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Volumn 117, Issue 2, 2003, Pages 145-151

Okadaic acid mediates tau phosphorylation via sustained activation of the L-voltage-sensitive calcium channel

Author keywords

Alzheimer's disease; Calcium; L voltage calcium channel; MAP kinase; Neurodegeneration; Okadaic acid; Phosphatase

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ANTIBODY; CALCIUM CHANNEL BLOCKING AGENT; CALCIUM CHANNEL L TYPE; CALCIUM ION; ENZYME INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; NIMODIPINE; OKADAIC ACID; PHF 1 ANTIBODY; PHOSPHATASE INHIBITOR; TAU PROTEIN; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL;

EID: 1642353487     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(03)00294-8     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 0027276779 scopus 로고
    • Contrasting effects of two tumour promoters, phorbol myristate acetate and okadaic acid, on T-cell responses and activation of p42 MAP-kinase/ERK-2
    • Amaral M.C., Casillas A.M., Nel A.E. Contrasting effects of two tumour promoters, phorbol myristate acetate and okadaic acid, on T-cell responses and activation of p42 MAP-kinase/ERK-2. Immunology. 79:1993;24-31.
    • (1993) Immunology , vol.79 , pp. 24-31
    • Amaral, M.C.1    Casillas, A.M.2    Nel, A.E.3
  • 2
    • 0032191966 scopus 로고
    • The protein phosphatase inhibitor okadaic acid induces heat shock protein expression and neurodegeneration in rat hippocampus in vivo
    • Arias C., Becerra-Garcia F., Arrieta I., Tapia R. The protein phosphatase inhibitor okadaic acid induces heat shock protein expression and neurodegeneration in rat hippocampus in vivo. Exp. Neurol. 53:1993;242-254.
    • (1993) Exp. Neurol. , vol.53 , pp. 242-254
    • Arias, C.1    Becerra-Garcia, F.2    Arrieta, I.3    Tapia, R.4
  • 3
    • 0023630392 scopus 로고
    • Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids
    • Baudier J., Cole R.D. Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J. Biol. Chem. 262:1987;17577-17583.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17577-17583
    • Baudier, J.1    Cole, R.D.2
  • 5
    • 0037373149 scopus 로고    scopus 로고
    • Growth cones contain a highly-dynamic population of neurofilament subunits
    • Chan W.K.-H., Yabe J.T., Pimenta A.F., Shea T.B. Growth cones contain a highly-dynamic population of neurofilament subunits. Cell Motil. Cytoskel. 54:2002;195-207.
    • (2002) Cell Motil. Cytoskel. , vol.54 , pp. 195-207
    • Chan, W.K.-H.1    Yabe, J.T.2    Pimenta, A.F.3    Shea, T.B.4
  • 6
    • 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
  • 7
    • 0027753055 scopus 로고
    • Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A
    • Drewes G., Mandelkow E.M., Baumann K., Goris J., Merlevede W., Mandelkow E. Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A. FEBS Lett. 336:1993;425-432.
    • (1993) FEBS Lett. , vol.336 , pp. 425-432
    • Drewes, G.1    Mandelkow, E.M.2    Baumann, K.3    Goris, J.4    Merlevede, W.5    Mandelkow, E.6
  • 9
    • 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
  • 10
    • 0033569760 scopus 로고    scopus 로고
    • β-Amyloid induces calcium influx and neurodegeneration by MAP kinase-mediated activation of the L voltage-sensitive calcium channel
    • Ekinci F.J., Malik K.M., Shea T.B. β-Amyloid induces calcium influx and neurodegeneration by MAP kinase-mediated activation of the L voltage-sensitive calcium channel. J. Biol. Chem. 274:1999;30322-30327.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30322-30327
    • Ekinci, F.J.1    Malik, K.M.2    Shea, T.B.3
  • 11
    • 0030879686 scopus 로고    scopus 로고
    • Selective phosphorylation of adult tau isoforms in mature hippocampal neurons exposed to fibrillar Abeta
    • Ferrier A., Lu Q., Orecchio L., Kosik K.S. Selective phosphorylation of adult tau isoforms in mature hippocampal neurons exposed to fibrillar Abeta. Mol. Cell. Neurosci. 9:1997;220-234.
    • (1997) Mol. Cell. Neurosci. , vol.9 , pp. 220-234
    • Ferrier, A.1    Lu, Q.2    Orecchio, L.3    Kosik, K.S.4
  • 12
    • 0034469810 scopus 로고    scopus 로고
    • New insights into genetic and molecular mechanisms of brain degeneration in tauopathies
    • Forman M.S., Lee V.M.-Y., Trojanowski J.Q. New insights into genetic and molecular mechanisms of brain degeneration in tauopathies. J. Chem. Anat. 20:2000;225-244.
    • (2000) J. Chem. Anat. , vol.20 , pp. 225-244
    • Forman, M.S.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 13
    • 0027738677 scopus 로고
    • Opposite effects of phosphatase inhibitors on L-type calcium and delayed rectifier currents in frog cardiac myocytes
    • Frace A.M., Hartzell H.C. Opposite effects of phosphatase inhibitors on L-type calcium and delayed rectifier currents in frog cardiac myocytes. J. Physiol. 472:1993;305-326.
    • (1993) J. Physiol. , vol.472 , pp. 305-326
    • Frace, A.M.1    Hartzell, H.C.2
  • 14
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • Gong C.X., Shaikh S., Wang J.Z., Zaidi T., Grundke-Iqbal I., Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 65:(2):1995;732-738.
    • (1995) J. Neurochem. , vol.65 , Issue.2 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 15
    • 0034088846 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease
    • Gong C.X., Lidsky T., Wegiel J., Zuck L., Grundke-Iqbal I., Iqbal K. Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease. J. Biol. Chem. 275:(8):2000;5535-5544.
    • (2000) J. Biol. Chem. , vol.275 , Issue.8 , pp. 5535-5544
    • Gong, C.X.1    Lidsky, T.2    Wegiel, J.3    Zuck, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 16
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I., Iqbal K., Tung Y.C., Quinlan M., Wisniewski H.M., Binder L.I. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA. 83:(13):1986;4913-4917.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.13 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3    Quinlan, M.4    Wisniewski, H.M.5    Binder, L.I.6
  • 17
    • 0028295386 scopus 로고
    • Inhibition of serine/threonine protein phosphatases promotes opening of voltage-activated L-type Ca2+ channels in insulin-secreting cells
    • Haby C., Larsson O., Islam M.S., Aunis D., Berggren P.O., Zwiller J. Inhibition of serine/threonine protein phosphatases promotes opening of voltage-activated L-type Ca2+ channels in insulin-secreting cells. Biochem. J. 298:1994;341-346.
    • (1994) Biochem. J. , vol.298 , pp. 341-346
    • Haby, C.1    Larsson, O.2    Islam, M.S.3    Aunis, D.4    Berggren, P.O.5    Zwiller, J.6
  • 18
    • 0033296842 scopus 로고    scopus 로고
    • PHF-tau from Alzheimer brain is rapidly dephosphorylated and degraded when injected into neurons in situ
    • Hall G.F. PHF-tau from Alzheimer brain is rapidly dephosphorylated and degraded when injected into neurons in situ. J. Alzheimer's Dis. 1:1999;379-386.
    • (1999) J. Alzheimer's Dis. , vol.1 , pp. 379-386
    • Hall, G.F.1
  • 19
    • 0033988977 scopus 로고    scopus 로고
    • Neuronal morphology, axonal integrity and axonal regeneration in situ are regulated by cytoskeletal phosphorylation in identified lamprey central neurons
    • Hall G.F., Yao J. Neuronal morphology, axonal integrity and axonal regeneration in situ are regulated by cytoskeletal phosphorylation in identified lamprey central neurons. Microsc. Res. Tech. 48:2000;32-46H.
    • (2000) Microsc. Res. Tech. , vol.48 , pp. 32-46H
    • Hall, G.F.1    Yao, J.2
  • 21
    • 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
  • 22
    • 0032850718 scopus 로고
    • The role of protein phosphatases in the regulation of mitogen and stress-activated protein kinases
    • Keyse S.M. The role of protein phosphatases in the regulation of mitogen and stress-activated protein kinases. Free Radic. Res. 31:1993;341-349.
    • (1993) Free Radic. Res. , vol.31 , pp. 341-349
    • Keyse, S.M.1
  • 23
    • 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
  • 24
    • 0029798880 scopus 로고    scopus 로고
    • Reduction of calcineurin enzymatic activity in Alzheimer's disease: Correlation with neuropathologic changes
    • Ladner C.J., Czech J., Maurice J., Lorens S.A., Lee J.M. Reduction of calcineurin enzymatic activity in Alzheimer's disease: correlation with neuropathologic changes. J. Neuropathol. Exp. Neurol. 55:1996;924-931.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 924-931
    • Ladner, C.J.1    Czech, J.2    Maurice, J.3    Lorens, S.A.4    Lee, J.M.5
  • 26
    • 0035155854 scopus 로고    scopus 로고
    • Selective changes of calcineurin (protein phosphatase 2B) activity in Alzheimer's disease cerebral cortex
    • Lian Q., Ladner C.J., Magnuson D., Lee J.M. Selective changes of calcineurin (protein phosphatase 2B) activity in Alzheimer's disease cerebral cortex. Exp. Neurol. 167:2001;158-165.
    • (2001) Exp. Neurol. , vol.167 , pp. 158-165
    • Lian, Q.1    Ladner, C.J.2    Magnuson, D.3    Lee, J.M.4
  • 28
    • 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
  • 29
    • 0037025379 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxynonenal facilitates opening of voltage-dependent Ca2+ channels in neurons by increasing protein tyrosine phosphorylation
    • Lu C., Chan S.L., Fu W., Mattson M.P. The lipid peroxidation product 4-hydroxynonenal facilitates opening of voltage-dependent Ca2+ channels in neurons by increasing protein tyrosine phosphorylation. J. Biol. Chem. 277:2002;24368-24375.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24368-24375
    • Lu, C.1    Chan, S.L.2    Fu, W.3    Mattson, M.P.4
  • 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
    • 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
  • 32
    • 0037066075 scopus 로고    scopus 로고
    • Calcineurin enhances L-type Ca(2+) channel activity in hippocampal neurons: Increased effect with age in culture
    • Norris C.M., Blalock E.M., Chen K.C., Porter N.M., Landfield P.W. Calcineurin enhances L-type Ca(2+) channel activity in hippocampal neurons: increased effect with age in culture. Neuroscience. 110:2002;213-225.
    • (2002) Neuroscience , vol.110 , pp. 213-225
    • Norris, C.M.1    Blalock, E.M.2    Chen, K.C.3    Porter, N.M.4    Landfield, P.W.5
  • 33
    • 0027514060 scopus 로고
    • Dual effect of phosphatase inhibitors on calcium channels in intestinal smooth muscle cells
    • Obara K., Yabu H. Dual effect of phosphatase inhibitors on calcium channels in intestinal smooth muscle cells. Am. J. Physiol. 264:1993;296-301.
    • (1993) Am. J. Physiol. , vol.264 , pp. 296-301
    • Obara, K.1    Yabu, H.2
  • 34
    • 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
  • 36
    • 0032579949 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activated by lipopolysaccharide and beta-amyloid in cultured rat microglia
    • Pyo H., Jou I., Jung S., Hong S., Joe E.H. Mitogen-activated protein kinases activated by lipopolysaccharide and beta-amyloid in cultured rat microglia. Neuroreport. 30:1998;871-874.
    • (1998) Neuroreport , vol.30 , pp. 871-874
    • Pyo, H.1    Jou, I.2    Jung, S.3    Hong, S.4    Joe, E.H.5
  • 37
    • 0028799807 scopus 로고
    • Hyperphosphorylation of the cytoskeletal protein Tau by the MAP-kinase PK40erk2: Regulation by prior phosphorylation with cAMP-dependent protein kinase a
    • Raghunandan R., Ingram V.M. Hyperphosphorylation of the cytoskeletal protein Tau by the MAP-kinase PK40erk2: regulation by prior phosphorylation with cAMP-dependent protein kinase A. Biochem. Biophys. Res. Commun. 215:1995;1056-1066.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 1056-1066
    • Raghunandan, R.1    Ingram, V.M.2
  • 39
    • 0027308266 scopus 로고
    • Detection of Alzheimer type pathological epitopes on Tau proteins of neuroblastoma cells after treatment with okadaic acid
    • Sautiere P.E., Caillet-Boudin M.L., Wattez A., Buee-Scherrer V., Delacourte A. Detection of Alzheimer type pathological epitopes on Tau proteins of neuroblastoma cells after treatment with okadaic acid. C. R. Acad. Sci. III. 316:1993;533-535.
    • (1993) C. R. Acad. Sci. III , vol.316 , pp. 533-535
    • Sautiere, P.E.1    Caillet-Boudin, M.L.2    Wattez, A.3    Buee-Scherrer, V.4    Delacourte, A.5
  • 40
    • 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
  • 41
    • 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. 22:1998;39-44.
    • (1998) Neurosci. Res. Commun. , vol.22 , pp. 39-44
    • Shea, T.B.1    Didier, M.2
  • 42
    • 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
  • 43
    • 0029569152 scopus 로고
    • Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: Focusing on phosphatases
    • Trojanowski J.Q., Lee V.M. Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases. FASEB J. 9:1995;1570-1576.
    • (1995) FASEB J. , vol.9 , pp. 1570-1576
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 44
    • 0031035954 scopus 로고    scopus 로고
    • Amyloid beta protein potentiates Ca2+ influx through L-type voltage-sensitive Ca2+ channels: A possible involvement of free radicals
    • Ueda K., Shinohara S., Yagami T., Asakura K., Kawasaki K. Amyloid beta protein potentiates Ca2+ influx through L-type voltage-sensitive Ca2+ channels: a possible involvement of free radicals. J. Neurochem. 68:1997;265-271.
    • (1997) J. Neurochem. , vol.68 , pp. 265-271
    • Ueda, K.1    Shinohara, S.2    Yagami, T.3    Asakura, K.4    Kawasaki, K.5
  • 47
    • 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., 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
  • 48
    • 0029017890 scopus 로고
    • Two distinct functional effects of protein phosphatase inhibitors on guinea-pig cardiac L-type Ca2+ channels
    • Wiechen K., Yue D.T., Herzig S. Two distinct functional effects of protein phosphatase inhibitors on guinea-pig cardiac L-type Ca2+ channels. J. Physiol. 484:1995;583-592.
    • (1995) J. Physiol. , vol.484 , pp. 583-592
    • Wiechen, K.1    Yue, D.T.2    Herzig, S.3


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