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Volumn 8, Issue 10, 2005, Pages 1343-1349

Targeting BACE1 with siRNAs ameliorates Alzheimer disease neuropathology in a transgenic model

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; LENTIVIRUS VECTOR; RECOMBINANT ENZYME; SMALL INTERFERING RNA;

EID: 27744588007     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1531     Document Type: Article
Times cited : (383)

References (49)
  • 1
    • 0034531478 scopus 로고    scopus 로고
    • Recent advances in the understanding of the processing of APP to beta amyloid peptide
    • Sinha, S. et al. Recent advances in the understanding of the processing of APP to beta amyloid peptide. Ann. NY Acad. Sci. 920, 206-208 (2000).
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 206-208
    • Sinha, S.1
  • 2
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • Kamenetz, F. et al. APP processing and synaptic function. Neuron 37, 925-937 (2003).
    • (2003) Neuron , vol.37 , pp. 925-937
    • Kamenetz, F.1
  • 3
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • Selkoe, D.J. & Schenk, D. Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. 43, 545-584 (2003).
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 4
    • 0036861132 scopus 로고    scopus 로고
    • Emerging Alzheimer's disease therapies: Inhibition of β-secretase
    • Citron, M. Emerging Alzheimer's disease therapies: inhibition of β-secretase. Neurobiol. Aging 23, 1017-1022 (2002).
    • (2002) Neurobiol. Aging , vol.23 , pp. 1017-1022
    • Citron, M.1
  • 5
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein beta-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 6
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases-new features and familiar faces
    • Esler, W.P. & Wolfe, M.S. A portrait of Alzheimer secretases-new features and familiar faces. Science 293, 1449-1454 (2001).
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 7
    • 0001067847 scopus 로고
    • Beta-amyloid precursor protein of Alzheimer disease occurs as 110-to 135-kilodalton membrane-associated proteins in neural and nonneural tissue
    • Selkoe, D. et al. Beta-amyloid precursor protein of Alzheimer disease occurs as 110-to 135-kilodalton membrane-associated proteins in neural and nonneural tissue. Proc. Natl. Acad. Sci. USA 85, 7341-7345 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7341-7345
    • Selkoe, D.1
  • 8
    • 0029933153 scopus 로고    scopus 로고
    • The role of APP processing and trafficking pathways in the formation of amyloid beta-protein
    • Selkoe, D.J. et al. The role of APP processing and trafficking pathways in the formation of amyloid beta-protein. Ann. NY Acad. Sci. 777, 57-64 (1996).
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 57-64
    • Selkoe, D.J.1
  • 9
    • 0035197342 scopus 로고    scopus 로고
    • Spotlight on BACE: The secretases as targets for treatment in Alzheimer disease
    • Dingwall, C. Spotlight on BACE: the secretases as targets for treatment in Alzheimer disease. J. Clin. Invest. 108, 1243-1246 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 1243-1246
    • Dingwall, C.1
  • 10
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS deficits in Presenilin-1-deficient mice
    • Shen, J. et al. Skeletal and CNS deficits in Presenilin-1-deficient mice. Cell 89, 629-639 (1997).
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1
  • 11
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: Implications for Alzheimer's disease therapeutics
    • Roberds, S.L. et al. BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum. Mol. Genet. 10, 1317-1324 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1317-1324
    • Roberds, S.L.1
  • 12
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of alzheimer's disease
    • Ohno, M. et al. BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of alzheimer's disease. Neuron 41, 27-33 (2004).
    • (2004) Neuron , vol.41 , pp. 27-33
    • Ohno, M.1
  • 13
    • 12144286502 scopus 로고    scopus 로고
    • Amyloid beta peptide load is correlated with increased beta-secretase activity in sporadic Alzheimer's disease patients
    • Li, R. et al. Amyloid beta peptide load is correlated with increased beta-secretase activity in sporadic Alzheimer's disease patients. Proc. Natl. Acad. Sci. USA 101, 3632-3637 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3632-3637
    • Li, R.1
  • 14
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease
    • Holsinger, R.M., McLean, C.A., Beyreuther, K., Masters, C.L. & Evin, G. Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease. Ann. Neurol. 51, 783-786 (2002).
    • (2002) Ann. Neurol. , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 15
    • 0036718272 scopus 로고    scopus 로고
    • Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto, H., Cheung, B.S., Hyman, B.T. & Irizarry, M.C. Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch. Neurol. 59, 1381-1389 (2002).
    • (2002) Arch. Neurol. , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 16
    • 0035159756 scopus 로고    scopus 로고
    • The beta-secretase, BACE: A prime drug target for Alzheimer's disease
    • Vassar, R. The beta-secretase, BACE: a prime drug target for Alzheimer's disease. J. Mol. Neurosci. 17, 157-170 (2001).
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 157-170
    • Vassar, R.1
  • 17
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor
    • Hong, L. et al. Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor. Science 290, 150-153 (2000).
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1
  • 18
    • 1342306385 scopus 로고    scopus 로고
    • Targeting Alzheimer's disease genes with RNA interference: An efficient strategy for silencing mutant alleles
    • Miller, V.M., Gouvion, C.M., Davidson, B.L. & Paulson, H.L. Targeting Alzheimer's disease genes with RNA interference: an efficient strategy for silencing mutant alleles. Nucleic Acids Res. 32, 661-668 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 661-668
    • Miller, V.M.1    Gouvion, C.M.2    Davidson, B.L.3    Paulson, H.L.4
  • 19
    • 0037452812 scopus 로고    scopus 로고
    • A general method for gene knockdown in mice by using lentiviral vectors expressing small interfering RNA
    • Tiscornia, G., Singer, O., Ikawa, M. & Verma, I.M. A general method for gene knockdown in mice by using lentiviral vectors expressing small interfering RNA. Proc. Natl. Acad. Sci. USA 100, 1844-1848 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1844-1848
    • Tiscornia, G.1    Singer, O.2    Ikawa, M.3    Verma, I.M.4
  • 20
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L. et al. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272, 263-267 (1996).
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1
  • 21
    • 0041701529 scopus 로고    scopus 로고
    • Gene therapy for neurological disease
    • Tuszynski, M.H. Gene therapy for neurological disease. Expert Opin. Biol. Ther. 3, 815-828 (2003).
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 815-828
    • Tuszynski, M.H.1
  • 22
    • 0037444432 scopus 로고    scopus 로고
    • Neprilysin gene transfer reduces human amyloid pathology intransgenic mice
    • Marr, R.A. et al. Neprilysin gene transfer reduces human amyloid pathology intransgenic mice. J. Neurosci. 23, 1992-1996 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 1992-1996
    • Marr, R.A.1
  • 23
    • 1242316299 scopus 로고    scopus 로고
    • Molecular medicine for the brain: Silencing of disease genes with RNA interference
    • Davidson, B.L. & Paulson, H.L. Molecular medicine for the brain: silencing of disease genes with RNA interference. Lancet Neurol. 3, 145-149 (2004).
    • (2004) Lancet Neurol. , vol.3 , pp. 145-149
    • Davidson, B.L.1    Paulson, H.L.2
  • 24
    • 0345826094 scopus 로고    scopus 로고
    • BACE1 suppression by RNA interference in primary cortical neurons
    • Kao, S.C., Krichevsky, A.M., Kosik, K.S. & Tsai, L.H. BACE1 suppression by RNA interference in primary cortical neurons. J. Biol. Chem. 279, 1942-1949 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 1942-1949
    • Kao, S.C.1    Krichevsky, A.M.2    Kosik, K.S.3    Tsai, L.H.4
  • 25
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi, R.H. et al. Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain. J. Neurosci. 24, 3592-3599 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1
  • 26
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R. et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489 (2003).
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1
  • 27
    • 20844458090 scopus 로고    scopus 로고
    • Synaptic targeting by Alzheimer's-related amyloid beta oligomers
    • Lacor, P.N. et al. Synaptic targeting by Alzheimer's-related amyloid beta oligomers. J. Neurosci. 24, 10191-10200 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 10191-10200
    • Lacor, P.N.1
  • 28
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M. et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (2002).
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 29
    • 0033898887 scopus 로고    scopus 로고
    • Carboxyl-terminal fragment of Alzheimer's APP destabilizes calcium homeostasis and renders neuronal cells vulnerable to excitotoxicity
    • Kim, H.S. et al. Carboxyl-terminal fragment of Alzheimer's APP destabilizes calcium homeostasis and renders neuronal cells vulnerable to excitotoxicity. FASEB J. 14, 1508-1517 (2000).
    • (2000) FASEB J. , vol.14 , pp. 1508-1517
    • Kim, H.S.1
  • 30
    • 0031724004 scopus 로고    scopus 로고
    • Behavioral and neuropathologic changes induced by central injection of carboxyl-terminal fragment of beta-amyloid precursor protein in mice
    • Song, D.K. et al. Behavioral and neuropathologic changes induced by central injection of carboxyl-terminal fragment of beta-amyloid precursor protein in mice. J. Neurochem. 71, 875-878 (1998).
    • (1998) J. Neurochem. , vol.71 , pp. 875-878
    • Song, D.K.1
  • 31
    • 0029862137 scopus 로고    scopus 로고
    • Age-dependent neuronal and synaptic degradation in mice transgenic for the C terminus of the amyloid procursor protein
    • Oster-Granite, M., McPhie, D., Greenan, J. & Neve, R. Age-dependent neuronal and synaptic degradation in mice transgenic for the C terminus of the amyloid procursor protein. J. Neurosci. 16, 6732-6741 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 6732-6741
    • Oster-Granite, M.1    McPhie, D.2    Greenan, J.3    Neve, R.4
  • 32
    • 0033586449 scopus 로고    scopus 로고
    • Impairments in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein
    • Berger-Sweeney, J. et al. Impairments in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein. Brain Res. Mol. Brain Res. 66, 150-162 (1999).
    • (1999) Brain Res. Mol. Brain Res. , vol.66 , pp. 150-162
    • Berger-Sweeney, J.1
  • 34
    • 4043057946 scopus 로고    scopus 로고
    • RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia
    • Xia, H. et al. RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia. Nat. Med. 10, 816-820 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 816-820
    • Xia, H.1
  • 35
    • 0037013209 scopus 로고    scopus 로고
    • Beta-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain
    • Huse, J.T. et al. Beta-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain. J. Biol. Chem. 277, 16278-16284 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 16278-16284
    • Huse, J.T.1
  • 36
    • 0035370860 scopus 로고    scopus 로고
    • Neuronal and glial beta-secretase (BACE) protein expression in transgenic Tg2576 mice with amyloid plaque pathology
    • Rossner, S., Apelt, J., Schliebs, R., Perez-Polo, J.R. & Bigl, V. Neuronal and glial beta-secretase (BACE) protein expression in transgenic Tg2576 mice with amyloid plaque pathology. J. Neurosci. Res. 64, 437-446 (2001).
    • (2001) J. Neurosci. Res. , vol.64 , pp. 437-446
    • Rossner, S.1    Apelt, J.2    Schliebs, R.3    Perez-Polo, J.R.4    Bigl, V.5
  • 37
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • Kitazume, S. et al. Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc. Natl. Acad. Sci. USA 98, 13554-13559 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13554-13559
    • Kitazume, S.1
  • 38
    • 20044374165 scopus 로고    scopus 로고
    • In vivo cleavage of alpha2,6-sialyltransferase by Alzheimer beta-secretase
    • Kitazume, S. et al. In vivo cleavage of alpha2,6-sialyltransferase by Alzheimer beta-secretase. J. Biol. Chem. 280, 8589-8595 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 8589-8595
    • Kitazume, S.1
  • 39
    • 20744454142 scopus 로고    scopus 로고
    • Beta subunits of voltage-gated sodium channels are novel substrates of BACE1 and gamma-secretase
    • Wong, H .K. et al. Beta subunits of voltage-gated sodium channels are novel substrates of BACE1 and gamma-secretase. J. Biol. Chem. 280, 23009-23017 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 23009-23017
    • Wong, H.K.1
  • 40
    • 3042658599 scopus 로고    scopus 로고
    • In vivo inhibition of Abeta production by memapsin2 (beta-secretase) inhibitors
    • Chang, W.P. et al. In vivo inhibition of Abeta production by memapsin2 (beta-secretase) inhibitors. J. Neurochem. 89, 1409-1416 (2004).
    • (2004) J. Neurochem. , vol.89 , pp. 1409-1416
    • Chang, W.P.1
  • 41
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T.R., Bernards, R. & Agami, R. A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553 (2002).
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 42
    • 0029993858 scopus 로고    scopus 로고
    • Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector
    • Naldini, L., Blomer, U., Gage, F.H., Trono, D. & Verma, I.M. Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector. Proc. Natl. Acad. Sci. USA 93, 11382-11388 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11382-11388
    • Naldini, L.1    Blomer, U.2    Gage, F.H.3    Trono, D.4    Verma, I.M.5
  • 43
    • 0034710883 scopus 로고    scopus 로고
    • Suppression of angiogenesis by lentiviral delivery of PEX, a noncatalytic fragment of matrix metalloproteinase 2
    • Pfeifer, A., Kessler, T., Silletti, S., Cheresh, D.A. & Verma, I.M. Suppression of angiogenesis by lentiviral delivery of PEX, a noncatalytic fragment of matrix metalloproteinase 2. Proc. Natl. Acad. Sci. USA 97, 12227-12232 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12227-12232
    • Pfeifer, A.1    Kessler, T.2    Silletti, S.3    Cheresh, D.A.4    Verma, I.M.5
  • 44
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke, L. et al. High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J. Neurosci. 20, 4050-4058 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1
  • 45
    • 0038796307 scopus 로고    scopus 로고
    • Aβ1-42 promotes cholinergic sprouting in patients with Alzheimer disease and Lewy body variant of Alzheimer disease
    • Masliah, E. et al. Aβ1-42 promotes cholinergic sprouting in patients with Alzheimer disease and Lewy body variant of Alzheimer disease. Neurology 61, 206-211 (2003).
    • (2003) Neurology , vol.61 , pp. 206-211
    • Masliah, E.1
  • 46
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah, E. et al. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 287, 1265-1269 (2000).
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1
  • 47
    • 25444479179 scopus 로고    scopus 로고
    • High beta-secretase activity elicits neurodegeneration in transgenic mice despite reductions in amyloid-beta levels: Implications for the treatment of Alzheimer's disease
    • published online 15 July (doi:10.1074/jbc.M507016200)
    • Rockenstein, E. et al. High beta-secretase activity elicits neurodegeneration in transgenic mice despite reductions in amyloid-beta levels: implications for the treatment of Alzheimer's disease. J. Biol. Chem., published online 15 July 2005 (doi:10.1074/jbc.M507016200).
    • (2005) J. Biol. Chem.
    • Rockenstein, E.1
  • 48
    • 0035889404 scopus 로고    scopus 로고
    • Early formation of mature amyloid-b proteins deposits in a mutant APP transgenic model depends on levels of Ab1-42
    • Rockenstein, E., Mallory, M., Mante, M., Sisk, A. & Masliah, E. Early formation of mature amyloid-b proteins deposits in a mutant APP transgenic model depends on levels of Ab1-42. J. Neurosci. Res. 66, 573-582 (2001).
    • (2001) J. Neurosci. Res. , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliah, E.5
  • 49
    • 0345059236 scopus 로고    scopus 로고
    • The neuroprotective effects of Cerebrolysin in a transgenic model of Alzheimer's disease are associated with improved behavioral performance
    • Rockenstein, E. et al. The neuroprotective effects of Cerebrolysin in a transgenic model of Alzheimer's disease are associated with improved behavioral performance. J. Neural Transm. 110, 1313-1327 (2003).
    • (2003) J. Neural Transm. , vol.110 , pp. 1313-1327
    • Rockenstein, E.1


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