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Volumn 117, Issue 6, 2009, Pages 699-712

Neurofibrillary and neurodegenerative pathology in APP-transgenic mice injected with AAV2-mutant TAU: Neuroprotective effects of Cerebrolysin

Author keywords

Alzheimer's; Amyloid precursor protein; Hippocampus; Kinase; Phosphorylation; Viral vector

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CEREBROLYSIN; CYCLIN DEPENDENT KINASE 5; GLYCOGEN SYNTHASE KINASE 3BETA; PARVOVIRUS VECTOR; TAU PROTEIN;

EID: 67349281559     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-009-0505-4     Document Type: Article
Times cited : (43)

References (89)
  • 2
    • 0041803006 scopus 로고    scopus 로고
    • Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
    • doi: 10.1046/j.1471-4159.2003.01879.x
    • Andorfer C, Kress Y, Espinoza M, de Silva R, Tucker KL, Barde YA, Duff K, Davies P (2003) Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J Neurochem 86:582-590. doi: 10.1046/j.1471-4159.2003.01879.x
    • (2003) J Neurochem , vol.86 , pp. 582-590
    • Andorfer, C.1    Kress, Y.2    Espinoza, M.3    de Silva, R.4    Tucker, K.L.5    Barde, Y.A.6    Duff, K.7    Davies, P.8
  • 3
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • doi: 10.1523/JNEUROSCI.2361-07.2007
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM (2007) Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci 27:9115-9129. doi: 10.1523/JNEUROSCI.2361-07.2007
    • (2007) J Neurosci , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 4
    • 0345580607 scopus 로고    scopus 로고
    • Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease
    • Brion JP, Tremp G, Octave JN (1999) Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimer's disease. Am J Pathol 154:255-270
    • (1999) Am J Pathol , vol.154 , pp. 255-270
    • Brion, J.P.1    Tremp, G.2    Octave, J.N.3
  • 5
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles
    • doi: 10.2353/ajpath.2007.061178
    • Caccamo A, Oddo S, Tran LX, LaFerla FM (2007) Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles. Am J Pathol 170:1669-1675. doi: 10.2353/ajpath.2007.061178
    • (2007) Am J Pathol , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    LaFerla, F.M.4
  • 6
    • 0038516240 scopus 로고    scopus 로고
    • Two-dimensional assessment of cytoarchitecture in the anterior cingulate cortex in major depressive disorder, bipolar disorder, and schizophrenia: Evidence for decreased neuronal somal size and increased neuronal density
    • doi: 10.1016/S0006-3223(03)00114-8
    • Chana G, Landau S, Beasley C, Everall IP, Cotter D (2003) Two-dimensional assessment of cytoarchitecture in the anterior cingulate cortex in major depressive disorder, bipolar disorder, and schizophrenia: Evidence for decreased neuronal somal size and increased neuronal density. Biol Psychiatry 53:1086-1098. doi: 10.1016/ S0006-3223(03)00114-8
    • (2003) Biol Psychiatry , vol.53 , pp. 1086-1098
    • Chana, G.1    Landau, S.2    Beasley, C.3    Everall, I.P.4    Cotter, D.5
  • 8
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding
    • doi: 10.1074/jbc.M206236200
    • Cho JH, Johnson GV (2003) Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J Biol Chem 278:187-193. doi: 10.1074/jbc.M206236200
    • (2003) J Biol Chem , vol.278 , pp. 187-193
    • Cho, J.H.1    Johnson, G.V.2
  • 9
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • Cho JH, Johnson GV (2004) Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J Neurochem 88:349-358
    • (2004) J Neurochem , vol.88 , pp. 349-358
    • Cho, J.H.1    Johnson, G.V.2
  • 11
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • doi: 10.1002/ana.410270502
    • DeKosky S, Scheff S (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity. Ann Neurol 27:457-464. doi: 10.1002/ana.410270502
    • (1990) Ann Neurol , vol.27 , pp. 457-464
    • DeKosky, S.1    Scheff, S.2
  • 13
    • 0035223911 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease: Phenotype and mechanisms of pathogenesis
    • Duff K (2001) Transgenic mouse models of Alzheimer's disease: Phenotype and mechanisms of pathogenesis. Biochem Soc Symp 67:195-202
    • (2001) Biochem Soc Symp , vol.67 , pp. 195-202
    • Duff, K.1
  • 14
    • 0034329543 scopus 로고    scopus 로고
    • Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants
    • doi: 10.1002/1097-4547(20001101)62:3<463::AID-JNR16>3.0.CO;2-7
    • Flaherty DB, Soria JP, Tomasiewicz HG, Wood JG (2000) Phosphorylation of human tau protein by microtubule-associated kinases: GSK3beta and cdk5 are key participants. J Neurosci Res 62:463-472. doi: 10.1002/ 1097-4547(20001101)62:3<463::AID-JNR16>3.0.CO;2-7
    • (2000) J Neurosci Res , vol.62 , pp. 463-472
    • Flaherty, D.B.1    Soria, J.P.2    Tomasiewicz, H.G.3    Wood, J.G.4
  • 15
    • 17044458021 scopus 로고    scopus 로고
    • Nerve growth factor and nootropic drug Cerebrolysin but not fibroblast growth factor can reduce spatial memory impairment elicited by fimbria-fornix transection: Short-term study
    • doi: 10.1016/0304-3940(95)12240-0
    • Francis-Turner L, Valouskova V (1996) Nerve growth factor and nootropic drug Cerebrolysin but not fibroblast growth factor can reduce spatial memory impairment elicited by fimbria-fornix transection: Short-term study. Neurosci Lett 202:1-4. doi: 10.1016/0304-3940(95)12240-0
    • (1996) Neurosci Lett , vol.202 , pp. 1-4
    • Francis-Turner, L.1    Valouskova, V.2
  • 16
    • 0032894227 scopus 로고    scopus 로고
    • The tauopathies: Toward an experimental animal model
    • Goedert M, Hasegawa M (1999) The tauopathies: Toward an experimental animal model. Am J Pathol 154:1-6
    • (1999) Am J Pathol , vol.154 , pp. 1-6
    • Goedert, M.1    Hasegawa, M.2
  • 18
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J, Probst A, Spillantini MG, Schafer T, Jakes R, Burki K, Goedert M (1995) Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J 14:1304-1313
    • (1995) EMBO J , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6    Goedert, M.7
  • 19
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • doi: 10.1074/jbc.M006531200
    • Gotz J, Chen F, Barmettler R, Nitsch RM (2001) Tau filament formation in transgenic mice expressing P301L tau. J Biol Chem 276:529-534. doi: 10.1074/jbc.M006531200
    • (2001) J Biol Chem , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 20
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • doi: 10.1126/science.1062097
    • Gotz J, Chen F, van Dorpe J, Nitsch RM (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293:1491-1495. doi: 10.1126/science.1062097
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 21
    • 0037031934 scopus 로고    scopus 로고
    • Fibroblast growth factor 1 regulates signaling via the GSK3β pathway: Implications for neuroprotection
    • doi: 10.1074/jbc.M202803200
    • Hashimoto M, Sagara Y, Everall IP, Mallory M, Everson A, Langford D, Masliah E (2002) Fibroblast growth factor 1 regulates signaling via the GSK3β pathway: Implications for neuroprotection. J Biol Chem 277:32985-32991. doi: 10.1074/jbc.M202803200
    • (2002) J Biol Chem , vol.277 , pp. 32985-32991
    • Hashimoto, M.1    Sagara, Y.2    Everall, I.P.3    Mallory, M.4    Everson, A.5    Langford, D.6    Masliah, E.7
  • 22
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • doi: 10.1074/jbc.272.40.25326
    • Hong M, Chen DC, Klein PS, Lee VM (1997) Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J Biol Chem 272:25326-25332. doi: 10.1074/jbc.272.40.25326
    • (1997) J Biol Chem , vol.272 , pp. 25326-25332
    • Hong, M.1    Chen, D.C.2    Klein, P.S.3    Lee, V.M.4
  • 23
    • 0034788203 scopus 로고    scopus 로고
    • Analysis of tauopathies with transgenic mice
    • doi: 10.1016/S1471-4914(01)02123-2
    • Hutton M, Lewis J, Dickson D, Yen S, McGowan E (2001) Analysis of tauopathies with transgenic mice. Trends Mol Med 7:467-470. doi: 10.1016/ S1471-4914(01)02123-2
    • (2001) Trends Mol Med , vol.7 , pp. 467-470
    • Hutton, M.1    Lewis, J.2    Dickson, D.3    Yen, S.4    McGowan, E.5
  • 24
    • 0028319095 scopus 로고
    • Alzheimer's disease is a laminar regional and neural system specific disease, not a global brain disease
    • doi: 10.1016/0197-4580(94)90031-0
    • Hyman B, Gomez-Isla T (1994) Alzheimer's disease is a laminar regional and neural system specific disease, not a global brain disease. Neurobiol Aging 15:353-354. doi: 10.1016/0197-4580(94)90031-0
    • (1994) Neurobiol Aging , vol.15 , pp. 353-354
    • Hyman, B.1    Gomez-Isla, T.2
  • 25
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman BT, Augustinack JC, Ingelsson M (2005) Transcriptional and conformational changes of the tau molecule in Alzheimer's disease. Biochim Biophys Acta 1739:150-157
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 150-157
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 27
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • doi: 10.1002/(SICI)1097-4547(19970415)48:2<128::AID-JNR5>3.0.CO;2-E
    • Jicha GA, Bowser R, Kazam IG, Davies P (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J Neurosci Res 48:128-132. doi: 10.1002/(SICI)1097-4547(19970415)48:2<128::AID-JNR5>3.0.CO;2-E
    • (1997) J Neurosci Res , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 29
    • 32944471565 scopus 로고    scopus 로고
    • Efficient neuronal gene transfer with AAV8 leads to neurotoxic levels of tau or green fluorescent proteins
    • doi: 10.1016/j.ymthe.2005.10.008
    • Klein RL, Dayton RD, Leidenheimer NJ, Jansen K, Golde TE, Zweig RM (2006) Efficient neuronal gene transfer with AAV8 leads to neurotoxic levels of tau or green fluorescent proteins. Mol Ther 13:517-527. doi: 10.1016/j.ymthe.2005.10.008
    • (2006) Mol Ther , vol.13 , pp. 517-527
    • Klein, R.L.1    Dayton, R.D.2    Leidenheimer, N.J.3    Jansen, K.4    Golde, T.E.5    Zweig, R.M.6
  • 30
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • doi: 10.1073/pnas.96.18.9989
    • Koo E, Lansbury PJ, Kelly J (1999) Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci USA 96:9989-9990. doi: 10.1073/pnas.96.18.9989
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.1    Lansbury, P.J.2    Kelly, J.3
  • 32
    • 0029917884 scopus 로고    scopus 로고
    • Regulation of tau phosphorylation in Alzheimer's disease
    • doi: 10.1111/j.1749-6632.1996.tb34408.x
    • Lee VM (1996) Regulation of tau phosphorylation in Alzheimer's disease. Ann N Y Acad Sci 777:107-113. doi: 10.1111/j.1749-6632.1996.tb34408.x
    • (1996) Ann N Y Acad Sci , vol.777 , pp. 107-113
    • Lee, V.M.1
  • 33
    • 0033231262 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies: Human disease and transgenic mouse models
    • doi: 10.1016/S0896-6273(00)81106-X
    • Lee VM, Trojanowski JQ (1999) Neurodegenerative tauopathies: Human disease and transgenic mouse models. Neuron 24:507-510. doi: 10.1016/ S0896-6273(00)81106-X
    • (1999) Neuron , vol.24 , pp. 507-510
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 34
    • 0034940160 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies
    • doi: 10.1146/annurev.neuro.24.1.1121
    • Lee VM, Goedert M, Trojanowski JQ (2001) Neurodegenerative tauopathies. Annu Rev Neurosci 24:1121-1159. doi: 10.1146/annurev.neuro.24.1.1121
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1121-1159
    • Lee, V.M.1    Goedert, M.2    Trojanowski, J.Q.3
  • 36
    • 33644849088 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta
    • doi: 10.1021/bi051635j
    • Li T, Hawkes C, Qureshi HY, Kar S, Paudel HK (2006) Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta. Biochemistry 45:3134-3145. doi: 10.1021/bi051635j
    • (2006) Biochemistry , vol.45 , pp. 3134-3145
    • Li, T.1    Hawkes, C.2    Qureshi, H.Y.3    Kar, S.4    Paudel, H.K.5
  • 37
    • 33644870413 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism
    • doi: 10.1021/bi051634r
    • Li T, Paudel HK (2006) Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism. Biochemistry 45:3125-3133. doi: 10.1021/ bi051634r
    • (2006) Biochemistry , vol.45 , pp. 3125-3133
    • Li, T.1    Paudel, H.K.2
  • 38
    • 0032915920 scopus 로고    scopus 로고
    • In vitro synaptotrophic effects of Cerebrolysin in NT2N cells
    • doi: 10.1007/s004010051012
    • Mallory M, Honer W, Hsu L, Johnson R, Masliah E (1999) In vitro synaptotrophic effects of Cerebrolysin in NT2N cells. Acta Neuropathol 97:437-446. doi: 10.1007/s004010051012
    • (1999) Acta Neuropathol , vol.97 , pp. 437-446
    • Mallory, M.1    Honer, W.2    Hsu, L.3    Johnson, R.4    Masliah, E.5
  • 39
    • 0029034870 scopus 로고
    • Tau domains, phosphorylation, and interactions with microtubules
    • doi: 10.1016/0197-4580(95)00025-A discussion 362-353
    • Mandelkow EM, Biernat J, Drewes G, Gustke N, Trinczek B, Mandelkow E (1995) Tau domains, phosphorylation, and interactions with microtubules. Neurobiol Aging 16:355-362. doi: 10.1016/0197-4580(95)00025-A discussion 362-353
    • (1995) Neurobiol Aging , vol.16 , pp. 355-362
    • Mandelkow, E.M.1    Biernat, J.2    Drewes, G.3    Gustke, N.4    Trinczek, B.5    Mandelkow, E.6
  • 41
    • 0028898888 scopus 로고
    • Mechanisms of synaptic dysfunction in Alzheimer's disease
    • Masliah E (1995) Mechanisms of synaptic dysfunction in Alzheimer's disease. Histol Histopathol 10:509-519
    • (1995) Histol Histopathol , vol.10 , pp. 509-519
    • Masliah, E.1
  • 42
    • 0032932837 scopus 로고    scopus 로고
    • Cerebrolysin ameliorates performance deficits and neuronal damage in apolipoprotein E-deficient mice
    • Masliah E, Armasolo F, Veinbergs I, Mallory M, Samuel W (1999) Cerebrolysin ameliorates performance deficits and neuronal damage in apolipoprotein E-deficient mice. Pharmacol Biochem Behav 62:239-245
    • (1999) Pharmacol Biochem Behav , vol.62 , pp. 239-245
    • Masliah, E.1    Armasolo, F.2    Veinbergs, I.3    Mallory, M.4    Samuel, W.5
  • 43
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • doi: 10.1126/science.287.5456.1265
    • Masliah E, Rockenstein E, Veinbergs I, Mallory M, Hashimoto M, Takeda A, Sagara Y, Sisk A, Mucke L (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 287:1265-1269. doi: 10.1126/science.287.5456.1265
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 44
    • 21244490473 scopus 로고    scopus 로고
    • Adeno-associated virus (AAV) vectors in the CNS
    • doi: 10.2174/1566523054064995
    • McCown TJ (2005) Adeno-associated virus (AAV) vectors in the CNS. Curr Gene Ther 5:333-338. doi: 10.2174/1566523054064995
    • (2005) Curr Gene Ther , vol.5 , pp. 333-338
    • McCown, T.J.1
  • 45
    • 33846054445 scopus 로고    scopus 로고
    • The role of tau phosphorylation in the pathogenesis of Alzheimer's disease
    • doi: 10.2174/156720506779025279
    • Mi K, Johnson GV (2006) The role of tau phosphorylation in the pathogenesis of Alzheimer's disease. Curr Alzheimer Res 3:449-463. doi: 10.2174/156720506779025279
    • (2006) Curr Alzheimer Res , vol.3 , pp. 449-463
    • Mi, K.1    Johnson, G.V.2
  • 46
    • 0032502829 scopus 로고    scopus 로고
    • Characterization of tau phosphorylation in glycogen synthase kinase-3beta and cyclin dependent kinase-5 activator (p23) transfected cells
    • Michel G, Mercken M, Murayama M, Noguchi K, Ishiguro K, Imahori K, Takashima A (1998) Characterization of tau phosphorylation in glycogen synthase kinase-3beta and cyclin dependent kinase-5 activator (p23) transfected cells. Biochim Biophys Acta 1380:177-182
    • (1998) Biochim Biophys Acta , vol.1380 , pp. 177-182
    • Michel, G.1    Mercken, M.2    Murayama, M.3    Noguchi, K.4    Ishiguro, K.5    Imahori, K.6    Takashima, A.7
  • 49
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction
    • doi: 10.1016/S0896-6273(03)00434-3
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, Metherate R, Mattson MP, Akbari Y, LaFerla FM (2003) Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction. Neuron 39:409-421. doi: 10.1016/ S0896-6273(03)00434-3
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 50
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • doi: 10.1016/j.neuron.2004.07.003
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM (2004) Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43:321-332. doi: 10.1016/j.neuron.2004.07.003
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 51
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • doi: 10.1074/jbc.M608485200
    • Oddo S, Vasilevko V, Caccamo A, Kitazawa M, Cribbs DH, LaFerla FM (2006) Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem 281:39413-39423. doi: 10.1074/jbc.M608485200
    • (2006) J Biol Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 53
    • 0034212887 scopus 로고    scopus 로고
    • Adeno-associated virus vectors: Activity and applications in the CNS
    • doi: 10.1016/S0165-0270(00)00183-7
    • Peel AL, Klein RL (2000) Adeno-associated virus vectors: Activity and applications in the CNS. J Neurosci Methods 98:95-104. doi: 10.1016/ S0165-0270(00)00183-7
    • (2000) J Neurosci Methods , vol.98 , pp. 95-104
    • Peel, A.L.1    Klein, R.L.2
  • 54
    • 0242720372 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model
    • Perez M, Hernandez F, Lim F, Diaz-Nido J, Avila J (2003) Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J Alzheimers Dis 5:301-308
    • (2003) J Alzheimers Dis , vol.5 , pp. 301-308
    • Perez, M.1    Hernandez, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 55
    • 12344306018 scopus 로고    scopus 로고
    • Characterization of a double (amyloid precursor protein-tau) transgenic: Tau phosphorylation and aggregation
    • doi: 10.1016/j.neuroscience.2004.09.029
    • Perez M, Ribe E, Rubio A, Lim F, Moran MA, Ramos PG, Ferrer I, Isla MT, Avila J (2005) Characterization of a double (amyloid precursor protein-tau) transgenic: Tau phosphorylation and aggregation. Neuroscience 130:339-347. doi: 10.1016/j.neuroscience.2004.09.029
    • (2005) Neuroscience , vol.130 , pp. 339-347
    • Perez, M.1    Ribe, E.2    Rubio, A.3    Lim, F.4    Moran, M.A.5    Ramos, P.G.6    Ferrer, I.7    Isla, M.T.8    Avila, J.9
  • 57
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta
    • doi: 10.1046/j.1471-4159.2000.0741587.x
    • Reynolds CH, Betts JC, Blackstock WP, Nebreda AR, Anderton BH (2000) Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. J Neurochem 74:1587-1595. doi: 10.1046/ j.1471-4159.2000.0741587.x
    • (2000) J Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Anderton, B.H.5
  • 58
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • doi: 10.1126/science.1141736
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T, Gerstein H, Yu GQ, Mucke L (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316:750-754. doi: 10.1126/science.1141736
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.Q.8    Mucke, L.9
  • 59
    • 0028875687 scopus 로고
    • Levels and alternative splicing of amyloid β protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer's disease
    • doi: 10.1074/jbc.270.47.28257
    • Rockenstein E, McConlogue L, Tan H, Power M, Masliah E, Mucke L (1995) Levels and alternative splicing of amyloid β protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer's disease. J Biol Chem 270:28257-28267. doi: 10.1074/ jbc.270.47.28257
    • (1995) J Biol Chem , vol.270 , pp. 28257-28267
    • Rockenstein, E.1    McConlogue, L.2    Tan, H.3    Power, M.4    Masliah, E.5    Mucke, L.6
  • 60
    • 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
    • doi: 10.1002/jnr.1247
    • Rockenstein E, Mallory M, Mante M, Sisk A, Masliah E (2001) 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. doi: 10.1002/jnr.1247
    • (2001) J Neurosci Res , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliah, E.5
  • 62
    • 0345059236 scopus 로고    scopus 로고
    • The neuroprotective effects of Cerebrolysin trade mark in a transgenic model of Alzheimer's disease are associated with improved behavioral performance
    • doi: 10.1007/s00702-003-0025-7
    • Rockenstein E, Adame A, Mante M, Moessler H, Windisch M, Masliah E (2003) The neuroprotective effects of Cerebrolysin trade mark in a transgenic model of Alzheimer's disease are associated with improved behavioral performance. J Neural Transm 110:1313-1327. doi: 10.1007/ s00702-003-0025-7
    • (2003) J Neural Transm , vol.110 , pp. 1313-1327
    • Rockenstein, E.1    Adame, A.2    Mante, M.3    Moessler, H.4    Windisch, M.5    Masliah, E.6
  • 63
    • 13144258773 scopus 로고    scopus 로고
    • Amelioration of the cerebrovascular amyloidosis in a transgenic model of Alzheimer's disease with the neurotrophic compound cerebrolysin
    • doi: 10.1007/s00702-004-0181-4
    • Rockenstein E, Adame A, Mante M, Larrea G, Crews L, Windisch M, Moessler H, Masliah E (2005) Amelioration of the cerebrovascular amyloidosis in a transgenic model of Alzheimer's disease with the neurotrophic compound cerebrolysin. J Neural Transm 112:269-282. doi: 10.1007/s00702-004-0181-4
    • (2005) J Neural Transm , vol.112 , pp. 269-282
    • Rockenstein, E.1    Adame, A.2    Mante, M.3    Larrea, G.4    Crews, L.5    Windisch, M.6    Moessler, H.7    Masliah, E.8
  • 64
    • 33646364811 scopus 로고    scopus 로고
    • Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease
    • Rockenstein E, Torrance M, Mante M, Adame A, Paulino A, Rose JB, Crews L, Moessler H, Masliah E (2006) Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease. J Neurosci Res 83(7):1252-1261
    • (2006) J Neurosci Res , vol.83 , Issue.7 , pp. 1252-1261
    • Rockenstein, E.1    Torrance, M.2    Mante, M.3    Adame, A.4    Paulino, A.5    Rose, J.B.6    Crews, L.7    Moessler, H.8    Masliah, E.9
  • 65
    • 33646364811 scopus 로고    scopus 로고
    • Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease
    • doi: 10.1002/jnr.20818
    • Rockenstein E, Torrance M, Mante M, Adame A, Paulino A, Rose JB, Crews L, Moessler H, Masliah E (2006) Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease. J Neurosci Res 83:1252-1261. doi: 10.1002/jnr.20818
    • (2006) J Neurosci Res , vol.83 , pp. 1252-1261
    • Rockenstein, E.1    Torrance, M.2    Mante, M.3    Adame, A.4    Paulino, A.5    Rose, J.B.6    Crews, L.7    Moessler, H.8    Masliah, E.9
  • 66
    • 33947389569 scopus 로고    scopus 로고
    • Effects of Cerebrolysin trade mark on neurogenesis in an APP transgenic model of Alzheimer's disease
    • doi: 10.1007/s00401-006-0166-5
    • Rockenstein E, Mante M, Adame A, Crews L, Moessler H, Masliah E (2007) Effects of Cerebrolysin trade mark on neurogenesis in an APP transgenic model of Alzheimer's disease. Acta Neuropathol 113:265-275. doi: 10.1007/ s00401-006-0166-5
    • (2007) Acta Neuropathol , vol.113 , pp. 265-275
    • Rockenstein, E.1    Mante, M.2    Adame, A.3    Crews, L.4    Moessler, H.5    Masliah, E.6
  • 67
    • 33847214486 scopus 로고    scopus 로고
    • Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation
    • doi: 10.1523/JNEUROSCI.4321-06.2007
    • Rockenstein E, Torrance M, Adame A, Mante M, Bar-on P, Rose JB, Crews L, Masliah E (2007) Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation. J Neurosci 27:1981-1991. doi: 10.1523/ JNEUROSCI.4321-06.2007
    • (2007) J Neurosci , vol.27 , pp. 1981-1991
    • Rockenstein, E.1    Torrance, M.2    Adame, A.3    Mante, M.4    Bar-on, P.5    Rose, J.B.6    Crews, L.7    Masliah, E.8
  • 69
    • 0028217297 scopus 로고
    • Efficacy of the peptidergic nootropic drug cerebrolysin in patients with senile dementia of the Alzheimer's type (SDAT)
    • doi: 10.1055/s-2007-1014271
    • Ruther E, Ritter R, Apecechea M, Freytag S, Windisch M (1994) Efficacy of the peptidergic nootropic drug cerebrolysin in patients with senile dementia of the Alzheimer's type (SDAT). Pharmacopsychiatry 27:32-40. doi: 10.1055/s-2007-1014271
    • (1994) Pharmacopsychiatry , vol.27 , pp. 32-40
    • Ruther, E.1    Ritter, R.2    Apecechea, M.3    Freytag, S.4    Windisch, M.5
  • 70
    • 0344926464 scopus 로고    scopus 로고
    • Divergent roles of GSK3 and CDK5 in APP processing
    • doi: 10.1016/j.bbrc.2003.11.014
    • Ryder J, Su Y, Liu F, Li B, Zhou Y, Ni B (2003) Divergent roles of GSK3 and CDK5 in APP processing. Biochem Biophys Res Commun 312:922-929. doi: 10.1016/j.bbrc.2003.11.014
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 922-929
    • Ryder, J.1    Su, Y.2    Liu, F.3    Li, B.4    Zhou, Y.5    Ni, B.6
  • 72
    • 36048983139 scopus 로고    scopus 로고
    • Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation
    • doi: 10.1038/sj.bjp.0707471
    • Selenica ML, Jensen HS, Larsen AK, Pedersen ML, Helboe L, Leist M, Lotharius J (2007) Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation. Br J Pharmacol 152:959-979. doi: 10.1038/sj.bjp.0707471
    • (2007) Br J Pharmacol , vol.152 , pp. 959-979
    • Selenica, M.L.1    Jensen, H.S.2    Larsen, A.K.3    Pedersen, M.L.4    Helboe, L.5    Leist, M.6    Lotharius, J.7
  • 73
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • doi: 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe DJ, Schenk D (2003) Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol 43:545-584. doi: 10.1146/annurev.pharmtox.43.100901.140248
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 74
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior
    • doi: 10.1016/j.bbr.2008.02.016
    • Selkoe DJ (2008) Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior. Behav Brain Res 192:106-113. doi: 10.1016/j.bbr.2008.02.016
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 75
    • 54249156984 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies
    • Sigurdsson EM (2008) Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies. J Alzheimers Dis 15:157-168
    • (2008) J Alzheimers Dis , vol.15 , pp. 157-168
    • Sigurdsson, E.M.1
  • 77
    • 37049030172 scopus 로고    scopus 로고
    • Novel strategies for Alzheimer's disease treatment
    • doi: 10.1517/14712598.7.12.1853
    • Spencer B, Rockenstein E, Crews L, Marr R, Masliah E (2007) Novel strategies for Alzheimer's disease treatment. Expert Opin Biol Ther 7:1853-1867. doi: 10.1517/14712598.7.12.1853
    • (2007) Expert Opin Biol Ther , vol.7 , pp. 1853-1867
    • Spencer, B.1    Rockenstein, E.2    Crews, L.3    Marr, R.4    Masliah, E.5
  • 78
    • 0032717803 scopus 로고    scopus 로고
    • Lithium inhibits neurite growth and tau protein kinase I/glycogen synthase kinase-3beta-dependent phosphorylation of juvenile tau in cultured hippocampal neurons
    • Takahashi M, Yasutake K, Tomizawa K (1999) Lithium inhibits neurite growth and tau protein kinase I/glycogen synthase kinase-3beta-dependent phosphorylation of juvenile tau in cultured hippocampal neurons. J Neurochem 73:2073-2083
    • (1999) J Neurochem , vol.73 , pp. 2073-2083
    • Takahashi, M.1    Yasutake, K.2    Tomizawa, K.3
  • 79
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • Takashima A (2006) GSK-3 is essential in the pathogenesis of Alzheimer's disease. J Alzheimers Dis 9:309-317
    • (2006) J Alzheimers Dis , vol.9 , pp. 309-317
    • Takashima, A.1
  • 80
    • 0037362773 scopus 로고    scopus 로고
    • The dentate gyrus neurogenesis: A therapeutic target for Alzheimer's disease
    • Tatebayashi Y, Lee MH, Li L, Iqbal K, Grundke-Iqbal I (2003) The dentate gyrus neurogenesis: A therapeutic target for Alzheimer's disease. Acta Neuropathol 105:225-232
    • (2003) Acta Neuropathol , vol.105 , pp. 225-232
    • Tatebayashi, Y.1    Lee, M.H.2    Li, L.3    Iqbal, K.4    Grundke-Iqbal, I.5
  • 81
    • 0000354585 scopus 로고
    • Structural basis of the cognitive alterations in Alzheimer disease
    • In: Terry R, Katzman R (eds) Raven Press, New York
    • Terry R, Hansen L, Masliah E (1994) Structural basis of the cognitive alterations in Alzheimer disease. In: Terry R, Katzman R (eds) Alzheimer disease. Raven Press, New York, pp 179-196
    • (1994) Alzheimer Disease , pp. 179-196
    • Terry, R.1    Hansen, L.2    Masliah, E.3
  • 82
    • 0027479150 scopus 로고
    • Altered Tau and neurofilament proteins in neurodegenerative diseases: Diagnostic implications for Alzheimer's disease and Lewy body dementias
    • doi: 10.1111/j.1750-3639.1993.tb00725.x
    • Trojanowski J, Schmidt M, Shin R-W, Bramblett G, Rao D, Lee V-Y (1993) Altered Tau and neurofilament proteins in neurodegenerative diseases: diagnostic implications for Alzheimer's disease and Lewy body dementias. Brain Pathol 3:45-54. doi: 10.1111/j.1750-3639.1993.tb00725.x
    • (1993) Brain Pathol , vol.3 , pp. 45-54
    • Trojanowski, J.1    Schmidt, M.2    Shin, R.-W.3    Bramblett, G.4    Rao, D.5    Lee, V.-Y.6
  • 83
    • 0028644131 scopus 로고
    • Phosphorylation of neuronal cytoskeletal proteins in Alzheimer's disease and Lewy body dementias
    • Trojanowski JQ, Lee VM (1994) Phosphorylation of neuronal cytoskeletal proteins in Alzheimer's disease and Lewy body dementias. Ann N Y Acad Sci 747:92-109
    • (1994) Ann N Y Acad Sci , vol.747 , pp. 92-109
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 84
    • 0033624431 scopus 로고    scopus 로고
    • Neurotrophic effects of Cerebrolysin in animal models of excitotoxicity
    • Veinbergs I, Mante M, Mallory M, Masliah E (2000) Neurotrophic effects of Cerebrolysin in animal models of excitotoxicity. J Neural Transm Suppl 59:273-280
    • (2000) J Neural Transm Suppl , vol.59 , pp. 273-280
    • Veinbergs, I.1    Mante, M.2    Mallory, M.3    Masliah, E.4
  • 85
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • doi: 10.1111/j.1471-4159.2006.04426.x
    • Walsh DM, Selkoe DJ (2007) A beta oligomers - a decade of discovery. J Neurochem 101:1172-1184. doi: 10.1111/j.1471-4159.2006.04426.x
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 86
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • doi: 10.1016/S0197-4580(00)00157-3
    • Weaver CL, Espinoza M, Kress Y, Davies P (2000) Conformational change as one of the earliest alterations of tau in Alzheimer's disease. Neurobiol Aging 21:719-727. doi: 10.1016/S0197-4580(00)00157-3
    • (2000) Neurobiol Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 87
    • 34247492801 scopus 로고    scopus 로고
    • Meta-analysis: The efficacy of nootropic agent Cerebrolysin in the treatment of Alzheimer's disease
    • doi: 10.1007/s00702-007-0630-y
    • Wei ZH, He QB, Wang H, Su BH, Chen HZ (2007) Meta-analysis: The efficacy of nootropic agent Cerebrolysin in the treatment of Alzheimer's disease. J Neural Transm 114:629-634. doi: 10.1007/s00702-007-0630-y
    • (2007) J Neural Transm , vol.114 , pp. 629-634
    • Wei, Z.H.1    He, Q.B.2    Wang, H.3    Su, B.H.4    Chen, H.Z.5
  • 89
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Woods YL, Cohen P, Becker W, Jakes R, Goedert M, Wang X, Proud CG (2001) The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem J 355:609-615
    • (2001) Biochem J , vol.355 , pp. 609-615
    • Woods, Y.L.1    Cohen, P.2    Becker, W.3    Jakes, R.4    Goedert, M.5    Wang, X.6    Proud, C.G.7


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