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Volumn 68, Issue 1, 1997, Pages 106-111

Okadaic acid induces hyperphosphorylation of τ independently of mitogen-activated protein kinase activation

Author keywords

Alzheimer's disease; Microtubule; Mitogen activated protein kinase; Okadaic acid; protein

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; OKADAIC ACID; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 0031018774     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68010106.x     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi D. R., Cuenda A., Cohen P., Dudley D. T., and Saltiel A. R. (1995) PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270, 27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 2
    • 0027162369 scopus 로고
    • Okadaic acid induces early changes in microtubule-associated protein 2 and τ phosphorylation prior to neurodegeneration in cultured cortical neurons
    • Arias C., Sharma N., Davies P., and Shafit-Zagardo B. (1993) Okadaic acid induces early changes in microtubule-associated protein 2 and τ phosphorylation prior to neurodegeneration in cultured cortical neurons. J. Neurochem. 61, 673-682.
    • (1993) J. Neurochem. , vol.61 , pp. 673-682
    • Arias, C.1    Sharma, N.2    Davies, P.3    Shafit-Zagardo, B.4
  • 3
    • 0027391496 scopus 로고
    • Identification of p42 mitogen-activated protein kinase as a tyrosine kinase substrate activated by maximal electroconvulsive shock in hippocampus
    • Baraban J. M., Fiore R. S., Sanghera J. S., Paddon H. B., and Pelech S. L. (1993) Identification of p42 mitogen-activated protein kinase as a tyrosine kinase substrate activated by maximal electroconvulsive shock in hippocampus. J. Neurochem. 60, 330-336.
    • (1993) J. Neurochem. , vol.60 , pp. 330-336
    • Baraban, J.M.1    Fiore, R.S.2    Sanghera, J.S.3    Paddon, H.B.4    Pelech, S.L.5
  • 4
    • 0028879044 scopus 로고
    • Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: Implication of phosphoprotein phosphatase involvement
    • Baum L., Seger R., Woodgett J. R., Kawabata S., Maruyama K., Koyama M., Silver J., and Saitoh T. (1995) Overexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement. Mol. Brain Res. 34, 1-17.
    • (1995) Mol. Brain Res. , vol.34 , pp. 1-17
    • Baum, L.1    Seger, R.2    Woodgett, J.R.3    Kawabata, S.4    Maruyama, K.5    Koyama, M.6    Silver, J.7    Saitoh, T.8
  • 5
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K., Mandelkow E.-M. Biernat J., Piwnica-Worms H., and Mandelkow E. (1993) Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett. 336, 417-424.
    • (1993) FEBS Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Biernat J, M.E.-M.2    Piwnica-Worms, H.3    Mandelkow, E.4
  • 7
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11, 153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 9
    • 0029925968 scopus 로고    scopus 로고
    • Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons
    • Burack M. A. and Halpain S. (1996) Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons. Neuroscience 72, 167-184.
    • (1996) Neuroscience , vol.72 , pp. 167-184
    • Burack, M.A.1    Halpain, S.2
  • 10
    • 0027394488 scopus 로고
    • Okadaic acid activates p42 mitogen-activated protein kinase (MAP kinase; ERK-2) in B-lymphocytes but inhibits rather than augments cellular proliferation: Contrast with phorbol 12-myristate 13-acetate
    • Casillas A. M., Amaral K., Chegini-Farahani S., and Nel A. E. (1993) Okadaic acid activates p42 mitogen-activated protein kinase (MAP kinase; ERK-2) in B-lymphocytes but inhibits rather than augments cellular proliferation: contrast with phorbol 12-myristate 13-acetate. Biochem J. 290, 545-550.
    • (1993) Biochem J. , vol.290 , pp. 545-550
    • Casillas, A.M.1    Amaral, K.2    Chegini-Farahani, S.3    Nel, A.E.4
  • 11
    • 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., and Kirschner M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3, 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.W.4
  • 13
  • 14
    • 0027438048 scopus 로고
    • Activation of p42 mitogen-activated protein kinase by glutamate receptor stimulation in rat primary cortical cultures
    • Fiore R. S., Murphy T. H., Sanghera J. S., Pelech S. L., and Baraban J. M. (1993) Activation of p42 mitogen-activated protein kinase by glutamate receptor stimulation in rat primary cortical cultures. J. Neurochem. 61, 1626-1633.
    • (1993) J. Neurochem. , vol.61 , pp. 1626-1633
    • Fiore, R.S.1    Murphy, T.H.2    Sanghera, J.S.3    Pelech, S.L.4    Baraban, J.M.5
  • 16
    • 0024461007 scopus 로고
    • Tau protein becomes long and stiff upon phosphorylation: Correlation between paracrystalline structure and degree of phosphorylation
    • Hagestedt T., Lichtenberg B., Wille H., Mandelkow E.-M., and Mandelkow E. (1989) Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation. J. Cell Biol. 109, 1643-1651.
    • (1989) J. Cell Biol. , vol.109 , pp. 1643-1651
    • Hagestedt, T.1    Lichtenberg, B.2    Wille, H.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 19
    • 0026694067 scopus 로고
    • Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease
    • Ledesma M. D., Correas I., Avila J., and Diaz-Nido J. (1992) Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease. FEBS Lett. 308, 218-224.
    • (1992) FEBS Lett. , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, I.2    Avila, J.3    Diaz-Nido, J.4
  • 21
    • 0027335781 scopus 로고
    • p44mpk MAP kinase induces Alzheimer type alterations in tau function and in primary hippocampal neurons
    • Lu Q., Soria J. P., and Wood J. G. (1993) p44mpk MAP kinase induces Alzheimer type alterations in tau function and in primary hippocampal neurons. J. Neurosci. Res. 35, 439-444.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 439-444
    • Lu, Q.1    Soria, J.P.2    Wood, J.G.3
  • 23
    • 0028274129 scopus 로고
    • Differential regulation of calcium/ calmodulin-dependent protein kinase II and p42 MAP kinase activity by synaptic transmission
    • Murphy T. H., Blatter L. A., Bhat R. V., Fiore R. S., Wier W. G., and Baraban J. M. (1994) Differential regulation of calcium/ calmodulin-dependent protein kinase II and p42 MAP kinase activity by synaptic transmission. J. Neurosci. 14, 1320-1331.
    • (1994) J. Neurosci. , vol.14 , pp. 1320-1331
    • Murphy, T.H.1    Blatter, L.A.2    Bhat, R.V.3    Fiore, R.S.4    Wier, W.G.5    Baraban, J.M.6
  • 24
    • 0029063781 scopus 로고
    • Networking with proline-directed protein kinases implicated in tau phosphorylation
    • Pelech S. L. (1995) Networking with proline-directed protein kinases implicated in tau phosphorylation. Neurobiol. Aging 16, 247-256.
    • (1995) Neurobiol. Aging , vol.16 , pp. 247-256
    • Pelech, S.L.1
  • 25
    • 0028865376 scopus 로고
    • In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons
    • Saito T., Ishiguro K., Uchida T., Miyamoto E., Kishimoto T., and Hisanaga S. (1995) In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons. FEBS Lett. 376, 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
  • 27
    • 0027388775 scopus 로고
    • Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location
    • Szendrei G. I., Lee V. M.-Y., and Otvos L. Jr. (1993) Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location. J. Neurosci. Res. 34, 243-249.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 243-249
    • Szendrei, G.I.1    Lee, V.M.-Y.2    Otvos Jr., L.3
  • 29
    • 0026521716 scopus 로고
    • A protein kinase associated with paired helical filaments in Alzheimer disease
    • Vincent I. J. and Davies P. (1992) A protein kinase associated with paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. USA 89, 2878-2882.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2878-2882
    • Vincent, I.J.1    Davies, P.2
  • 30
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • Vincent I. J., Rosado M., and Davies P. (1996) Mitotic mechanisms in Alzheimer's disease? J. Cell Biol. 132, 413-425.
    • (1996) J. Cell Biol. , vol.132 , pp. 413-425
    • Vincent, I.J.1    Rosado, M.2    Davies, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.