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Volumn 583, Issue 13, 2009, Pages 2194-2200

Excitatory amino acid transporter 2 associates with phosphorylated tau and is localized in neurofibrillary tangles of tauopathic brains

Author keywords

Alzheimer's disease; Corticobasal degeneration; EAAT2; Neurofibrillary tangle; Progressive supranuclear palsy; Tau

Indexed keywords

EXCITATORY AMINO ACID TRANSPORTER 2; GLUTAMIC ACID; TAU PROTEIN;

EID: 67649336238     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.06.015     Document Type: Article
Times cited : (21)

References (24)
  • 2
    • 0034530634 scopus 로고    scopus 로고
    • Molecular genetics of chromosome 17 tauopathies
    • Hutton M. Molecular genetics of chromosome 17 tauopathies. Ann. NY Acad. Sci. 920 (2000) 63-73
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 63-73
    • Hutton, M.1
  • 3
    • 0029569152 scopus 로고
    • Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases
    • Trojanowski J.Q., and Lee V.M. Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases. FASEB J. 9 (1995) 1570-1576
    • (1995) FASEB J. , vol.9 , pp. 1570-1576
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 4
    • 0025478743 scopus 로고
    • Tau protein and neurodegeneration
    • Kosik K.S. Tau protein and neurodegeneration. Mol. Neurobiol. 4 (1990) 171-179
    • (1990) Mol. Neurobiol. , vol.4 , pp. 171-179
    • Kosik, K.S.1
  • 5
    • 0344688272 scopus 로고    scopus 로고
    • Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg?
    • Geschwind D.H. Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg?. Neuron 40 (2003) 457-460
    • (2003) Neuron , vol.40 , pp. 457-460
    • Geschwind, D.H.1
  • 6
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • Noble W., et al. Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron 38 (2003) 555-565
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1
  • 7
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson G.R., Wiedau-Pazos M., Sang T.K., Wagle N., Brown C.A., Massachi S., and Geschwind D.H. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 34 (2002) 509-519
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 8
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H., Schwartz D., Gygi S.P., and Kosik K.S. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279 (2004) 4869-4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 9
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of phosphorylated tau and enhanced cell survival
    • Shimura H., Miura-Shimura Y., and Kosik K.S. Binding of tau to heat shock protein 27 leads to decreased concentration of phosphorylated tau and enhanced cell survival. J. Biol. Chem. 279 (2004) 17957-17962
    • (2004) J. Biol. Chem. , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 10
    • 0027274623 scopus 로고
    • Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity
    • Rothstein J.D., Jin L., Dykes-Hoberg M., and Kuncl R.W. Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity. Proc. Natl. Acad. Sci. USA 90 (1993) 6591-6595
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6591-6595
    • Rothstein, J.D.1    Jin, L.2    Dykes-Hoberg, M.3    Kuncl, R.W.4
  • 12
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg S.G., Davies P., Schein J.D., and Binder L.I. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267 (1992) 564-569
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 14
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang Q., Woltjer R.L., Cimino P.J., Pan C., Montine K.S., Zhang J., and Montine T.J. Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 19 (2005) 869-871
    • (2005) FASEB J. , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 15
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S., and Lansbury Jr. P.T. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?. Nat. Cell Biol. 2 (2000) E115-E119
    • (2000) Nat. Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 16
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 17
    • 0028961895 scopus 로고
    • Variant forms of neuronal glutamate transporter sites in Alzheimer disease cerebral cortex
    • Scott H.L., Tannenberg A.E.G., and Dodd P.R. Variant forms of neuronal glutamate transporter sites in Alzheimer disease cerebral cortex. J. Neurochem. 64 (1995) 2193-2202
    • (1995) J. Neurochem. , vol.64 , pp. 2193-2202
    • Scott, H.L.1    Tannenberg, A.E.G.2    Dodd, P.R.3
  • 18
    • 0032449129 scopus 로고    scopus 로고
    • The family of sodium-dependent glutamate transporters: a focus on the GLT-1/EAAT2 subtype
    • Robinson M.B. The family of sodium-dependent glutamate transporters: a focus on the GLT-1/EAAT2 subtype. Neurochem. Int. 33 (1999) 479-491
    • (1999) Neurochem. Int. , vol.33 , pp. 479-491
    • Robinson, M.B.1
  • 19
  • 20
    • 65249104851 scopus 로고    scopus 로고
    • Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases
    • Dong X.X., Wang Y., and Qin Z.H. Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases. Acta Pharmacol. Sin. 30 (2009) 379-387
    • (2009) Acta Pharmacol. Sin. , vol.30 , pp. 379-387
    • Dong, X.X.1    Wang, Y.2    Qin, Z.H.3
  • 21
    • 0030812843 scopus 로고    scopus 로고
    • Epilepsy and exacerbation of brain injury in mice lacking the glutamate transporter GLT-1
    • Tanaka K., et al. Epilepsy and exacerbation of brain injury in mice lacking the glutamate transporter GLT-1. Science 276 (1997) 1699-1702
    • (1997) Science , vol.276 , pp. 1699-1702
    • Tanaka, K.1
  • 22
    • 0029811226 scopus 로고    scopus 로고
    • Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease
    • Masliah E., et al. Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease. Ann. Neurol. 40 (1996) 759-766
    • (1996) Ann. Neurol. , vol.40 , pp. 759-766
    • Masliah, E.1
  • 23
    • 0036479889 scopus 로고    scopus 로고
    • Aberrant expression of the glutamate transporter excitatory amino acid transporter 1 (EAAT1) in Alzheimer's disease
    • Scott H.L., Pow D.V., Tannenberg A.E., and Dodd P.R. Aberrant expression of the glutamate transporter excitatory amino acid transporter 1 (EAAT1) in Alzheimer's disease. J. Neurosci. 22 (2002) RC206
    • (2002) J. Neurosci. , vol.22
    • Scott, H.L.1    Pow, D.V.2    Tannenberg, A.E.3    Dodd, P.R.4
  • 24
    • 0036793766 scopus 로고    scopus 로고
    • Excitatory amino acid transporter EAAT-2 in tangle-bearing neurons in Alzheimer's disease
    • Thai D.R. Excitatory amino acid transporter EAAT-2 in tangle-bearing neurons in Alzheimer's disease. Brain Pathol. 12 (2002) 405-411
    • (2002) Brain Pathol. , vol.12 , pp. 405-411
    • Thai, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.