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Volumn 211, Issue 4, 2015, Pages 897-911

TDP-43 is intercellularly transmitted across axon terminals

Author keywords

[No Author keywords available]

Indexed keywords

TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; TDP-43 PROTEIN, HUMAN;

EID: 84970952328     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201504057     Document Type: Article
Times cited : (241)

References (48)
  • 1
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H., and E. Braak. 1991. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82:239-259. http://dx.doi.org/10.1007/BF00308809
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 2
  • 6
    • 84857768992 scopus 로고    scopus 로고
    • Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region
    • Budini, M., E. Buratti, C. Stuani, C. Guarnaccia, V. Romano, L. De Conti, and F.E. Baralle. 2012. Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region. J. Biol. Chem. 287:7512-7525. http://dx.doi.org/10.1074/jbc.M111.288720
    • (2012) J. Biol. Chem , vol.287 , pp. 7512-7525
    • Budini, M.1    Buratti, E.2    Stuani, C.3    Guarnaccia, C.4    Romano, V.5    De Conti, L.6    Baralle, F.E.7
  • 7
    • 78049454066 scopus 로고
    • Amyotrophies spinales deuteropathiques sclérose latérale amyotrophique & sclérose latérale amyotrophique
    • Charcot, J.M. 1874. Amyotrophies spinales deuteropathiques sclérose latérale amyotrophique & sclérose latérale amyotrophique. Bureaux du Progrès Médical. 2:234-266
    • (1874) Bureaux du Progrès Médical , vol.2 , pp. 234-266
    • Charcot, J.M.1
  • 9
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology
    • Danzer, K.M., S.K. Krebs, M. Wolff, G. Birk, and B. Hengerer. 2009. Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology. J. Neurochem. 111:192-203. http://dx.doi.org/10.1111/j.1471-4159.2009.06324.x
    • (2009) J. Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 10
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer, K.M., W.P. Ruf, P. Putcha, D. Joyner, T. Hashimoto, C. Glabe, B.T. Hyman, and P.J. McLean. 2011. Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FAS EB J. 25:326-336. http://dx.doi.org/10.1096/fj.10-164624
    • (2011) FAS EB J , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6    Hyman, B.T.7    McLean, P.J.8
  • 12
    • 79952268025 scopus 로고    scopus 로고
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • Dewey, C.M., B. Cenik, C.F. Sephton, D.R. Dries, P. Mayer III, S.K. Good, B.A. Johnson, J. Herz, and G. Yu. 2011. TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol. Cell. Biol. 31:1098-1108. http://dx.doi.org/10.1128/MCB.01279-10
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1098-1108
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Dries, D.R.4    Mayer, P.5    Good, S.K.6    Johnson, B.A.7    Herz, J.8    Yu, G.9
  • 14
    • 80052968310 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: cellular functions and implications for neurodegeneration
    • Fiesel, F.C., and P.J. Kahle. 2011. TDP-43 and FUS/TLS: cellular functions and implications for neurodegeneration. FEBS J. 278:3550-3568. http://dx.doi.org/10.1111/j.1742-4658.2011.08258.x
    • (2011) FEBS J , vol.278 , pp. 3550-3568
    • Fiesel, F.C.1    Kahle, P.J.2
  • 15
    • 84918565681 scopus 로고    scopus 로고
    • Prion-like mechanisms in the pathogenesis of tauopathies and synucleinopathies
    • Goedert, M., B. Falcon, F. Clavaguera, and M. Tolnay. 2014. Prion-like mechanisms in the pathogenesis of tauopathies and synucleinopathies. Curr. Neurol. Neurosci. Rep. 14:495. http://dx.doi.org/10.1007/s11910-014-0495-z
    • (2014) Curr. Neurol. Neurosci. Rep , vol.14 , pp. 495
    • Goedert, M.1    Falcon, B.2    Clavaguera, F.3    Tolnay, M.4
  • 18
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B.S., D. Snead, J.J. Lee, J.M. McCaffery, J. Shorter, and A.D. Gitler. 2009. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284:20329-20339. http://dx.doi.org/10.1074/jbc.M109.010264
    • (2009) J. Biol. Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 19
    • 84861841901 scopus 로고    scopus 로고
    • Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation?
    • Kanouchi, T., T. Ohkubo, and T. Yokota. 2012. Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation? J. Neurol. Neurosurg. Psychiatry. 83:739-745. http://dx.doi.org/10.1136/jnnp-2011-301826
    • (2012) J. Neurol. Neurosurg. Psychiatry , vol.83 , pp. 739-745
    • Kanouchi, T.1    Ohkubo, T.2    Yokota, T.3
  • 20
    • 84857772495 scopus 로고    scopus 로고
    • TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes
    • Kawahara, Y., and A. Mieda-Sato. 2012. TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes. Proc. Natl. Acad. Sci. USA. 109:3347-3352. http://dx.doi.org/10.1073/pnas.1112427109
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 3347-3352
    • Kawahara, Y.1    Mieda-Sato, A.2
  • 21
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • Luk, K.C., C. Song, P. O'Brien, A. Stieber, J.R. Branch, K.R. Brunden, J.Q. Trojanowski, and V.M. Lee. 2009. Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc. Natl. Acad. Sci. USA. 106:20051-20056. http://dx.doi.org/10.1073/pnas.0908005106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20051-20056
    • Luk, K.C.1    Song, C.2    O'Brien, P.3    Stieber, A.4    Branch, J.R.5    Brunden, K.R.6    Trojanowski, J.Q.7    Lee, V.M.8
  • 22
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
    • Luk, K.C., V.M. Kehm, B. Zhang, P. O'Brien, J.Q. Trojanowski, and V.M. Lee. 2012. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J. Exp. Med. 209:975-986. http://dx.doi.org/10.1084/jem.20112457
    • (2012) J. Exp. Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 23
    • 84938740314 scopus 로고    scopus 로고
    • From nucleation to widespread propagation: A prion-like concept for ALS
    • Maniecka, Z., and M. Polymenidou. 2015. From nucleation to widespread propagation: A prion-like concept for ALS. Virus Res. 207:94-105. http://dx.doi.org/10.1016/j.virusres.2014.12.032
    • (2015) Virus Res , vol.207 , pp. 94-105
    • Maniecka, Z.1    Polymenidou, M.2
  • 31
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli, P., and R.H. Brown. 2006. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7:710-723. http://dx.doi.org/10.1038/nrn1971
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 32
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis, G.S., V.M. Lee, and J.Q. Trojanowski. 2009. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet. 18(R2):R156-R162. http://dx.doi.org/10.1093/hmg/ddp303
    • (2009) Hum. Mol. Genet , vol.18 , Issue.R2 , pp. R156-R162
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 33
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: prion-like spreading in ALS
    • Polymenidou, M., and D.W. Cleveland. 2011. The seeds of neurodegeneration: prion-like spreading in ALS. Cell. 147:498-508. http://dx.doi.org/10.1016/j.cell.2011.10.011
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 34
    • 70349581626 scopus 로고    scopus 로고
    • ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration
    • Ravits, J.M., and A.R. La Spada. 2009. ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration. Neurology. 73:805-811. http://dx.doi.org/10.1212/WNL.0b013e3181b6bbbd
    • (2009) Neurology , vol.73 , pp. 805-811
    • Ravits, J.M.1    La Spada, A.R.2
  • 35
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy, I., and S.W. Michnick. 2006. A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat. Methods. 3:977-979. http://dx.doi.org/10.1038/nmeth979
    • (2006) Nat. Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 36
    • 84939884559 scopus 로고    scopus 로고
    • A cell culture model for monitoring α-synuclein cell-to-cell transfer
    • Reyes, J.F., T.T. Olsson, J.T. Lamberts, M.J. Devine, T. Kunath, and P. Brundin. 2014. A cell culture model for monitoring α-synuclein cell-to-cell transfer. Neurobiol. Dis. 77:266-275. http://dx.doi.org/10.1016/j.nbd.2014.07.003
    • (2014) Neurobiol. Dis , vol.77 , pp. 266-275
    • Reyes, J.F.1    Olsson, T.T.2    Lamberts, J.T.3    Devine, M.J.4    Kunath, T.5    Brundin, P.6
  • 37
    • 85027906412 scopus 로고    scopus 로고
    • Potential of cellular and animal models based on a prion-like propagation of α-synuclein for assessing antiparkinson agents
    • Sato, H., T. Kato, and S. Arawaka. 2014. Potential of cellular and animal models based on a prion-like propagation of α-synuclein for assessing antiparkinson agents. Mol. Neurobiol
    • (2014) Mol. Neurobiol
    • Sato, H.1    Kato, T.2    Arawaka, S.3
  • 39
    • 84939789089 scopus 로고    scopus 로고
    • Comparative analysis of cesium chloride- and iodixanol-based purification of recombinant Adeno-associated virus (AAV) vectors for preclinical applications
    • Strobel, B., F.D. Miller, W. Rist, and T. Lamla. 2015. Comparative analysis of cesium chloride- and iodixanol-based purification of recombinant Adeno-associated virus (AAV) vectors for preclinical applications. Hum. Gene Ther. Methods. 26:147-157. http://dx.doi.org/10.1089/hgtb.2015.051
    • (2015) Hum. Gene Ther. Methods , vol.26 , pp. 147-157
    • Strobel, B.1    Miller, F.D.2    Rist, W.3    Lamla, T.4
  • 40
    • 14044250981 scopus 로고    scopus 로고
    • Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo
    • Tannous, B.A., D.E. Kim, J.L. Fernandez, R. Weissleder, and X.O. Breakefield. 2005. Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Mol. Ther. 11:435-443. http://dx.doi.org/10.1016/j.ymthe.2004.10.016
    • (2005) Mol. Ther , vol.11 , pp. 435-443
    • Tannous, B.A.1    Kim, D.E.2    Fernandez, J.L.3    Weissleder, R.4    Breakefield, X.O.5
  • 41
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • John Wiley & Sons Inc., New York, 3.22., .22.29
    • Thery, C., S. Amigorena, G. Raposo, and A. Clayton. 2006. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. In Current Protocols in Cell Biology. John Wiley & Sons Inc., New York. 3.22.1-3.22.29. http://dx.doi.org/10.1002/0471143030.cb0322s30
    • (2006) Current Protocols in Cell Biology , pp. 1-3
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 42
    • 77955395385 scopus 로고    scopus 로고
    • Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U. J. Exp
    • Tsai, K.J., C.H. Yang, Y.H. Fang, K.H. Cho, W.L. Chien, W.T. Wang, T.W. Wu, C.P. Lin, W.M. Fu, and C.K. Shen. 2010. Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U. J. Exp. Med. 207:1661-1673. http://dx.doi.org/10.1084/jem.20092164
    • (2010) Med , vol.207 , pp. 1661-1673
    • Tsai, K.J.1    Yang, C.H.2    Fang, Y.H.3    Cho, K.H.4    Chien, W.L.5    Wang, W.T.6    Wu, T.W.7    Lin, C.P.8    Fu, W.M.9    Shen, C.K.10
  • 43
    • 84905045481 scopus 로고    scopus 로고
    • Electron tomography and cryo-SEM characterization reveals novel ultrastructural features of host-parasite interaction during Chlamydia abortus infection
    • Wilkat, M., E. Herdoiza, V. Forsbach-Birk, P. Walther, and A. Essig. 2014. Electron tomography and cryo-SEM characterization reveals novel ultrastructural features of host-parasite interaction during Chlamydia abortus infection. Histochem. Cell Biol. 142:171-184. http://dx.doi.org/10.1007/s00418-014-1189-y
    • (2014) Histochem. Cell Biol , vol.142 , pp. 171-184
    • Wilkat, M.1    Herdoiza, E.2    Forsbach-Birk, V.3    Walther, P.4    Essig, A.5
  • 45
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu, Y.F., T.F. Gendron, Y.J. Zhang, W.L. Lin, S. D'Alton, H. Sheng, M.C. Casey, J. Tong, J. Knight, X. Yu, et al. 2010. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J. Neurosci. 30:10851-10859. http://dx.doi.org/10.1523/JNEUROSCI.1630-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 10851-10859
    • Xu, Y.F.1    Gendron, T.F.2    Zhang, Y.J.3    Lin, W.L.4    D'Alton, S.5    Sheng, H.6    Casey, M.C.7    Tong, J.8    Knight, J.9    Yu, X.10
  • 47
    • 84863337784 scopus 로고    scopus 로고
    • Predicting regional neurodegeneration from the healthy brain functional connectome
    • Zhou, J., E.D. Gennatas, J.H. Kramer, B.L. Miller, and W.W. Seeley. 2012. Predicting regional neurodegeneration from the healthy brain functional connectome. Neuron. 73:1216-1227. http://dx.doi.org/10.1016/j.neuron.2012.03.004
    • (2012) Neuron , vol.73 , pp. 1216-1227
    • Zhou, J.1    Gennatas, E.D.2    Kramer, J.H.3    Miller, B.L.4    Seeley, W.W.5
  • 48
    • 84929126317 scopus 로고    scopus 로고
    • An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution
    • Zhu, L., M. Xu, M. Yang, Y. Yang, Y. Li, J. Deng, L. Ruan, J. Liu, S. Du, X. Liu, et al. 2014. An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution. Hum. Mol. Genet. 23:6863-6877. http://dx.doi.org/10.1093/hmg/ddu409
    • (2014) Hum. Mol. Genet , vol.23 , pp. 6863-6877
    • Zhu, L.1    Xu, M.2    Yang, M.3    Yang, Y.4    Li, Y.5    Deng, J.6    Ruan, L.7    Liu, J.8    Du, S.9    Liu, X.10


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