메뉴 건너뛰기




Volumn 22, Issue 11, 2016, Pages 1268-1276

Caspase-2 cleavage of tau reversibly impairs memory

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; CASPASE 10; CASPASE 2; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; GLUTAMATE RECEPTOR; INTERLEUKIN 1BETA CONVERTING ENZYME; MESSENGER RNA; POSTSYNAPTIC DENSITY PROTEIN 95; TAU PROTEIN; CASP2 PROTEIN, MOUSE; CASPASE; MAPT PROTEIN, HUMAN; MORPHOLINO OLIGONUCLEOTIDE;

EID: 84990966921     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.4199     Document Type: Article
Times cited : (143)

References (43)
  • 1
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini, M.G. & Goedert, M. Tau pathology and neurodegeneration. Lancet Neurol. 12, 609-622 (2013).
    • (2013) Lancet Neurol. , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 2
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V.M. & Trojanowski, J.Q. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat. Rev. Neurosci. 8, 663-672 (2007).
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 3
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-β toxicity in Alzheimer's disease mouse models
    • Ittner, L.M. et al. Dendritic function of tau mediates amyloid-β toxicity in Alzheimer's disease mouse models. Cell 142, 387-397 (2010).
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1
  • 4
    • 84896830709 scopus 로고    scopus 로고
    • Neuronal activity regulates extracellular tau in vivo
    • Yamada, K. et al. Neuronal activity regulates extracellular tau in vivo. J. Exp. Med. 211, 387-393 (2014).
    • (2014) J. Exp. Med. , vol.211 , pp. 387-393
    • Yamada, K.1
  • 5
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit, R., Ross, J.L., Goldman, Y.E. & Holzbaur, E.L. Differential regulation of dynein and kinesin motor proteins by tau. Science 319, 1086-1089 (2008).
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 6
    • 0037111833 scopus 로고    scopus 로고
    • Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease
    • Fath, T., Eidenmüller, J. & Brandt, R. Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease. J. Neurosci. 22, 9733-9741 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 9733-9741
    • Fath, T.1    Eidenmüller, J.2    Brandt, R.3
  • 7
    • 77951540816 scopus 로고    scopus 로고
    • Caspase activation precedes and leads to tangles
    • de Calignon, A. et al. Caspase activation precedes and leads to tangles. Nature 464, 1201-1204 (2010).
    • (2010) Nature , vol.464 , pp. 1201-1204
    • De Calignon, A.1
  • 8
    • 0030050286 scopus 로고    scopus 로고
    • Clinical and pathological correlates of apolipoprotein E-ϵ4 in Alzheimer's disease
    • Gomez-Isla, T. et al. Clinical and pathological correlates of apolipoprotein E-ϵ4 in Alzheimer's disease. Ann. Neurol. 39, 62-70 (1996).
    • (1996) Ann. Neurol. , vol.39 , pp. 62-70
    • Gomez-Isla, T.1
  • 9
    • 77952554382 scopus 로고    scopus 로고
    • Structural and functional changes in tau-mutant mice neurons are not linked to the presence of NFTs
    • Rocher, A.B. et al. Structural and functional changes in tau-mutant mice neurons are not linked to the presence of NFTs. Exp. Neurol. 223, 385-393 (2010).
    • (2010) Exp. Neurol. , vol.223 , pp. 385-393
    • Rocher, A.B.1
  • 10
    • 84924284937 scopus 로고    scopus 로고
    • Pathological tau disrupts ongoing network activity
    • Menkes-Caspi, N. et al. Pathological tau disrupts ongoing network activity. Neuron 85, 959-966 (2015).
    • (2015) Neuron , vol.85 , pp. 959-966
    • Menkes-Caspi, N.1
  • 11
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1
  • 12
    • 27944491109 scopus 로고    scopus 로고
    • Age-dependent neurofbrillary tangle formation, neuron loss and memory impairment in a mouse model of human tauopathy (P301L)
    • Ramsden, M. et al. Age-dependent neurofbrillary tangle formation, neuron loss and memory impairment in a mouse model of human tauopathy (P301L). J. Neurosci. 25, 10637-10647 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 10637-10647
    • Ramsden, M.1
  • 13
    • 84874201513 scopus 로고    scopus 로고
    • Synaptic alterations in the rTg4510 mouse model of tauopathy
    • Kopeikina, K.J. et al. Synaptic alterations in the rTg4510 mouse model of tauopathy. J. Comp. Neurol. 521, 1334-1353 (2013).
    • (2013) J. Comp. Neurol. , vol.521 , pp. 1334-1353
    • Kopeikina, K.J.1
  • 14
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N.D., Waller, M., Barrett, A.J. & Bateman, A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 42, D503-D509 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 15
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover, B.R. et al. Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 68, 1067-1081 (2010).
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1
  • 16
    • 77956587739 scopus 로고    scopus 로고
    • 2+ elevation, missorting of endogenous tau into dendrites, tau phosphorylation and destruction of microtubules and spines
    • 2+ elevation, missorting of endogenous tau into dendrites, tau phosphorylation and destruction of microtubules and spines. J. Neurosci. 30, 11938-11950 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3
  • 17
    • 84898719221 scopus 로고    scopus 로고
    • Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer-induced AMPA glutamate receptor signaling defcits
    • Miller, E.C. et al. Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer-induced AMPA glutamate receptor signaling defcits. Eur. J. Neurosci. 39, 1214-1224 (2014).
    • (2014) Eur. J. Neurosci. , vol.39 , pp. 1214-1224
    • Miller, E.C.1
  • 18
    • 0033928035 scopus 로고    scopus 로고
    • The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis
    • Fasulo, L. et al. The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis. J. Neurochem. 75, 624-633 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 624-633
    • Fasulo, L.1
  • 20
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-defcient mice
    • Bergeron, L. et al. Defects in regulation of apoptosis in caspase-2-defcient mice. Genes Dev. 12, 1304-1314 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1304-1314
    • Bergeron, L.1
  • 21
    • 0029162513 scopus 로고
    • Evidence for silent synapses: Implications for the expression of LTP
    • Isaac, J.T., Nicoll, R.A. & Malenka, R.C. Evidence for silent synapses: implications for the expression of LTP. Neuron 15, 427-434 (1995).
    • (1995) Neuron , vol.15 , pp. 427-434
    • Isaac, J.T.1    Nicoll, R.A.2    Malenka, R.C.3
  • 22
    • 0029018512 scopus 로고
    • Activation of postsynaptically silent synapses during pairing-induced LTP in CA1 region of hippocampal slice
    • Liao, D., Hessler, N.A. & Malinow, R. Activation of postsynaptically silent synapses during pairing-induced LTP in CA1 region of hippocampal slice. Nature 375, 400-404 (1995).
    • (1995) Nature , vol.375 , pp. 400-404
    • Liao, D.1    Hessler, N.A.2    Malinow, R.3
  • 24
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme
    • Kumar, S., Kinoshita, M., Noda, M., Copeland, N.G. & Jenkins, N.A. Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme. Genes Dev. 8, 1613-1626 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 25
    • 84903649554 scopus 로고    scopus 로고
    • A non-apoptotic role for CASP2/caspase-2: Modulation of autophagy
    • Tiwari, M. et al. A non-apoptotic role for CASP2/caspase-2: modulation of autophagy. Autophagy 10, 1054-1070 (2014).
    • (2014) Autophagy , vol.10 , pp. 1054-1070
    • Tiwari, M.1
  • 26
    • 84941875597 scopus 로고    scopus 로고
    • Caspase-2 protects against oxidative stress in vivo
    • Shalini, S. et al. Caspase-2 protects against oxidative stress in vivo. Oncogene 34, 4995-5002 (2015).
    • (2015) Oncogene , vol.34 , pp. 4995-5002
    • Shalini, S.1
  • 27
    • 84868525253 scopus 로고    scopus 로고
    • IRE-1α cleaves select microRNAs during ER stress to de-repress translation of pro-apoptotic caspase-2
    • Upton, J.P. et al. IRE-1α cleaves select microRNAs during ER stress to de-repress translation of pro-apoptotic caspase-2. Science 338, 818-822 (2012).
    • (2012) Science , vol.338 , pp. 818-822
    • Upton, J.P.1
  • 28
    • 84891591874 scopus 로고    scopus 로고
    • Caspase-2 is required for dendritic spine and behavioral alterations in J20 APP transgenic mice
    • Pozueta, J. et al. Caspase-2 is required for dendritic spine and behavioral alterations in J20 APP transgenic mice. Nat. Commun. 4, 1939 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1939
    • Pozueta, J.1
  • 29
    • 80051788879 scopus 로고    scopus 로고
    • Mice lacking caspase-2 are protected from behavioral changes, but not pathology, in the YAC128 model of Huntington disease
    • Carroll, J.B. et al. Mice lacking caspase-2 are protected from behavioral changes, but not pathology, in the YAC128 model of Huntington disease. Mol. Neurodegener. 6, 59 (2011).
    • (2011) Mol. Neurodegener. , vol.6 , pp. 59
    • Carroll, J.B.1
  • 30
    • 84867028061 scopus 로고    scopus 로고
    • Caspase-mediated truncation of tau potentiates aggregation
    • Lee, S. & Shea, T.B. Caspase-mediated truncation of tau potentiates aggregation. Int. J. Alzheimers Dis. 2012, 731063 (2012).
    • (2012) Int. J. Alzheimers Dis. , vol.2012 , pp. 731063
    • Lee, S.1    Shea, T.B.2
  • 32
    • 77954571538 scopus 로고    scopus 로고
    • A caspase-cleaved form of tau is preferentially degraded through the autophagy pathway
    • Dolan, P.J. & Johnson, G.V. A caspase-cleaved form of tau is preferentially degraded through the autophagy pathway. J. Biol. Chem. 285, 21978-21987 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 21978-21987
    • Dolan, P.J.1    Johnson, G.V.2
  • 33
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofbrillary tangles in Alzheimer's disease
    • Gamblin, T.C. et al. Caspase cleavage of tau: linking amyloid and neurofbrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 100, 10032-10037 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1
  • 35
    • 84910669129 scopus 로고    scopus 로고
    • Cleavage of tau by asparagine endopeptidase mediates the neurofbrillary pathology in Alzheimer's disease
    • Zhang, Z. et al. Cleavage of tau by asparagine endopeptidase mediates the neurofbrillary pathology in Alzheimer's disease. Nat. Med. 20, 1254-1262 (2014).
    • (2014) Nat. Med. , vol.20 , pp. 1254-1262
    • Zhang, Z.1
  • 36
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha, A. et al. C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J. Cell Sci. 113, 3737-3745 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3737-3745
    • Abraha, A.1
  • 37
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama, Y. et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 53, 337-351 (2007).
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1
  • 38
    • 77049125847 scopus 로고    scopus 로고
    • Characterization and use of monoclonal antibodies to tau and paired-helical-flament tau
    • Davies, P. Characterization and use of monoclonal antibodies to tau and paired-helical-flament tau. Methods Mol. Med. 32, 361-373 (2000).
    • (2000) Methods Mol. Med. , vol.32 , pp. 361-373
    • Davies, P.1
  • 39
    • 84904462403 scopus 로고    scopus 로고
    • Effect size of memory defcits in mice with adult-onset P301L tau expression
    • Hunsberger, H.C. et al. Effect size of memory defcits in mice with adult-onset P301L tau expression. Behav. Brain Res. 272, 181-195 (2014).
    • (2014) Behav. Brain Res. , vol.272 , pp. 181-195
    • Hunsberger, H.C.1
  • 40
    • 0036489445 scopus 로고    scopus 로고
    • The relationship between Aβ and memory in the Tg2576 mouse model of Alzheimer's disease
    • Westerman, M.A. et al. The relationship between Aβ and memory in the Tg2576 mouse model of Alzheimer's disease. J. Neurosci. 22, 1858-1867 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 1858-1867
    • Westerman, M.A.1
  • 41
    • 0034828019 scopus 로고    scopus 로고
    • Extended analysis of path data from mutant mice using the public domain software Wintrack
    • Wolfer, D.P., Madani, R., Valenti, P. & Lipp, H.P. Extended analysis of path data from mutant mice using the public domain software Wintrack. Physiol. Behav. 73, 745-753 (2001).
    • (2001) Physiol. Behav. , vol.73 , pp. 745-753
    • Wolfer, D.P.1    Madani, R.2    Valenti, P.3    Lipp, H.P.4
  • 42
    • 33645038471 scopus 로고    scopus 로고
    • A specifc amyloid-β protein assembly in the brain impairs memory
    • Lesné, S. et al. A specifc amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1
  • 43
    • 84877254679 scopus 로고    scopus 로고
    • Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome
    • Wang, X. et al. Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome. Nat. Med. 19, 473-480 (2013).
    • (2013) Nat. Med. , vol.19 , pp. 473-480
    • Wang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.