메뉴 건너뛰기




Volumn 28, Issue 7, 2008, Pages 1682-1687

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice

Author keywords

Alzheimer's disease; Fast axonal transport; Neurofilament; Slow axonal transport; snap25; Tau

Indexed keywords

SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TAU PROTEIN;

EID: 39549117998     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.5242-07.2008     Document Type: Article
Times cited : (147)

References (22)
  • 1
    • 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
  • 4
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess DT, Slater TM, Wilson MC, Skene JH (1992) The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J Neurosci 12:4634-4641.
    • (1992) J Neurosci , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.4
  • 5
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa N, Takemura R (2005) Molecular motors and mechanisms of directional transport in neurons. Nat Rev Neurosci 6:201-214.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 6
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara T, Hong M, Zhang B, Nakagawa Y, Lee MK, Trojanowski JQ, Lee VM (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24:751-762.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 7
    • 0026694783 scopus 로고
    • Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein
    • Khatoon S, Grundke-Iqbal I, Iqbal K (1992) Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein. J Neurochem 59:750-753.
    • (1992) J Neurochem , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 8
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik KS, Orecchio LD, Bakalis S, Neve RL (1989) Developmentally regulated expression of specific tau sequences. Neuron 2:1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 9
    • 0023899370 scopus 로고
    • Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1
    • Ksiezak-Reding H, Binder LI, Yen SH (1988) Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. J Biol Chem 263:7948-7953.
    • (1988) J Biol Chem , vol.263 , pp. 7948-7953
    • Ksiezak-Reding, H.1    Binder, L.I.2    Yen, S.H.3
  • 10
    • 0347717732 scopus 로고    scopus 로고
    • Axonal transport of human alpha-synuclein slows with aging but is not affected by familial Parkinson's disease-linked mutations
    • Li W, Hoffman PN, Stirling W, Price DL, Lee MK (2004) Axonal transport of human alpha-synuclein slows with aging but is not affected by familial Parkinson's disease-linked mutations. J Neurochem 88:401-410.
    • (2004) J Neurochem , vol.88 , pp. 401-410
    • Li, W.1    Hoffman, P.N.2    Stirling, W.3    Price, D.L.4    Lee, M.K.5
  • 11
    • 0029588380 scopus 로고
    • Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: Evidence for dynamic interactions of tau with microtubules in vivo
    • Mercken M, Fischer I, Kosik KS, Nixon RA (1995) Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: evidence for dynamic interactions of tau with microtubules in vivo. J Neurosci 15:8259-8267.
    • (1995) J Neurosci , vol.15 , pp. 8259-8267
    • Mercken, M.1    Fischer, I.2    Kosik, K.S.3    Nixon, R.A.4
  • 12
    • 34250317264 scopus 로고    scopus 로고
    • Tau binding to microtubules does not directly affect microtubule-based vesicle motility
    • Morfini G, Pigino G, Mizuno N, Kikkawa M, Brady ST (2007) Tau binding to microtubules does not directly affect microtubule-based vesicle motility. J Neurosci Res 85:2620-2630.
    • (2007) J Neurosci Res , vol.85 , pp. 2620-2630
    • Morfini, G.1    Pigino, G.2    Mizuno, N.3    Kikkawa, M.4    Brady, S.T.5
  • 13
    • 0027931132 scopus 로고
    • Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber
    • Nixon RA, Paskevich PA, Sihag RK, Thayer CY (1994) Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber. J Cell Biol 126:1031-1046.
    • (1994) J Cell Biol , vol.126 , pp. 1031-1046
    • Nixon, R.A.1    Paskevich, P.A.2    Sihag, R.K.3    Thayer, C.Y.4
  • 15
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 156:1051-1063.
    • (2002) J Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 16
    • 0035152814 scopus 로고    scopus 로고
    • Neurotrophins are required for nerve growth during development
    • Tucker KL, Meyer M, Barde YA (2001) Neurotrophins are required for nerve growth during development. Nat Neurosci 4:29-37.
    • (2001) Nat Neurosci , vol.4 , pp. 29-37
    • Tucker, K.L.1    Meyer, M.2    Barde, Y.A.3
  • 17
    • 0036703743 scopus 로고    scopus 로고
    • The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons
    • Utton MA, Connell J, Asuni AA, van Slegtenhorst M, Hutton M, de Silva R, Lees AJ, Miller CC, Anderton BH (2002) The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons. J Neurosci 22:6394-6400.
    • (2002) J Neurosci , vol.22 , pp. 6394-6400
    • Utton, M.A.1    Connell, J.2    Asuni, A.A.3    van Slegtenhorst, M.4    Hutton, M.5    de Silva, R.6    Lees, A.J.7    Miller, C.C.8    Anderton, B.H.9
  • 18
    • 39649101596 scopus 로고    scopus 로고
    • Neurofilament protein partnership, export, transport, phosphorylation and neurodegeneration
    • Arlen R, ed, pp, New York: Nova Science
    • Yuan A (2006) Neurofilament protein partnership, export, transport, phosphorylation and neurodegeneration. In: New research on neurofilament proteins (Arlen R, ed), pp 53-79. New York: Nova Science.
    • (2006) New research on neurofilament proteins , pp. 53-79
    • Yuan, A.1
  • 19
    • 0142250822 scopus 로고    scopus 로고
    • Neurofilament transport in vivo minimally requires hetero-oligomer formation
    • Yuan A, Rao MV, Kumar A, Julien JP, Nixon RA (2003) Neurofilament transport in vivo minimally requires hetero-oligomer formation. J Neurosci 23:9452-9458.
    • (2003) J Neurosci , vol.23 , pp. 9452-9458
    • Yuan, A.1    Rao, M.V.2    Kumar, A.3    Julien, J.P.4    Nixon, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.