메뉴 건너뛰기




Volumn 288, Issue 46, 2013, Pages 33081-33095

Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathology

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; BINDING PROFILES; BRAIN SLICE CULTURES; COGNITIVE DECLINE; HYPERPHOSPHORYLATED; MECHANISTIC STUDIES; MONOCLONAL ANTIBODIES (MABS); PASSIVE IMMUNIZATION;

EID: 84887837879     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.494922     Document Type: Article
Times cited : (130)

References (57)
  • 3
    • 77951086901 scopus 로고    scopus 로고
    • Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid β monoclonal antibody in subjects with Alzheimer disease
    • Siemers, E. R., Friedrich, S., Dean, R. A., Gonzales, C. R., Farlow, M. R., Paul, S. M., and Demattos, R. B. (2010) Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid β monoclonal antibody in subjects with Alzheimer disease. Clin. Neuropharmacol. 33, 67-73
    • (2010) Clin. Neuropharmacol. , vol.33 , pp. 67-73
    • Siemers, E.R.1    Friedrich, S.2    Dean, R.A.3    Gonzales, C.R.4    Farlow, M.R.5    Paul, S.M.6    Demattos, R.B.7
  • 6
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-β immunotherapy?
    • Lemere, C. A., and Masliah, E. (2010) Can Alzheimer disease be prevented by amyloid-β immunotherapy? Nat. Rev. Neurol. 6, 108-119
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 7
    • 80054904670 scopus 로고    scopus 로고
    • Stages of the pathologic process in Alzheimer disease. Age categories from 1 to 100 years
    • Braak, H., Thal, D. R., Ghebremedhin, E., and Del Tredici, K. (2011) Stages of the pathologic process in Alzheimer disease. Age categories from 1 to 100 years. J. Neuropathol. Exp. Neurol. 70, 960-969
    • (2011) J. Neuropathol. Exp. Neurol. , vol.70 , pp. 960-969
    • Braak, H.1    Thal, D.R.2    Ghebremedhin, E.3    Del Tredici, K.4
  • 8
    • 0026070054 scopus 로고
    • Effects of injected Alzheimer β-amyloid cores in rat brain
    • Frautschy, S. A., Baird, A., and Cole, G. M. (1991) Effects of injected Alzheimer β-amyloid cores in rat brain. Proc. Natl. Acad. Sci. U.S.A. 88, 8362-8366
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8362-8366
    • Frautschy, S.A.1    Baird, A.2    Cole, G.M.3
  • 9
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-β and Tau. A toxic pas de deux in Alzheimer's disease
    • Ittner, L. M., and Gotz, J. (2011) Amyloid-β and Tau. A toxic pas de deux in Alzheimer's disease. Nat. Rev. Neurosci. 12, 65-72
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 10
  • 13
    • 0024369761 scopus 로고
    • The neuroanatomy of Alzheimer's disease
    • Pearson, R. C., and Powell, T. P. (1989) The neuroanatomy of Alzheimer's disease. Rev. Neurosci. 2, 101-122
    • (1989) Rev. Neurosci. , vol.2 , pp. 101-122
    • Pearson, R.C.1    Powell, T.P.2
  • 14
    • 0031457782 scopus 로고    scopus 로고
    • Bilateral injections of amyloid-β 25-35 into the amygdala of young Fischer rats. Behavioral, neurochemical, and time dependent histopathological effects
    • Sigurdsson, E. M., Lee, J. M., Dong, X. W., Hejna, M. J., and Lorens, S. A. (1997) Bilateral injections of amyloid-β 25-35 into the amygdala of young Fischer rats. Behavioral, neurochemical, and time dependent histopathological effects. Neurobiol. Aging 18, 591-608
    • (1997) Neurobiol. Aging , vol.18 , pp. 591-608
    • Sigurdsson, E.M.1    Lee, J.M.2    Dong, X.W.3    Hejna, M.J.4    Lorens, S.A.5
  • 15
    • 0030292993 scopus 로고    scopus 로고
    • Local and distant histopathological effects of unilateral amyloid-β 25-35 injections into the amygdala of young F344 rats
    • Sigurdsson, E. M., Lorens, S. A., Hejna, M. J., Dong, X. W., and Lee, J. M. (1996) Local and distant histopathological effects of unilateral amyloid-β 25-35 injections into the amygdala of young F344 rats. Neurobiol. Aging 17, 893-901
    • (1996) Neurobiol. Aging , vol.17 , pp. 893-901
    • Sigurdsson, E.M.1    Lorens, S.A.2    Hejna, M.J.3    Dong, X.W.4    Lee, J.M.5
  • 16
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils
    • Götz, J., Chen, F., van Dorpe, J., and Nitsch, R. M. (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils. Science 293, 1491-1495
    • (2001) Science , vol.293 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 18
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., and Hyman, B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42, 631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 19
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278-284
    • Braak, H., and Braak, E. (1995) Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16, 271-278; discussion 278-284
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 20
    • 0019935804 scopus 로고
    • Plaques, tangles and dementia. A quantitative study
    • Wilcock, G. K., and Esiri, M. M. (1982) Plaques, tangles and dementia. A quantitative study. J. Neurol. Sci. 56, 343-356
    • (1982) J. Neurol. Sci. , vol.56 , pp. 343-356
    • Wilcock, G.K.1    Esiri, M.M.2
  • 23
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni, A. A., Boutajangout, A., Quartermain, D., and Sigurdsson, E. M. (2007) Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J. Neurosci. 27, 9115-9129
    • (2007) J. Neurosci. , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 24
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., and Rosenmann, H. (2010) Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp. Neurol. 224, 472-485
    • (2010) Exp. Neurol. , vol.224 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5    Rosenmann, H.6
  • 25
    • 78650065372 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model
    • Boutajangout, A., Quartermain, D., and Sigurdsson, E. M. (2010) Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model. J. Neurosci. 30, 16559-16566
    • (2010) J. Neurosci. , vol.30 , pp. 16559-16566
    • Boutajangout, A.1    Quartermain, D.2    Sigurdsson, E.M.3
  • 26
    • 79960563632 scopus 로고    scopus 로고
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain
    • Boutajangout, A., Ingadottir, J., Davies, P., and Sigurdsson, E. M. (2011) Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. J. Neurochem. 118, 658-667
    • (2011) J. Neurochem. , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 28
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L Tau transgenic mice
    • Bi, M., Ittner, A., Ke, Y. D., Götz, J., and Ittner, L. M. (2011) Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L Tau transgenic mice. PLoS One 6, e26860
    • (2011) PLoS One , vol.6
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Götz, J.4    Ittner, L.M.5
  • 30
    • 84876908676 scopus 로고    scopus 로고
    • Tau passive immunotherapy in mutant P301L mice. Antibody affinity versus specificity
    • d'Abramo, C., Acker, C. M., Jimenez, H. T., and Davies, P. (2013) Tau passive immunotherapy in mutant P301L mice. Antibody affinity versus specificity. PLoS One 8, e62402
    • (2013) PLoS One , vol.8
    • D'Abramo, C.1    Acker, C.M.2    Jimenez, H.T.3    Davies, P.4
  • 31
    • 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
  • 33
    • 84865607168 scopus 로고    scopus 로고
    • Mechanistic studies of antibody-mediated clearance of Tau aggregates using an ex vivo brain slice model
    • Krishnamurthy, P. K., Deng, Y., and Sigurdsson, E. M. (2011) Mechanistic studies of antibody-mediated clearance of Tau aggregates using an ex vivo brain slice model. Front. Psychiatry 2, 59
    • (2011) Front Psychiatry , vol.2 , pp. 59
    • Krishnamurthy, P.K.1    Deng, Y.2    Sigurdsson, E.M.3
  • 35
    • 34547110577 scopus 로고    scopus 로고
    • Internalized antibodies to the Aβ domain of APP reduce neuronal Aβ and protect against synaptic alterations
    • Tampellini, D., Magrané, J., Takahashi, R. H., Li, F., Lin, M. T., Almeida, C. G., and Gouras, G. K. (2007) Internalized antibodies to the Aβ domain of APP reduce neuronal Aβ and protect against synaptic alterations. J. Biol. Chem. 282, 18895-18906
    • (2007) J. Biol. Chem. , vol.282 , pp. 18895-18906
    • Tampellini, D.1    Magrané, J.2    Takahashi, R.H.3    Li, F.4    Lin, M.T.5    Almeida, C.G.6    Gouras, G.K.7
  • 37
    • 0036931816 scopus 로고    scopus 로고
    • Organotypic slice cultures from transgenic mice as disease model systems
    • Duff, K., Noble, W., Gaynor, K., and Matsuoka, Y. (2002) Organotypic slice cultures from transgenic mice as disease model systems. J. Mol. Neurosci. 19, 317-320
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 317-320
    • Duff, K.1    Noble, W.2    Gaynor, K.3    Matsuoka, Y.4
  • 38
    • 0034472890 scopus 로고    scopus 로고
    • Metabolically active rat brain slices as a model to study the regulation of protein phosphorylation in mammalian brain
    • Gong, C. X., Lidsky, T., Wegiel, J., Grundke-Iqbal, I., and Iqbal, K. (2001) Metabolically active rat brain slices as a model to study the regulation of protein phosphorylation in mammalian brain. Brain Res. Brain Res. Protoc. 6, 134-140
    • (2001) Brain Res. Brain Res. Protoc. , vol.6 , pp. 134-140
    • Gong, C.X.1    Lidsky, T.2    Wegiel, J.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 39
    • 33846226521 scopus 로고    scopus 로고
    • The roles of autophagy in cerebral ischemia
    • Adhami, F., Schloemer, A., and Kuan, C. Y. (2007) The roles of autophagy in cerebral ischemia. Autophagy 3, 42-44
    • (2007) Autophagy , vol.3 , pp. 42-44
    • Adhami, F.1    Schloemer, A.2    Kuan, C.Y.3
  • 40
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • Komatsu, M., and Ichimura, Y. (2010) Physiological significance of selective degradation of p62 by autophagy. FEBS Lett. 584, 1374-1378
    • (2010) FEBS Lett , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 41
    • 77956393132 scopus 로고    scopus 로고
    • Involvement of Fc receptors in disorders of the central nervous system
    • Okun, E., Mattson, M. P., and Arumugam, T. V. (2010) Involvement of Fc receptors in disorders of the central nervous system. Neuromol. Med. 12, 164-178
    • (2010) Neuromol. Med. , vol.12 , pp. 164-178
    • Okun, E.1    Mattson, M.P.2    Arumugam, T.V.3
  • 42
    • 0023640751 scopus 로고
    • Intraneuronal IgG in the central nervous system. Uptake by retrograde axonal transport
    • Fabian, R. H., and Petroff, G. (1987) Intraneuronal IgG in the central nervous system. Uptake by retrograde axonal transport. Neurology 37, 1780-1784
    • (1987) Neurology , vol.37 , pp. 1780-1784
    • Fabian, R.H.1    Petroff, G.2
  • 44
    • 70249127559 scopus 로고    scopus 로고
    • Tau-focused immunotherapy for Alzheimer's disease and related tauopathies
    • Sigurdsson, E. M. (2009) Tau-focused immunotherapy for Alzheimer's disease and related tauopathies. Curr. Alzheimer Res. 6, 446-450
    • (2009) Curr. Alzheimer Res. , vol.6 , pp. 446-450
    • Sigurdsson, E.M.1
  • 45
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease. Neuropathologic evidence for a mechanism of increased β-amyloidogenesis
    • Cataldo, A. M., Barnett, J. L., Pieroni, C., and Nixon, R. A. (1997) Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease. Neuropathologic evidence for a mechanism of increased β-amyloidogenesis. J. Neurosci. 17, 6142-6151
    • (1997) J. Neurosci. , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 48
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • Maas, T., Eidenmüller, J., and Brandt, R. (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J. Biol. Chem. 275, 15733-15740
    • (2000) J. Biol. Chem. , vol.275 , pp. 15733-15740
    • Maas, T.1    Eidenmüller, J.2    Brandt, R.3
  • 49
    • 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
  • 52
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C., and Hall, G. F. (2012) Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J. Biol. Chem. 287, 3842-3849
    • (2012) J. Biol. Chem. , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6    Jackson, B.7    McKee, A.C.8    Alvarez, V.E.9    Lee, N.C.10    Hall, G.F.11
  • 54
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • Chai, X., Dage, J. L., and Citron, M. (2012) Constitutive secretion of tau protein by an unconventional mechanism. Neurobiol. Dis. 48, 356-366
    • (2012) Neurobiol. Dis. , vol.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 55
    • 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
  • 56
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways. Genes to neurodegeneration in Alzheimer's disease
    • Nixon, R. A., and Cataldo, A. M. (2006) Lysosomal system pathways. Genes to neurodegeneration in Alzheimer's disease. J. Alzheimers Dis. 9, 277-289
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 57
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease. Possible role in tangle formation
    • Kuusisto, E., Salminen, A., and Alafuzoff, I. (2002) Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease. Possible role in tangle formation. Neuropathol. Appl. Neurobiol. 28, 228-237
    • (2002) Neuropathol. Appl. Neurobiol. , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.