메뉴 건너뛰기




Volumn 2, Issue 3, 2015, Pages 241-255

Passive immunotherapy of tauopathy targeting pSer413-tau: a pilot study in mice

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; SYNAPTOPHYSIN;

EID: 84930536875     PISSN: None     EISSN: 23289503     Source Type: Journal    
DOI: 10.1002/acn3.171     Document Type: Article
Times cited : (56)

References (38)
  • 2
    • 36949014742 scopus 로고    scopus 로고
    • Tauopathy models and human neuropathology: similarities and differences
    • Frank S, Clavaguera F, Tolnay M. Tauopathy models and human neuropathology: similarities and differences. Acta Neuropathol 2008;115:39–53.
    • (2008) Acta Neuropathol , vol.115 , pp. 39-53
    • Frank, S.1    Clavaguera, F.2    Tolnay, M.3
  • 3
    • 84879330487 scopus 로고    scopus 로고
    • Neurodegenerative disorder FTDP-17-related tau intron 10 + 16C → T mutation increases tau exon 10 splicing and causes tauopathy in transgenic mice
    • Umeda T, Yamashita T, Kimura T, et al. Neurodegenerative disorder FTDP-17-related tau intron 10 + 16C → T mutation increases tau exon 10 splicing and causes tauopathy in transgenic mice. Am J Pathol 2013;183:211–225.
    • (2013) Am J Pathol , vol.183 , pp. 211-225
    • Umeda, T.1    Yamashita, T.2    Kimura, T.3
  • 4
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci 2007;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
  • 5
    • 78650065372 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model
    • Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model. J Neurosci 2010;30:16559–16566.
    • (2010) J Neurosci , vol.30 , pp. 16559-16566
    • Boutajangout, A.1    Quartermain, D.2    Sigurdsson, E.M.3
  • 6
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice
    • Bi M, Ittner A, Ke YD, et al. Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice. PLoS One 2011;6:e26860.
    • (2011) PLoS One , vol.6
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3
  • 7
    • 84922479255 scopus 로고    scopus 로고
    • Efficacy and safety of a liposome-based vaccine against protein tau, assessed in tau.P301L mice that model tauopathy
    • Theunis C, Crespo-Biel N, Gafner V, et al. Efficacy and safety of a liposome-based vaccine against protein tau, assessed in tau.P301L mice that model tauopathy. PLoS One 2013;8:e72301.
    • (2013) PLoS One , vol.8
    • Theunis, C.1    Crespo-Biel, N.2    Gafner, V.3
  • 8
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A, et al. Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp Neurol 2010;224:472–485.
    • (2010) Exp Neurol , vol.224 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3
  • 9
    • 84860531636 scopus 로고    scopus 로고
    • Targeting phospho-Ser422 by active tau immunotherapy in the THYTau22 mouse model: a suitable therapeutic approach
    • Troquier L, Caillierez R, Burnouf S, et al. Targeting phospho-Ser422 by active tau immunotherapy in the THYTau22 mouse model: a suitable therapeutic approach. Curr Alzheimer Res 2012;9:397–405.
    • (2012) Curr Alzheimer Res , vol.9 , pp. 397-405
    • Troquier, L.1    Caillierez, R.2    Burnouf, S.3
  • 10
    • 84901784841 scopus 로고    scopus 로고
    • Vaccination with sarkosyl insoluble PHF-tau decrease neurofibrillary tangles formation in aged tau transgenic mouse model: a pilot study
    • Suppl 1
    • Ando K, Kabova A, Stygelbout V, et al. Vaccination with sarkosyl insoluble PHF-tau decrease neurofibrillary tangles formation in aged tau transgenic mouse model: a pilot study. J Alzheimers Dis 2014;40 Suppl 1:S135–145.
    • (2014) J Alzheimers Dis , vol.40 , pp. S135-145
    • Ando, K.1    Kabova, A.2    Stygelbout, V.3
  • 11
    • 33749614555 scopus 로고    scopus 로고
    • Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein
    • Rosenmann H, Grigoriadis N, Karussis D, et al. Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein. Arch Neurol 2006;63:1459–1467.
    • (2006) Arch Neurol , vol.63 , pp. 1459-1467
    • Rosenmann, H.1    Grigoriadis, N.2    Karussis, D.3
  • 12
    • 84882793431 scopus 로고    scopus 로고
    • Repeated immunization of mice with phos-phorylated-tau peptides causes neuroinflammation
    • Rozenstein-Tsalkovich L, Grigoriadis N, Lourbopoulos A, et al. Repeated immunization of mice with phos-phorylated-tau peptides causes neuroinflammation. Exp Neurol 2013;248:451–456.
    • (2013) Exp Neurol , vol.248 , pp. 451-456
    • Rozenstein-Tsalkovich, L.1    Grigoriadis, N.2    Lourbopoulos, A.3
  • 13
    • 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, Sigurdsson EM. Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. J Neurochem 2011;118:658–667.
    • (2011) J Neurochem , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 14
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti-tau antibodies in two transgenic models: reduction of tau pathology and delay of disease progression
    • Chai X, Wu S, Murray TK, et al. Passive immunization with anti-tau antibodies in two transgenic models: reduction of tau pathology and delay of disease progression. J Biol Chem 2011;286:34457–34467.
    • (2011) J Biol Chem , vol.286 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3
  • 15
    • 84876908676 scopus 로고    scopus 로고
    • Tau passive immunotherapy in mutant P301L mice: antibody affinity versus specificity
    • d'Abramo C, Acker CM, Jimenez HT, Davies P. Tau passive immunotherapy in mutant P301L mice: antibody affinity versus specificity. PLoS One 2013;8:e62402.
    • (2013) PLoS One , vol.8
    • d'Abramo, C.1    Acker, C.M.2    Jimenez, H.T.3    Davies, P.4
  • 16
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • Berger Z, Roder H, Hanna A, et al. Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J Neurosci 2007;27:3650–3662.
    • (2007) J Neurosci , vol.27 , pp. 3650-3662
    • Berger, Z.1    Roder, H.2    Hanna, A.3
  • 17
    • 77950617631 scopus 로고    scopus 로고
    • A mouse model of amyloid beta oligomers: their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo
    • Tomiyama T, Matsuyama S, Iso H, et al. A mouse model of amyloid beta oligomers: their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo. J Neurosci 2010;30:4845–4856.
    • (2010) J Neurosci , vol.30 , pp. 4845-4856
    • Tomiyama, T.1    Matsuyama, S.2    Iso, H.3
  • 18
    • 84858965241 scopus 로고    scopus 로고
    • Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
    • Lasagna-Reeves CA, Castillo-Carranza DL, Sengupta U, et al. Identification of oligomers at early stages of tau aggregation in Alzheimer's disease. FASEB J 2012;26:1946–1959.
    • (2012) FASEB J , vol.26 , pp. 1946-1959
    • Lasagna-Reeves, C.A.1    Castillo-Carranza, D.L.2    Sengupta, U.3
  • 19
    • 84868269943 scopus 로고    scopus 로고
    • Alzheimer brain-derived tau oligomers propagate  pathology from endogenous tau
    • Lasagna-Reeves CA, Castillo-Carranza DL, Sengupta U, et al. Alzheimer brain-derived tau oligomers propagate  pathology from endogenous tau. Sci Rep 2012;2:700.
    • (2012) Sci Rep , vol.2 , pp. 700
    • Lasagna-Reeves, C.A.1    Castillo-Carranza, D.L.2    Sengupta, U.3
  • 20
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J, McGowan E, Rockwood J, et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat Genet 2000;25:402–405.
    • (2000) Nat Genet , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 21
    • 0036850725 scopus 로고    scopus 로고
    • Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein
    • Allen B, Ingram E, Takao M, et al. Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein. J Neurosci 2002;22:9340–9351.
    • (2002) J Neurosci , vol.22 , pp. 9340-9351
    • Allen, B.1    Ingram, E.2    Takao, M.3
  • 22
    • 0026619472 scopus 로고
    • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
    • Ishiguro K, Omori A, Takamatsu M, et al. Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments. Neurosci Lett 1992;148:202–206.
    • (1992) Neurosci Lett , vol.148 , pp. 202-206
    • Ishiguro, K.1    Omori, A.2    Takamatsu, M.3
  • 23
    • 0030597165 scopus 로고    scopus 로고
    • Immunocytochemistry of tau phosphoserine 413 and tau protein kinase I in Alzheimer pathology
    • Shiurba RA, Ishiguro K, Takahashi M, et al. Immunocytochemistry of tau phosphoserine 413 and tau protein kinase I in Alzheimer pathology. Brain Res 1996;737:119–132.
    • (1996) Brain Res , vol.737 , pp. 119-132
    • Shiurba, R.A.1    Ishiguro, K.2    Takahashi, M.3
  • 24
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 2009;15:112–119.
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 25
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack JC, Schneider A, Mandelkow EM, Hyman BT. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol 2002;103:26–35.
    • (2002) Acta Neuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 26
    • 33644870413 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism
    • Li T, Paudel HK. Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism. Biochemistry 2006;45:3125–3133.
    • (2006) Biochemistry , vol.45 , pp. 3125-3133
    • Li, T.1    Paudel, H.K.2
  • 27
    • 77952888156 scopus 로고    scopus 로고
    • The pattern of human tau phosphorylation is the result of priming and feedback events in primary hippocampal neurons
    • Bertrand J, Plouffe V, Sénéchal P, Leclerc N. The pattern of human tau phosphorylation is the result of priming and feedback events in primary hippocampal neurons. Neuroscience 2010;168:323–334.
    • (2010) Neuroscience , vol.168 , pp. 323-334
    • Bertrand, J.1    Plouffe, V.2    Sénéchal, P.3    Leclerc, N.4
  • 28
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K, Lewis J, Spires T, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 2005;309:476–481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3
  • 29
    • 79959571777 scopus 로고    scopus 로고
    • Characterization of prefibrillar tau oligomers in vitro and in Alzheimer disease
    • Patterson KR, Remmers C, Fu Y, et al. Characterization of prefibrillar tau oligomers in vitro and in Alzheimer disease. J Biol Chem 2011;286:23063–23076.
    • (2011) J Biol Chem , vol.286 , pp. 23063-23076
    • Patterson, K.R.1    Remmers, C.2    Fu, Y.3
  • 30
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai HC, Serrano-Pozo A, Hashimoto T, et al. The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am J Pathol 2012;181:1426–1435.
    • (2012) Am J Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3
  • 31
    • 84896830709 scopus 로고    scopus 로고
    • Neuronal activity regulates extracellular tau in vivo
    • Yamada K, Holth JK, Liao F, et al. Neuronal activity regulates extracellular tau in vivo. J Exp Med 2014;211:387–393.
    • (2014) J Exp Med , vol.211 , pp. 387-393
    • Yamada, K.1    Holth, J.K.2    Liao, F.3
  • 32
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B, Diamond MI. Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 2010;11:155–159.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 33
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010;11:301–307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 34
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M, Clavaguera F, Tolnay M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci 2010;33:317–325.
    • (2010) Trends Neurosci , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 35
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • Yanamandra K, Kfoury N, Jiang H, et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 2013;80:402–414.
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1    Kfoury, N.2    Jiang, H.3
  • 36
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama Y, Higuchi M, Zhang B, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 2007;53:337–351.
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3
  • 37
    • 84896269359 scopus 로고    scopus 로고
    • Passive immunization with tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles
    • Castillo-Carranza DL, Sengupta U, Guerrero-Muñoz MJ, et al. Passive immunization with tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles. J Neurosci 2014;34:4260–4272.
    • (2014) J Neurosci , vol.34 , pp. 4260-4272
    • Castillo-Carranza, D.L.1    Sengupta, U.2    Guerrero-Muñoz, M.J.3
  • 38
    • 84899962287 scopus 로고    scopus 로고
    • Neurofibrillary tangle formation by introducing wild-type human tau into APP transgenic mice
    • Umeda T, Maekawa S, Kimura T, et al. Neurofibrillary tangle formation by introducing wild-type human tau into APP transgenic mice. Acta Neuropathol 2014;127:685–698.
    • (2014) Acta Neuropathol , vol.127 , pp. 685-698
    • Umeda, T.1    Maekawa, S.2    Kimura, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.