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Volumn 464, Issue 7292, 2010, Pages 1201-1204

Caspase activation precedes and leads to tangles

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 6; CASPASE 7;

EID: 77951540816     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08890     Document Type: Article
Times cited : (443)

References (30)
  • 1
    • 27944491109 scopus 로고    scopus 로고
    • Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L)
    • Ramsden, M. et al. Age-dependent neurofibrillary 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
  • 2
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • Gómez-Isla, T. et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann. Neurol. 41, 17-24 (1997).
    • (1997) Ann. Neurol. , vol.41 , pp. 17-24
    • Gómez-Isla, T.1
  • 3
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack, J. C., Schneider, A., Mandelkow, E. M. & Hyman, B. T. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol. 103, 26-35 (2002).
    • (2002) Acta Neuropathol. , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 4
    • 44649156233 scopus 로고    scopus 로고
    • Apoptosis in transgenic mice expressing the P301L mutated form of human tau
    • Ramalho, R. M. et al. Apoptosis in transgenic mice expressing the P301L mutated form of human tau. Mol. Med. 14, 309-317 (2008).
    • (2008) Mol. Med. , vol.14 , pp. 309-317
    • Ramalho, R.M.1
  • 5
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo, H. et al. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 165, 523-531 (2004).
    • (2004) Am. J. Pathol. , vol.165 , pp. 523-531
    • Guo, H.1
  • 6
    • 0035141757 scopus 로고    scopus 로고
    • Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease
    • Rohn, T. T. et al. Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease. Am. J. Pathol. 158, 189-198 (2001).
    • (2001) Am. J. Pathol. , vol.158 , pp. 189-198
    • Rohn, T.T.1
  • 7
    • 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
  • 8
    • 33646519920 scopus 로고    scopus 로고
    • Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • Spires, T. L. et al. Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy. Am. J. Pathol. 168, 1598-1607 (2006).
    • (2006) Am. J. Pathol. , vol.168 , pp. 1598-1607
    • Spires, T.L.1
  • 9
    • 38549120646 scopus 로고    scopus 로고
    • In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons
    • Spires-Jones, T. L. et al. In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons. J. Neurosci. 28, 862-867 (2008).
    • (2008) J. Neurosci. , vol.28 , pp. 862-867
    • Spires-Jones, T.L.1
  • 11
    • 0033857342 scopus 로고    scopus 로고
    • X-34, a fluorescent derivative of Congo red: A novel histochemical stain for Alzheimer's disease pathology
    • Styren, S. D., Hamilton, R. L., Styren, G. C. & Klunk, W. E. X-34, a fluorescent derivative of Congo red: a novel histochemical stain for Alzheimer's disease pathology. J. Histochem. Cytochem. 48, 1223-1232 (2000).
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1223-1232
    • Styren, S.D.1    Hamilton, R.L.2    Styren, G.C.3    Klunk, W.E.4
  • 12
    • 40149109154 scopus 로고    scopus 로고
    • Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy) styrylbenzene]
    • Velasco, A. et al. Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3- hydroxycarbonyl-4-hydroxy)styrylbenzene]. FEBS Lett. 582, 901-906 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 901-906
    • Velasco, A.1
  • 13
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • Rissman, R. A. et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J. Clin. Invest. 114, 121-130 (2004).
    • (2004) J. Clin. Invest. , vol.114 , pp. 121-130
    • Rissman, R.A.1
  • 14
    • 67349191008 scopus 로고    scopus 로고
    • Truncated tau at D421 is associated with neurodegeneration and tangle formation in the brain of Alzheimer transgenic models
    • Zhang, Q., Zhang, X. & Sun, A. Truncated tau at D421 is associated with neurodegeneration and tangle formation in the brain of Alzheimer transgenic models. Acta Neuropathol. 117, 687-697 (2009).
    • (2009) Acta Neuropathol. , vol.117 , pp. 687-697
    • Zhang, Q.1    Zhang, X.2    Sun, A.3
  • 15
    • 43249129441 scopus 로고    scopus 로고
    • Accumulation of aspartic acid421-and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease
    • Basurto-Islas, G. et al. Accumulation of aspartic acid421-and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease. J. Neuropathol. Exp. Neurol. 67, 470-483 (2008).
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 470-483
    • Basurto-Islas, G.1
  • 16
    • 20044381844 scopus 로고    scopus 로고
    • Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease
    • Guillozet-Bongaarts, A. L. et al. Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol. Aging 26, 1015-1022 (2005).
    • (2005) Neurobiol. Aging , vol.26 , pp. 1015-1022
    • Guillozet-Bongaarts, A.L.1
  • 17
    • 38749144389 scopus 로고    scopus 로고
    • Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy
    • Delobel, P. et al. Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy. Am. J. Pathol. 172, 123-131 (2008).
    • (2008) Am. J. Pathol. , vol.172 , pp. 123-131
    • Delobel, P.1
  • 18
    • 4544248870 scopus 로고    scopus 로고
    • Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease
    • Horowitz, P. M. et al. Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease. J. Neurosci. 24, 7895-7902 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 7895-7902
    • Horowitz, P.M.1
  • 19
    • 33646080573 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: In vitro evidence and implications for tangle formation in vivo
    • Guillozet-Bongaarts, A. L. et al. Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J. Neurochem. 97, 1005-1014 (2006).
    • (2006) J. Neurochem. , vol.97 , pp. 1005-1014
    • Guillozet-Bongaarts, A.L.1
  • 20
    • 70349705552 scopus 로고    scopus 로고
    • AAV-tau mediates pyramidal neurodegeneration by cell-cycle re-entry without neurofibrillary tangle formation in wild-type mice
    • Jaworski, T. et al. AAV-tau mediates pyramidal neurodegeneration by cell-cycle re-entry without neurofibrillary tangle formation in wild-type mice. PLoS One 4, e7280 (2009).
    • (2009) PLoS One , vol.4
    • Jaworski, T.1
  • 21
    • 0041803006 scopus 로고    scopus 로고
    • Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
    • Andorfer, C. et al. Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J. Neurochem. 86, 582-590 (2003).
    • (2003) J. Neurochem. , vol.86 , pp. 582-590
    • Andorfer, C.1
  • 22
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin, T. C. et al. Caspase cleavage of tau: linking amyloid and neurofibrillary 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
  • 23
    • 29344434456 scopus 로고    scopus 로고
    • C-terminal truncation modulates both nucleation and extension phases of tau fibrillization
    • Yin, H. & Kuret, J. C-terminal truncation modulates both nucleation and extension phases of tau fibrillization. FEBS Lett. 580, 211-215 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 211-215
    • Yin, H.1    Kuret, J.2
  • 24
    • 33745827715 scopus 로고    scopus 로고
    • Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation
    • Ding, H., Matthews, T. A. & Johnson, G. V. Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation. J. Biol. Chem. 281, 19107-19114 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 19107-19114
    • Ding, H.1    Matthews, T.A.2    Johnson, G.V.3
  • 25
    • 38549129613 scopus 로고    scopus 로고
    • The potential for b-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy
    • Mocanu, M. M. et al. The potential for b-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J. Neurosci. 28, 737-748 (2008).
    • (2008) J. Neurosci. , vol.28 , pp. 737-748
    • Mocanu, M.M.1
  • 26
    • 70349987102 scopus 로고    scopus 로고
    • Tau fragmentation, aggregation and clearance: The dual role of lysosomal processing
    • Wang, Y. et al. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum. Mol. Genet. 18, 4153-4170 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4153-4170
    • Wang, Y.1
  • 27
    • 33751557958 scopus 로고    scopus 로고
    • Caspase-3-and calpain-mediated tau cleavage are differentially prevented by estrogen and testosterone in b-amyloid-treated hippocampal neurons
    • Park, S. Y., Tournell, C., Sinjoanu, R. C. & Ferreira, A. Caspase-3-and calpain-mediated tau cleavage are differentially prevented by estrogen and testosterone in b-amyloid-treated hippocampal neurons. Neuroscience 144, 119-127 (2007).
    • (2007) Neuroscience , vol.144 , pp. 119-127
    • Park, S.Y.1    Tournell, C.2    Sinjoanu, R.C.3    Ferreira, A.4
  • 28
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M. & Bujard, H. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl Acad. Sci. USA 89, 5547-5551 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 29
    • 0029807527 scopus 로고    scopus 로고
    • Control of memory formation through regulated expression of a CaMKII transgene
    • Mayford, M. et al. Control of memory formation through regulated expression of a CaMKII transgene. Science 274, 1678-1683 (1996).
    • (1996) Science , vol.274 , pp. 1678-1683
    • Mayford, M.1


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