메뉴 건너뛰기




Volumn 88, Issue 15, 2010, Pages 3399-3413

Neuron-selective toxicity of tau peptide in a cell culture model of neurodegenerative tauopathy: Essential role for aggregation in neurotoxicity

Author keywords

Alzheimer's disease; Neurodegenerative diseases; Neuronal cell death; Tau proteins; Tauopathies

Indexed keywords

PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; VALYLGLUTAMINYLISOLEUCYLVALYLLYSYLLYSINAMIDE; VALYLGLUTAMINYLISOLEUCYLVALYLPHENYLALANYLLYSINAMIDE; VALYLGLUTAMINYLVALYLVALYLTYROSYLLYSINAMIDE; VALYLGLUTAMINYLVALYLVALYLVALYLLYSINAMIDE;

EID: 78649416009     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.22485     Document Type: Article
Times cited : (23)

References (60)
  • 2
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • Alonso Adel C, Li B, Grundke-Iqbal I, Iqbal K. 2006. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc Natl Acad Sci U S A 103:8864-8869.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8864-8869
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 3
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer C, Acker CM, Kress Y, Hof PR, Duff K, Davies P. 2005. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 25:5446-5454.
    • (2005) J Neurosci , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 4
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ. 2007. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8:663-672.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn S, Mandelkow E. 2002. Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41:14885-14896.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 10
    • 42549132243 scopus 로고    scopus 로고
    • Inhibition of ATF-3 expression by B-Raf mediates the neuroprotective action of GW5074
    • Chen HM, Wang L, D'Mello SR. 2008. Inhibition of ATF-3 expression by B-Raf mediates the neuroprotective action of GW5074. J Neurochem 105:1300-1312.
    • (2008) J Neurochem , vol.105 , pp. 1300-1312
    • Chen, H.M.1    Wang, L.2    D'Mello, S.R.3
  • 13
    • 0027483920 scopus 로고
    • Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP
    • D'Mello SR, Galli C, Ciotti T, Calissano P. 1993. Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP. Proc Natl Acad Sci U S A 90:10989-10993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10989-10993
    • D'Mello, S.R.1    Galli, C.2    Ciotti, T.3    Calissano, P.4
  • 15
    • 0029790283 scopus 로고    scopus 로고
    • Neurodegenerative disorders with extensive tau pathology: a comparative study and review
    • Feany MB, Dickson DW. 1996. Neurodegenerative disorders with extensive tau pathology: a comparative study and review. Ann Neurol 40:139-148.
    • (1996) Ann Neurol , vol.40 , pp. 139-148
    • Feany, M.B.1    Dickson, D.W.2
  • 16
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. 2009. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284:12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 17
    • 0036804013 scopus 로고    scopus 로고
    • Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms
    • Futaki S. 2002. Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms. Int J Pharmacol 245:1-7.
    • (2002) Int J Pharmacol , vol.245 , pp. 1-7
    • Futaki, S.1
  • 18
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membranepermeable peptides having potential as carriers for intracellular protein delivery
    • Futaki S, Suzuki T, Ohashi W, Yagami T, Tanaka S, Ueda K, Sugiura Y. 2001. Arginine-rich peptides. An abundant source of membranepermeable peptides having potential as carriers for intracellular protein delivery. J Biol Chem 276:5836-5840.
    • (2001) J Biol Chem , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 21
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
    • Gomez-Ramos A, Diaz-Hernandez M, Rubio A, Miras-Portugal MT, Avila J. 2008. Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Mol Cell Neurosci 37:673-681.
    • (2008) Mol Cell Neurosci , vol.37 , pp. 673-681
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 23
    • 49149116213 scopus 로고    scopus 로고
    • Tau aggregates and tau pathology
    • Hernandez F, Avila J. 2008. Tau aggregates and tau pathology. J Alzheimers Dis 14:449-452.
    • (2008) J Alzheimers Dis , vol.14 , pp. 449-452
    • Hernandez, F.1    Avila, J.2
  • 24
    • 49149117491 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in tauopathic neurodegenerative diseases
    • Honson NS, Kuret J. 2008. Tau aggregation and toxicity in tauopathic neurodegenerative diseases. J Alzheimers Dis 14:417-422.
    • (2008) J Alzheimers Dis , vol.14 , pp. 417-422
    • Honson, N.S.1    Kuret, J.2
  • 25
    • 0025785076 scopus 로고
    • Identification of 3-and 4-repeat tau isoforms within the PHF in Alzheimer's disease
    • Jakes R, Novak M, Davison M, Wischik CM. 1991. Identification of 3-and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO J 10:2725-2729.
    • (1991) EMBO J , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 27
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, Hall JE, Glabe CG. 2004. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279:46363-46366.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 28
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova I, Biernat J, Wang Y, Pickhardt M, von Bergen M, Gazova Z, Mandelkow E, Mandelkow EM. 2006. Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J Biol Chem 281:1205-1214.
    • (2006) J Biol Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    von Bergen, M.5    Gazova, Z.6    Mandelkow, E.7    Mandelkow, E.M.8
  • 30
    • 0035112978 scopus 로고    scopus 로고
    • NF-kappaB is involved in the survival of cerebellar granule neurons: association of IkappaBbeta [correction of Ikappabeta] phosphorylation with cell survival
    • Koulich E, Nguyen T, Johnson K, Giardina C, D'mello S. 2001. NF-kappaB is involved in the survival of cerebellar granule neurons: association of IkappaBbeta [correction of Ikappabeta] phosphorylation with cell survival. J Neurochem 76:1188-1198.
    • (2001) J Neurochem , vol.76 , pp. 1188-1198
    • Koulich, E.1    Nguyen, T.2    Johnson, K.3    Giardina, C.4    D'mello, S.5
  • 33
    • 0942265972 scopus 로고    scopus 로고
    • Amyloid-beta-induced toxicity of primary neurons is dependent upon differentiation-associated increases in tau and cyclin-dependent kinase 5 expression
    • Liu T, Perry G, Chan HW, Verdile G, Martins RN, Smith MA, Atwood CS. 2004. Amyloid-beta-induced toxicity of primary neurons is dependent upon differentiation-associated increases in tau and cyclin-dependent kinase 5 expression. J Neurochem 88:554-563.
    • (2004) J Neurochem , vol.88 , pp. 554-563
    • Liu, T.1    Perry, G.2    Chan, H.W.3    Verdile, G.4    Martins, R.N.5    Smith, M.A.6    Atwood, C.S.7
  • 37
    • 9644273963 scopus 로고    scopus 로고
    • Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro
    • Necula M, Kuret J. 2004. Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro. J Biol Chem 279:49694-49703.
    • (2004) J Biol Chem , vol.279 , pp. 49694-49703
    • Necula, M.1    Kuret, J.2
  • 39
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M, Kabat J, Wischik CM. 1993. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J 12:365-370.
    • (1993) EMBO J , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 43
    • 0025830873 scopus 로고
    • J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential
    • Reers M, Smith TW, Chen LB. 1991. J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential. Biochemistry 30:4480-4486.
    • (1991) Biochemistry , vol.30 , pp. 4480-4486
    • Reers, M.1    Smith, T.W.2    Chen, L.B.3
  • 45
    • 33645669165 scopus 로고    scopus 로고
    • Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides
    • Rojas Quijano FA, Morrow D, Wise BM, Brancia FL, Goux WJ. 2006. Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides. Biochemistry 45:4638-4652.
    • (2006) Biochemistry , vol.45 , pp. 4638-4652
    • Rojas Quijano, F.A.1    Morrow, D.2    Wise, B.M.3    Brancia, F.L.4    Goux, W.J.5
  • 48
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A, Biernat J, von Bergen M, Mandelkow E, Mandelkow EM. 1999. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38:3549-3558.
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 49
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes
    • Singer SJ, Dewji NN. 2006. Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes. Proc Natl Acad Sci U S A 103:1546-1550.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 50
    • 0036193799 scopus 로고    scopus 로고
    • Comparative analysis of an improved thioflavin-s stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections
    • Sun A, Nguyen XV, Bing G. 2002. Comparative analysis of an improved thioflavin-s stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections. J Histochem Cytochem 50:463-472.
    • (2002) J Histochem Cytochem , vol.50 , pp. 463-472
    • Sun, A.1    Nguyen, X.V.2    Bing, G.3
  • 51
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among argininerich peptides
    • Suzuki T, Futaki S, Niwa M, Tanaka S, Ueda K, Sugiura Y. 2002. Possible existence of common internalization mechanisms among argininerich peptides. J Biol Chem 277:2437-2443.
    • (2002) J Biol Chem , vol.277 , pp. 2437-2443
    • Suzuki, T.1    Futaki, S.2    Niwa, M.3    Tanaka, S.4    Ueda, K.5    Sugiura, Y.6
  • 52
    • 49149120285 scopus 로고    scopus 로고
    • Hyperphosphorylated tau is a cause of neuronal dysfunction in tauopathy
    • Takashima A. 2008. Hyperphosphorylated tau is a cause of neuronal dysfunction in tauopathy. J Alzheimers Dis 14:371-375.
    • (2008) J Alzheimers Dis , vol.14 , pp. 371-375
    • Takashima, A.1
  • 53
    • 0037117535 scopus 로고    scopus 로고
    • Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
    • Vauthey S, Santoso S, Gong H, Watson N, Zhang S. 2002. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc Natl Acad Sci U S A 99:5355-5360.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 56
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow EM, Mandelkow E. 2001. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J Biol Chem 276:48165-48174.
    • (2001) J Biol Chem , vol.276 , pp. 48165-48174
    • von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 58
    • 34547203592 scopus 로고    scopus 로고
    • Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model
    • Wang YP, Biernat J, Pickhardt M, Mandelkow E, Mandelkow EM. 2007. Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model. Proc Natl Acad Sci U S A 104:10252-10257.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10252-10257
    • Wang, Y.P.1    Biernat, J.2    Pickhardt, M.3    Mandelkow, E.4    Mandelkow, E.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.