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Volumn 255, Issue 1, 1998, Pages 13-16

Alzheimer-specific epitope of AT100 in transfected cell lines with tau: Toward an efficient cell model of tau abnormal phosphorylation

Author keywords

Alzheimer's disease; COS cells; Phosphorylation; SY5Y neuroblastoma cells; Tau protein; Transfection

Indexed keywords

OKADAIC ACID; TAU PROTEIN;

EID: 0032500861     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(98)00693-4     Document Type: Article
Times cited : (32)

References (21)
  • 2
    • 0030942149 scopus 로고    scopus 로고
    • Phosphorylated Ser422, a specific Alzheimer epitope is expressed by SKNSH-SY5Y cells after okadaic acid
    • Caillet-Boudin M.L., Delacourte A. Phosphorylated Ser422, a specific Alzheimer epitope is expressed by SKNSH-SY5Y cells after okadaic acid. NeuroReport. 8:1996;307-310.
    • (1996) NeuroReport , vol.8 , pp. 307-310
    • Caillet-Boudin, M.L.1    Delacourte, A.2
  • 3
    • 0030905501 scopus 로고    scopus 로고
    • Normal and pathological tau proteins as factors for microtubule assembly
    • Delacourte A., Buée L. Normal and pathological tau proteins as factors for microtubule assembly. Int. Rev. Cytol. 171:1997;167-224.
    • (1997) Int. Rev. Cytol. , vol.171 , pp. 167-224
    • Delacourte, A.1    Buée, L.2
  • 4
    • 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
  • 5
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles
    • Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles. Neuron. 3:1989;519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 6
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer's disease
    • Gong C.X., Shaikh S., Wang J.Z., Zaidi T., Grundke-Iqbal I., Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer's disease. J. Neurochem. 65:1995;732-738.
    • (1995) J. Neurochem. , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 7
    • 0029879046 scopus 로고    scopus 로고
    • Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau proteins
    • Hasegawa M., Jakes R., Crowther R.A., Lee V.M.Y., Ihara Y., Goedert M. Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau proteins. FEBS Lett. 384:1996;25-30.
    • (1996) FEBS Lett. , vol.384 , pp. 25-30
    • Hasegawa, M.1    Jakes, R.2    Crowther, R.A.3    Lee, V.M.Y.4    Ihara, Y.5    Goedert, M.6
  • 8
    • 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
  • 9
    • 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 L., Jr.5
  • 10
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • Hong M., Lee V.M.Y. Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J. Biol. Chem. 272:1997;19547-19553.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19547-19553
    • Hong, M.1    Lee, V.M.Y.2
  • 11
    • 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 de Voorde 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 De Voorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 12
    • 0028172239 scopus 로고
    • The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases
    • Mawal-Dewan M., Henley J., Van de Voorde A., Trojanowski J.Q., Lee V.M.Y. The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269:1994;30981-30987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van De Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.Y.5
  • 13
  • 14
    • 0027990436 scopus 로고
    • PHF-Tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by an in vitro phosphorylation of human brain tau by glycogen synthase kinase-3β
    • Mulot S.F.C., Hughes K., Woodgett J.R., Anderton B.H., Hanger D.P. PHF-Tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by an in vitro phosphorylation of human brain tau by glycogen synthase kinase-3β FEBS Lett. 349:1994;359-364.
    • (1994) FEBS Lett. , vol.349 , pp. 359-364
    • Mulot, S.F.C.1    Hughes, K.2    Woodgett, J.R.3    Anderton, B.H.4    Hanger, D.P.5
  • 15
    • 0031567583 scopus 로고    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. 411:1997;183-188.
    • (1997) FEBS Lett. , vol.411 , pp. 183-188
    • Munoz-Montano, J.R.1    Moreno, F.J.2    Avila, J.3    Diaz-Nido, J.4
  • 16
    • 0028803726 scopus 로고
    • Isoelectric point differentiates PHF-Tau from biopsy-derived human brain Tau proteins
    • Sergeant N., Bussière T., Vermersch P., Lejeune J.P., Delacourte A. Isoelectric point differentiates PHF-Tau from biopsy-derived human brain Tau proteins. NeuroReport. 6:1995;2217-2220.
    • (1995) NeuroReport , vol.6 , pp. 2217-2220
    • Sergeant, N.1    Bussière, T.2    Vermersch, P.3    Lejeune, J.P.4    Delacourte, A.5
  • 17
    • 0030840778 scopus 로고    scopus 로고
    • Two-dimensional characterization of paired helical filament-Tau from Alzheimer's disease: Demonstration of an additional 74 kDa component and age-related biochemical modifications
    • Sergeant N., David J.P., Goedert M., Jakes R., Vermersch P., Buée L., Lefranc D., Wattez A., Delacourte A. Two-dimensional characterization of paired helical filament-Tau from Alzheimer's disease: demonstration of an additional 74 kDa component and age-related biochemical modifications. J. Neurochem. 69:1997;834-844.
    • (1997) J. Neurochem. , vol.69 , pp. 834-844
    • Sergeant, N.1    David, J.P.2    Goedert, M.3    Jakes, R.4    Vermersch, P.5    Buée, L.6    Lefranc, D.7    Wattez, A.8    Delacourte, A.9
  • 18
    • 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., Fisher 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    Fisher, I.2
  • 19
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • Vincent I., Rosado M., Davies P. Mitotic mechanisms in Alzheimer's disease? J. Cell Biol. 132:1996;413-425.
    • (1996) J. Cell Biol. , vol.132 , pp. 413-425
    • Vincent, I.1    Rosado, M.2    Davies, P.3
  • 20
    • 0027221605 scopus 로고
    • Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation
    • Wadzinski B.E., Wheat W.H., Jaspers S., Peruski L.F. Jr., Lickteig R.L., Johnson G.L., Klemm D.J. Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation. Mol. Cell Biol. 13:1993;2822-2834.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2822-2834
    • Wadzinski, B.E.1    Wheat, W.H.2    Jaspers, S.3    Peruski L.F., Jr.4    Lickteig, R.L.5    Johnson, G.L.6    Klemm, D.J.7
  • 21
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3β 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-Fischhöfer Q., Biernat J., Mandelkow E.M., Illenberger S., Godemann R., Mandelkow E. Sequential phosphorylation of Tau by glycogen synthase kinase-3β 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-Fischhöfer, 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.