메뉴 건너뛰기




Volumn 290, Issue 2, 2015, Pages 1049-1065

Conformation determines the seeding potencies of native and recombinant Tau aggregates

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; MAMMALS;

EID: 84920901644     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.589309     Document Type: Article
Times cited : (205)

References (76)
  • 1
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini, M. G., and Goedert, M. (2013) Tau pathology and neurodegeneration. Lancet Neurol. 12, 609-622
    • (2013) Lancet Neurol. , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 2
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein Tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989) Multiple isoforms of human microtubule-associated protein Tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 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
  • 3
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the mi-crotubule-associated protein Tau
    • Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., and Klug, A. (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the mi-crotubule-associated protein Tau. Proc. Natl. Acad. Sci. 85, 4051-4055
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 5
    • 84875279731 scopus 로고    scopus 로고
    • The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
    • Wegmann, S., Medalsy, I. D., Mandelkow, E., and Müller, D. J. (2013) The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush. Proc. Natl. Acad. Sci. 110, E313-E321
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. E313-E321
    • Wegmann, S.1    Medalsy, I.D.2    Mandelkow, E.3    Müller, D.J.4
  • 6
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J., and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8, 159-168
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 7
    • 33751277941 scopus 로고    scopus 로고
    • Quantitative analysis of neurofibrillary pathology in a general population to reappraise neuropathological criteria for senile dementia of the neurofibrillary tangle type (tangle-only dementia): The Hisayama Study
    • Noda, K., Sasaki, K., Fujimi, K., Wakisaka, Y., Tanizaki, Y., Wakugawa, Y., Kiyohara, Y., Iida, M., Aizawa, H., and Iwaki, T. (2006) Quantitative analysis of neurofibrillary pathology in a general population to reappraise neuropathological criteria for senile dementia of the neurofibrillary tangle type (tangle-only dementia): the Hisayama Study. Neuropathology 26, 508-518
    • (2006) Neuropathology , vol.26 , pp. 508-518
    • Noda, K.1    Sasaki, K.2    Fujimi, K.3    Wakisaka, Y.4    Tanizaki, Y.5    Wakugawa, Y.6    Kiyohara, Y.7    Iida, M.8    Aizawa, H.9    Iwaki, T.10
  • 8
    • 0034963745 scopus 로고    scopus 로고
    • Tau isoform profile and phosphorylation state in dementia pugilistica recapitulate Alzheimer's disease
    • Schmidt, M. L., Zhukareva, V., Newell, K. L., Lee, V. M. Y., and Trojanowski J. Q. (2001) Tau isoform profile and phosphorylation state in dementia pugilistica recapitulate Alzheimer's disease. Acta Neuropathol. 101, 518-524
    • (2001) Acta Neuropathol. , vol.101 , pp. 518-524
    • Schmidt, M.L.1    Zhukareva, V.2    Newell, K.L.3    Lee, V.M.Y.4    Trojanowski, J.Q.5
  • 10
    • 0025857173 scopus 로고
    • Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type
    • Flament, S., Delacourte, A., Verny, M., Hauw, J. J., and Javoy-Agid, F. (1991) Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol. 81, 591-596
    • (1991) Acta Neuropathol. , vol.81 , pp. 591-596
    • Flament, S.1    Delacourte, A.2    Verny, M.3    Hauw, J.J.4    Javoy-Agid, F.5
  • 13
  • 18
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 19
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Pérez, M., Valpuesta, J. M., Medina, M., Montejo de Garcini, E., and Avila, J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J. Neurochem. 67, 1183-1190
    • (1996) J. Neurochem. , vol.67 , pp. 1183-1190
    • Pérez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 20
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344-349
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 21
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid beta peptides: In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson, D. M., and Binder, L. I. (1997) Free fatty acids stimulate the polymerization of tau and amyloid beta peptides: in vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am. J. Pathol. 150, 2181-2195
    • (1997) Am. J. Pathol. , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 22
    • 80655128134 scopus 로고    scopus 로고
    • Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein
    • Ramachandran, G., and Udgaonkar, J. B. (2011) Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein. J. Biol. Chem. 286, 38948-38959
    • (2011) J. Biol. Chem. , vol.286 , pp. 38948-38959
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 23
    • 84867390250 scopus 로고    scopus 로고
    • Identification of an aggrega-tion-prone structure of tau
    • Elbaum-Garfinkle, S., and Rhoades, E. (2012) Identification of an aggrega-tion-prone structure of tau. J. Am. Chem. Soc. 134, 16607-16613
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16607-16613
    • Elbaum-Garfinkle, S.1    Rhoades, E.2
  • 24
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming βstructure
    • von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., and Mandelkow, E. (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming βstructure. Proc. Natl. Acad. Sci. 97, 5129-5134
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.5
  • 25
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of Tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure
    • von Bergen, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2001) Mutations of Tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure. J. Biol. Chem. 276, 48165-48174
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 26
    • 79958110883 scopus 로고    scopus 로고
    • Alzheimer's pathogenesis: Is there neuron-to-neuron propagation?
    • Braak, H., and Del Tredici, K. (2011) Alzheimer's pathogenesis: is there neuron-to-neuron propagation? Acta Neuropathol. 121, 589-595
    • (2011) Acta Neuropathol. , vol.121 , pp. 589-595
    • Braak, H.1    Del Tredici, K.2
  • 27
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimerrelated changes
    • Braak, H., and Braak, E. (1991) Neuropathological stageing of Alzheimerrelated changes. Acta Neuropathol. 82, 239-259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 29
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert, M., Clavaguera, F., and Tolnay, M. (2010) The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 33, 317-325
    • (2010) Trends Neurosci. , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 31
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. K., and Lee, V. M. Y. (2013) Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J. Neurosci. 33, 1024-1037
    • (2013) J. Neurosci. , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.K.5    Lee, V.M.Y.6
  • 34
    • 0027229676 scopus 로고
    • Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes
    • Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S. L., DeArmond, S. J., and Prusiner, S. B. (1993) Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73, 979-988
    • (1993) Cell , vol.73 , pp. 979-988
    • Scott, M.1    Groth, D.2    Foster, D.3    Torchia, M.4    Yang, S.L.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 38
    • 0032763817 scopus 로고    scopus 로고
    • Sporadic Creutzfeldt-Jakob disease: Co-occurrence of different types of PrPSc in the same brain
    • Puoti, G., Giaccone, G., Rossi, G., Canciani, B., Bugiani, O., and Tagliavini, F. (1999) Sporadic Creutzfeldt-Jakob disease: co-occurrence of different types of PrPSc in the same brain. Neurology 53, 2173-2176
    • (1999) Neurology , vol.53 , pp. 2173-2176
    • Puoti, G.1    Giaccone, G.2    Rossi, G.3    Canciani, B.4    Bugiani, O.5    Tagliavini, F.6
  • 41
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of Tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L., and Diamond, M. I. (2009) Propagation of Tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845-12852
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 42
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo, J. L., and Lee, V. M. Y. (2011) Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J. Biol. Chem. 286, 15317-15331
    • (2011) J. Biol. Chem. , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.Y.2
  • 43
    • 84862003756 scopus 로고    scopus 로고
    • Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes
    • Santa-Maria, I., Varghese, M., Ksiezak-Reding, H., Dzhun, A., Wang, J., and Pasinetti, G. M. (2012) Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes. J. Biol. Chem. 287, 20522-20533
    • (2012) J. Biol. Chem. , vol.287 , pp. 20522-20533
    • Santa-Maria, I.1    Varghese, M.2    Ksiezak-Reding, H.3    Dzhun, A.4    Wang, J.5    Pasinetti, G.M.6
  • 44
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of Tau aggregation by fibrillar species
    • Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., and Diamond, M. I. (2012) Trans-cellular propagation of Tau aggregation by fibrillar species. J. Biol. Chem. 287, 19440-19451
    • (2012) J. Biol. Chem. , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 47
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo, J. L., and Lee, V. M. Y. (2014) Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat. Med. 20, 130-138
    • (2014) Nat. Med. , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.Y.2
  • 50
    • 33748715165 scopus 로고    scopus 로고
    • Sequential phosphorylation of tau protein by cAMP-dependent protein kinase and SAPK4/p38δ; or JNK2 in the presence of heparin generates the AT100 epitope
    • Yoshida, H., and Goedert, M. (2006) Sequential phosphorylation of tau protein by cAMP-dependent protein kinase and SAPK4/p38δ; or JNK2 in the presence of heparin generates the AT100 epitope. J. Neurochem. 99, 154-164
    • (2006) J. Neurochem. , vol.99 , pp. 154-164
    • Yoshida, H.1    Goedert, M.2
  • 52
    • 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., and Davies, P. (1999) Hierarchical phosphorylation of recombinant tau by the paired helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase. J. Neurochem. 72, 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
  • 53
    • 77049126656 scopus 로고    scopus 로고
    • Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase
    • Tremblay, M. A., Acker, C. M., and Davies, P. (2010) Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase, Arg. J. Alzheimers Dis. 19, 721-733
    • (2010) Arg. J. Alzheimers Dis. , vol.19 , pp. 721-733
    • Tremblay, M.A.1    Acker, C.M.2    Davies, P.3
  • 54
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • Vincent, I., 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.1    Rosado, M.2    Davies, P.3
  • 55
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha, G. A., Bowser, R., Kazam, I. G., and Davies, P. (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J. Neurosci. Res. 48, 128-132
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 56
    • 0030783142 scopus 로고    scopus 로고
    • A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha, G. A., Lane, E., Vincent, I., Otvos, L., Jr., Hoffmann, R., and Davies, P. (1997) A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J. Neurochem. 69, 2087-2095
    • (1997) J. Neurochem. , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos, L.4    Hoffmann, R.5    Davies, P.6
  • 57
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert, M., Jakes, R., and Vanmechelen, E. (1995) Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189, 167-169
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 59
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stressactivated protein kinases
    • Goedert, M., Hasegawa, M., Jakes, R., Lawler, S., Cuenda, A., and Cohen, P. (1997) Phosphorylation of microtubule-associated protein tau by stressactivated protein kinases. FEBS Lett. 409, 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
  • 61
    • 84888594143 scopus 로고    scopus 로고
    • Biology and genetics of prions causing neurodegeneration
    • Prusiner, S. B. (2013) Biology and genetics of prions causing neurodegeneration. Annu. Rev. Genet. 47, 601-623
    • (2013) Annu. Rev. Genet. , vol.47 , pp. 601-623
    • Prusiner, S.B.1
  • 66
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
    • Luk, K. C., Kehm, V. M., Zhang, B., O'Brien, P., Trojanowski, J. Q., and Lee, V. M. Y. (2012) Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J. Exp. Med. 209, 975-986
    • (2012) J. Exp. Med. , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 67
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotype
    • Tanaka, M., Collins, S. R., Toyama, B. H., and Weissman, J. S. (2006) The physical basis of how prion conformations determine strain phenotype. Nature 442, 585-589
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 70
    • 84885455505 scopus 로고    scopus 로고
    • Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein
    • Morozova, O. A., March, Z. M., Robinson, A. S., and Colby, D. W. (2013) Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein. Biochemistry 52, 6960-6967
    • (2013) Biochemistry , vol.52 , pp. 6960-6967
    • Morozova, O.A.1    March, Z.M.2    Robinson, A.S.3    Colby, D.W.4
  • 73
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkin-son-like neurodegeneration in nontransgenic mice
    • Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O'Brien, P., Trojanowski, J. Q., and Lee, V. M. Y. (2012) Pathological α-synuclein transmission initiates Parkin-son-like neurodegeneration in nontransgenic mice. Science 338, 949-953
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.