitor of protein kinase C, 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7), induces morphological change and cell differentiaton of human neuroal crest-derived lineages
    • Parodi M.T., Varesio L., Tonini G.P. The specific inhibitor of protein kinase C, 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7), induces morphological change and cell differentiaton of human neuroal crest-derived lineages. FEBS Lett. 269:1990;4-6.
    • (1990) FEBS Lett. , vol.269 , pp. 4-6
    • Parodi, M.T.1    Varesio, L.2    Tonini, G.P.3
  • 51
    • 0024384137 scopus 로고
    • Activation of neutrophil calpain following its translocation to the plasma membrane induced by phorbol ester or fMet-Leu-Phe
    • Pontremoli S., Melloni E., Salamino F., Patrone M., Michetti M., Horecker B.L. Activation of neutrophil calpain following its translocation to the plasma membrane induced by phorbol ester or fMet-Leu-Phe. Biochem. Biophys. Res. Commun. 160:1989;737-743.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 737-743
    • Pontremoli, S.1    Melloni, E.2    Salamino, F.3    Patrone, M.4    Michetti, M.5    Horecker, B.L.6
  • 53
    • 0031464106 scopus 로고    scopus 로고
    • AD-like tau phosphorylation in human neuroblastoma cells following PKC hyperactivation is mediated by MAP kinase
    • Pundreddy S., Shea T.B. AD-like tau phosphorylation in human neuroblastoma cells following PKC hyperactivation is mediated by MAP kinase. Neurosci. Res. Commun. 21:1997;173-177.
    • (1997) Neurosci. Res. Commun. , vol.21 , pp. 173-177
    • Pundreddy, S.1    Shea, T.B.2
  • 54
    • 0030943263 scopus 로고    scopus 로고
    • Stress-activated protein kinase/c-jun N-terminal kinase phosphorylates tau protein
    • Reynolds C.H., Utton M., Gibb G.M., Yates A., Anderton B.H. Stress-activated protein kinase/c-jun N-terminal kinase phosphorylates tau protein. J. Neurochem. 68:1997;1736-1744.
    • (1997) J. Neurochem. , vol.68 , pp. 1736-1744
    • Reynolds, C.H.1    Utton, M.2    Gibb, G.M.3    Yates, A.4    Anderton, B.H.5
  • 56
    • 0028865376 scopus 로고
    • In situ dephosphorylation of tau by protein phosphatase 2A, 2B in fetal rat primary cultured neurons
    • Saito T., Ishiguro K., Uchida T., Miyamoto E., Kishimoto T., Hisanaga S. In situ dephosphorylation of tau by protein phosphatase 2A, 2B in fetal rat primary cultured neurons. FEBS Lett. 376:1995;238-242.
    • (1995) FEBS Lett. , vol.376 , pp. 238-242
    • Saito, T.1    Ishiguro, K.2    Uchida, T.3    Miyamoto, E.4    Kishimoto, T.5    Hisanaga, S.6
  • 57
    • 0002090729 scopus 로고
    • Detection of Alzheimer-type tau proteins in okadaic acid-treated SKNSH-SY-5Y neuroblastoma cells
    • Sautiére P.-E., Caillet-Boudin M.-L., Wattez A., Delacourte A. Detection of Alzheimer-type tau proteins in okadaic acid-treated SKNSH-SY-5Y neuroblastoma cells. Neurodegeneration. 3:1994;53-60.
    • (1994) Neurodegeneration , vol.3 , pp. 53-60
    • Sautiére, P.-E.1    Caillet-Boudin, M.-L.2    Wattez, A.3    Delacourte, A.4
  • 58
    • 0031052339 scopus 로고    scopus 로고
    • Potentiation of GSK-3β-catalyzed Alzheimer-like phosphorylation of human tau by cdk5
    • Sengupta A., Wu Q., Grundke-Iqbal I., Iqbal K., Singh T.J. Potentiation of GSK-3β-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Cell. Biochem. 167:1997;99-105.
    • (1997) Mol. Cell. Biochem. , vol.167 , pp. 99-105
    • Sengupta, A.1    Wu, Q.2    Grundke-Iqbal, I.3    Iqbal, K.4    Singh, T.J.5
  • 59
    • 0025972182 scopus 로고
    • Stauroporine-induced morphological differentiation of human neuroblastoma cells
    • Shea T.B., Beermann M.L. Stauroporine-induced morphological differentiation of human neuroblastoma cells. Cell. Biol. Int. Rep. 15:1991;161-168.
    • (1991) Cell. Biol. Int. Rep. , vol.15 , pp. 161-168
    • Shea, T.B.1    Beermann, M.L.2
  • 60
    • 0026488116 scopus 로고
    • Opposing influences of protein kinase activities on neurite outgrowth in human neuroblastoma cells: Initiation by kinase A, restriction by kinase C
    • Shea T.B., Beermann M.L., Leli U., Nixon R.A. Opposing influences of protein kinase activities on neurite outgrowth in human neuroblastoma cells: initiation by kinase A, restriction by kinase C. J. Neurosci. Res. 33:1992;398-407.
    • (1992) J. Neurosci. Res. , vol.33 , pp. 398-407
    • Shea, T.B.1    Beermann, M.L.2    Leli, U.3    Nixon, R.A.4
  • 61
    • 0027966112 scopus 로고
    • Degradation of protein kinase C alpha and its free catalytic subunit, protein kinase M, in intact human neuroblastoma cells and under cell-free conditions. Evidence that PKM is degraded by mM calpain-mediated proteolysis at a faster rate than PKC
    • Shea T.B., Beermann M.L., Griffin W.R., Leli U. Degradation of protein kinase C alpha and its free catalytic subunit, protein kinase M, in intact human neuroblastoma cells and under cell-free conditions. Evidence that PKM is degraded by mM calpain-mediated proteolysis at a faster rate than PKC. FEBS Lett. 350:1994;223-229.
    • (1994) FEBS Lett. , vol.350 , pp. 223-229
    • Shea, T.B.1    Beermann, M.L.2    Griffin, W.R.3    Leli, U.4
  • 62
    • 0029159809 scopus 로고
    • Enhancement of neurite outgrowth following calpain inhibition is mediated by protein kinase C
    • Shea T.B., Beermann M.L., Spencer M.A., Nixon R.A. Enhancement of neurite outgrowth following calpain inhibition is mediated by protein kinase C. J. Neurochem. 65:1995;517-527.
    • (1995) J. Neurochem. , vol.65 , pp. 517-527
    • Shea, T.B.1    Beermann, M.L.2    Spencer, M.A.3    Nixon, R.A.4
  • 63
    • 0029081735 scopus 로고
    • Calcium influx recruits an additional class of kinases to hyperphosphorylate tau
    • Shea T.B., Klinger E.P., Cressman C.M. Calcium influx recruits an additional class of kinases to hyperphosphorylate tau. Neuroreport. 6:1995;1437-1440.
    • (1995) Neuroreport , vol.6 , pp. 1437-1440
    • Shea, T.B.1    Klinger, E.P.2    Cressman, C.M.3
  • 65
    • 0030046767 scopus 로고    scopus 로고
    • Phosphatase inhibition in human neuroblastoma cells alters tau antigenicity and renders it incompetent to associate with exogenous microtubules
    • Shea T.B., Fischer I. Phosphatase inhibition in human neuroblastoma cells alters tau antigenicity and renders it incompetent to associate with exogenous microtubules. FEBS Lett. 380:1996;63-67.
    • (1996) FEBS Lett. , vol.380 , pp. 63-67
    • Shea, T.B.1    Fischer, I.2
  • 66
    • 0029874834 scopus 로고    scopus 로고
    • Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: Involvement of calpain-mediated hydrolysis of protein kinase C
    • Shea T.B., Spencer M.J., Beermann M.L., Cressman C.M., Nixon R.A. Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C. J. Neurochem. 66:1996;1539-1549.
    • (1996) J. Neurochem. , vol.66 , pp. 1539-1549
    • Shea, T.B.1    Spencer, M.J.2    Beermann, M.L.3    Cressman, C.M.4    Nixon, R.A.5
  • 67
    • 0030986545 scopus 로고    scopus 로고
    • β-amyloid and ionophore-mediated calcium influx evoke neurodegeneration by distinct intracellular pathways: Differential involvement of the calpain/protein kinase C system
    • Shea T.B., Parabhakar S., Ekinci F.J. β-amyloid and ionophore-mediated calcium influx evoke neurodegeneration by distinct intracellular pathways: differential involvement of the calpain/protein kinase C system. J. Neurosci. Res. 49:1997;759-768.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 759-768
    • Shea, T.B.1    Parabhakar, S.2    Ekinci, F.J.3
  • 68
    • 0031887999 scopus 로고    scopus 로고
    • Biphasic effects of phosphatase inhibition on accumulation of tau phospho-isoforms in cultured cerebellar neurons
    • Shea T.B., Didier M. Biphasic effects of phosphatase inhibition on accumulation of tau phospho-isoforms in cultured cerebellar neurons. Neurosci. Res. Commun. 22:1997;39-44.
    • (1997) Neurosci. Res. Commun. , vol.22 , pp. 39-44
    • Shea, T.B.1    Didier, M.2
  • 69
    • 0033294073 scopus 로고    scopus 로고
    • Biphasic influence of calcium influx on tau phosphorylation: Involvement of calcium-dependent phosphatases and kinases
    • in press
    • T.B. Shea, F.J. Ekinci, Biphasic influence of calcium influx on tau phosphorylation: involvement of calcium-dependent phosphatases and kinases. J Alzheimer's disease, 1999, in press.
    • (1999) J Alzheimer's Disease
    • Shea, T.B.1    Ekinci, F.J.2
  • 70
    • 0033048702 scopus 로고    scopus 로고
    • The order of exposure of tau to signal transduction kinases alters the generation of "aD-like" phospho-epitopes
    • Shea T.B., Cressman C.M. The order of exposure of tau to signal transduction kinases alters the generation of "AD-like" phospho-epitopes. Cell. Mol. Neurobiol. 19:1999;224-235.
    • (1999) Cell. Mol. Neurobiol. , vol.19 , pp. 224-235
    • Shea, T.B.1    Cressman, C.M.2
  • 71
    • 0028897322 scopus 로고
    • Modulation of GSK-3 catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases
    • Singh T.J., Zaidi T., Grundke-Iqbal I., Iqbal K. Modulation of GSK-3 catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS. 358:1994;4-8.
    • (1994) FEBS , vol.358 , pp. 4-8
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 72
    • 0028967378 scopus 로고
    • Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline dependent kinases and GSK-3
    • Singh T.J., Haque N., Grundke-Iqbal I., Iqbal K. Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline dependent kinases and GSK-3. FEBS Lett. 358:1994;267-272.
    • (1994) FEBS Lett. , vol.358 , pp. 267-272
    • Singh, T.J.1    Haque, N.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 73
    • 0028040942 scopus 로고
    • Protein kinase C isozyme distribution and down-regulation in relation to insulin-stimulated c-fos induction
    • Stumpo D.J., Haupt D.M., Blackshear P.J. Protein kinase C isozyme distribution and down-regulation in relation to insulin-stimulated c-fos induction. J. Biol. Chem. 269:1994;21184-21190.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21184-21190
    • Stumpo, D.J.1    Haupt, D.M.2    Blackshear, P.J.3
  • 75
    • 0027479150 scopus 로고
    • Altered tau and neurofilament proteins in neurodegenative diseases: Diagnostic implications for Alzheimer's disease and Lewy body dementias
    • Trojanowski J.Q., Schmidt M.L., Shin R.-W., Bramblett G.T., Rao D., Lee V.M.-Y., Altered tau and neurofilament proteins in neurodegenative diseases: diagnostic implications for Alzheimer's disease and Lewy body dementias. Brain Pathol. (1993a) 45-54.
    • (1993) Brain Pathol. , pp. 45-54
    • Trojanowski, J.Q.1    Schmidt, M.L.2    Shin, R.-W.3    Bramblett, G.T.4    Rao, D.5    Lee, V.M.-Y.6
  • 76
    • 0027135874 scopus 로고
    • PHF tau (A68): From pathological marker to potential mediator of neuronal dysfunction and degeneration in Alzheimer's disease
    • Trojanowski J.Q., Schmidt M.L., Shin R.-W., Bramblett G.T., Goedert M., Lee V.M.-Y. PHF tau (A68): from pathological marker to potential mediator of neuronal dysfunction and degeneration in Alzheimer's disease. Clin. Neurosci. 1:1993;184-191.
    • (1993) Clin. Neurosci. , vol.1 , pp. 184-191
    • Trojanowski, J.Q.1    Schmidt, M.L.2    Shin, R.-W.3    Bramblett, G.T.4    Goedert, M.5    Lee, V.M.-Y.6
  • 77
    • 0024455554 scopus 로고
    • Neurite outgrowth from mouse neuroblastoma and cerebellar cells induced by the protein kinase inhibitor H-7
    • Tsuda M., Ono K., Katayama N., Yamagata Y., Kikuchi K., Tsuchiya T. Neurite outgrowth from mouse neuroblastoma and cerebellar cells induced by the protein kinase inhibitor H-7. Neurosci. Lett. 105:1989;241-245.
    • (1989) Neurosci. Lett. , vol.105 , pp. 241-245
    • Tsuda, M.1    Ono, K.2    Katayama, N.3    Yamagata, Y.4    Kikuchi, K.5    Tsuchiya, T.6
  • 79
    • 0022539722 scopus 로고
    • Calcium-activated neutral proteinase of human brain: Subunit structure and enzymatic properties of multiple molecular forms
    • Vitto A., Nixon R.A. Calcium-activated neutral proteinase of human brain: subunit structure and enzymatic properties of multiple molecular forms. J. Neurochem. 47:1986;1039-1051.
    • (1986) J. Neurochem. , vol.47 , pp. 1039-1051
    • Vitto, A.1    Nixon, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.