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Volumn 2, Issue 7, 1996, Pages 783-787

Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

Author keywords

[No Author keywords available]

Indexed keywords

NEUROFILAMENT PROTEIN; TAU PROTEIN;

EID: 0029999787     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0796-783     Document Type: Article
Times cited : (732)

References (30)
  • 1
    • 0014851803 scopus 로고
    • Observations on the brains of demented old people
    • Tomlinson, B.E., Blessed, G. & Roth, M. Observations on the brains of demented old people. J. Neurol. Sci. 11, 205-242 (1970).
    • (1970) J. Neurol. Sci. , vol.11 , pp. 205-242
    • Tomlinson, B.E.1    Blessed, G.2    Roth, M.3
  • 2
    • 0023200370 scopus 로고
    • Histopathological criteria for progressive dementia disorders: Clinical-pathological correlation and classification by multivariate data analysis
    • Alafuzoff, I., Iqbal, K., Friden, H., Adolfsson, R. & Winblad, B. Histopathological criteria for progressive dementia disorders: Clinical-pathological correlation and classification by multivariate data analysis. Acta Neuropathol. 74, 209-225 (1987).
    • (1987) Acta Neuropathol. , vol.74 , pp. 209-225
    • Alafuzoff, I.1    Iqbal, K.2    Friden, H.3    Adolfsson, R.4    Winblad, B.5
  • 3
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal, I. et al. Abnormal phosphorylation of the microtubule-associated protein tau in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA 83, 4913-4917 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1
  • 4
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau: A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I. et al. Microtubule-associated protein tau: A component of Alzheimer paired helical filaments. J. Biol. Chem. 261, 6084-6089 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1
  • 5
    • 0027361281 scopus 로고
    • Microtubule associated protein tau: Abnormal phosphorylation of non-paired helical filament pool in Alzheimer disease
    • Köpke, E. et al. Microtubule associated protein tau: Abnormal phosphorylation of non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24374-24384 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Köpke, E.1
  • 6
    • 0026694783 scopus 로고
    • Brain levels of microtubule associated protein tau are elevated in Alzheimer's disease brain: A radioimmunoslot-blot assay for nanograms of the protein
    • Khatoon, S., Grundke-Iqbal, I. & Iqbal, K. Brain levels of microtubule associated protein tau are elevated in Alzheimer's disease brain: A radioimmunoslot-blot assay for nanograms of the protein. J. Neurochem. 59, 750-753 (1992).
    • (1992) J. Neurochem. , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 7
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso, A. d.C., Zaidi, T., Grundke-Iqbal, I. & Iqbal, K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. USA 91, 5562-5566 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5562-5566
    • Alonso, A.D.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 8
    • 0028361538 scopus 로고
    • Alzheimer paired helical filaments: Restoration of the biological activity by dephosphorylation
    • Iqbal, K., Zaidi, T., Bancher, C. & Grundke-Iqbal, I. Alzheimer paired helical filaments: Restoration of the biological activity by dephosphorylation. FEBS Lett. 349, 104-108 (1994).
    • (1994) FEBS Lett. , vol.349 , pp. 104-108
    • Iqbal, K.1    Zaidi, T.2    Bancher, C.3    Grundke-Iqbal, I.4
  • 9
    • 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, 4854-4860 (1995).
    • (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
  • 10
    • 0022550260 scopus 로고
    • Defective brain microtubule assembly in Alzheimer's disease
    • Iqbal, K. et al. Defective brain microtubule assembly in Alzheimer's disease. Lancet 2, 421-426 (1986).
    • (1986) Lancet , vol.2 , pp. 421-426
    • Iqbal, K.1
  • 11
    • 0025840546 scopus 로고
    • The microtubule associated protein tau forms a triple stranded left-hand helical polymer
    • Ruben, G.C. et al. The microtubule associated protein tau forms a triple stranded left-hand helical polymer. J. Biol. Chem. 266, 22019-22027 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 22019-22027
    • Ruben, G.C.1
  • 12
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule associated protein tau: An abnormal posttranslational modification in Alzheimer disease
    • see accompanying manuscript
    • Wang, J.-Z., Grundke-Iqbal, I. & Iqbal, K. Glycosylation of microtubule associated protein tau: An abnormal posttranslational modification in Alzheimer disease. Nature Medicine, see accompanying manuscript.
    • Nature Medicine
    • Wang, J.-Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 13
    • 0026712151 scopus 로고
    • Alzheimer neurofibrillary tangles contain 2.1-nm filaments structurally identical to the microtubule associated protein tau: A high resolution transmission electron microscope study of tangles and senile plaque core amyloid
    • Ruben, G.C., Iqbal, K., Wisniewski, H.M., Johnson, J.E. Jr. & Grundke-Iqbal, I. Alzheimer neurofibrillary tangles contain 2.1-nm filaments structurally identical to the microtubule associated protein tau: A high resolution transmission electron microscope study of tangles and senile plaque core amyloid. Brain Res. 590, 164-179 (1992).
    • (1992) Brain Res. , vol.590 , pp. 164-179
    • Ruben, G.C.1    Iqbal, K.2    Wisniewski, H.M.3    Johnson Jr., J.E.4    Grundke-Iqbal, I.5
  • 14
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille, H., Drewes, G., Biernat, J., Mandelkow, E.M. & Mandelkow, E. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 118, 573-584 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 15
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther, R.A., Olesen, O.F., Jakes, R. & Goedert, M. The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease. FEBS Lett. 309, 199-202 (1992).
    • (1992) FEBS Lett. , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 16
    • 0028121105 scopus 로고
    • Assembly of Alzheimer-like filaments from full-length tau protein
    • Crowther, R.A., Olesen, O.F., Smith, M., Jakes, R. & Goedert, M. Assembly of Alzheimer-like filaments from full-length tau protein. FEBS Lett. 337, 135-138 (1994).
    • (1994) FEBS Lett. , vol.337 , pp. 135-138
    • Crowther, R.A.1    Olesen, O.F.2    Smith, M.3    Jakes, R.4    Goedert, M.5
  • 17
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein τ controls the in vitro assembly of paired helical filaments
    • Schweers, O., Mandelkow, E.M., Biernat, J. & Mandelkow, E. Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein τ controls the in vitro assembly of paired helical filaments. Proc. Natl. Acad. Sci. USA 92, 8463-8467 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 18
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher, C. et al. Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 477, 90-99 (1989).
    • (1989) Brain Res. , vol.477 , pp. 90-99
    • Bancher, C.1
  • 19
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C.-X., Singh, T.J., Grundke-Iqbal, I. & Iqbal, K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61, 921-927 (1993).
    • (1993) J. Neurochem. , vol.61 , pp. 921-927
    • Gong, C.-X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 20
    • 0029113874 scopus 로고
    • Phosphatase activity towards abnormally phosphorylated τ: Decrease in Alzheimer disease brain
    • Gong, C.-X. et al. Phosphatase activity towards abnormally phosphorylated τ: Decrease in Alzheimer disease brain. J. Neurochem. 65, 732-738, 1995.
    • (1995) J. Neurochem. , vol.65 , pp. 732-738
    • Gong, C.-X.1
  • 21
    • 0023833792 scopus 로고
    • Electron microscope studies of free and proteinase-bound duck ovostatins (ovomacroglobins): Model of ovostatin structure and its transformation upon proteolysis
    • Ruben, G.C., Harris, E.D. Jr. & Nagase, H. Electron microscope studies of free and proteinase-bound duck ovostatins (ovomacroglobins): Model of ovostatin structure and its transformation upon proteolysis. J. Biol. Chem. 263, 2861-2869 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 2861-2869
    • Ruben, G.C.1    Harris Jr., E.D.2    Nagase, H.3
  • 22
    • 0026783215 scopus 로고
    • Immune electron microscopic characterization of monoclonal antibodies to Alzheimer neurofibrillary tangles
    • Wrzolek, M.A. et al. Immune electron microscopic characterization of monoclonal antibodies to Alzheimer neurofibrillary tangles. Am. J. Pathol. 141, 343-355 (1992).
    • (1992) Am. J. Pathol. , vol.141 , pp. 343-355
    • Wrzolek, M.A.1
  • 23
    • 0023772557 scopus 로고
    • Microtubule-associated polypeptides tau are altered in Alzheimer paired helical filaments
    • Grundke-Iqbal, I. et al. Microtubule-associated polypeptides tau are altered in Alzheimer paired helical filaments. Mol. Brain Res. 4, 43-52 (1988).
    • (1988) Mol. Brain Res. , vol.4 , pp. 43-52
    • Grundke-Iqbal, I.1
  • 24
    • 0029037696 scopus 로고
    • Bovine and human tau, highly homologous but less crossreactive: Implications for Alzheimer disease
    • Alonso, A. del C., Grundke-Iqbal, I. & Iqbal, K. Bovine and human tau, highly homologous but less crossreactive: Implications for Alzheimer disease. Brain Res. 31, 194-200 (1995).
    • (1995) Brain Res. , vol.31 , pp. 194-200
    • Alonso, A.D.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 25
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A. & Weinstein, D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70, 241-250 (1976).
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 27
    • 0018380690 scopus 로고
    • Decoration and stabilization of intact, smooth-walled microtubules with microtubule-associated proteins
    • Sloboda, R.D. & Rosenbaum, J.L. Decoration and stabilization of intact, smooth-walled microtubules with microtubule-associated proteins. Biochemistry 18, 48-55 (1979).
    • (1979) Biochemistry , vol.18 , pp. 48-55
    • Sloboda, R.D.1    Rosenbaum, J.L.2
  • 28
    • 0026551711 scopus 로고
    • The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region
    • Biernat, J. et al. The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J. 11, 1593-1597 (1992).
    • (1992) EMBO J. , vol.11 , pp. 1593-1597
    • Biernat, J.1
  • 29
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated τ PHF proteins display the same biochemical properties as normal τ
    • Greenberg, S.G., Davies, P., Schein, J.D. & Binder, L. Hydrofluoric acid-treated τ PHF proteins display the same biochemical properties as normal τ. J. Biol. Chem. 267, 564-569 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.4
  • 30
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residue 396 and residue 404
    • Otvos, L. et al. Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residue 396 and residue 404. J. Neurosci. Res. 39, 669-673 (1994).
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.