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Volumn 116, Issue 6, 2011, Pages 957-965

Biochemical and histopathological alterations in TAR DNA-binding protein-43 after acute ischemic stroke in rats

Author keywords

caspase 3; ischemia; proteolysis; rat; TAR DNA binding protein 43

Indexed keywords

TAR DNA BINDING PROTEIN; UBIQUITIN;

EID: 79952375490     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06860.x     Document Type: Article
Times cited : (31)

References (28)
  • 3
    • 69549114542 scopus 로고    scopus 로고
    • The molecular links between TDP-43 dysfunction and neurodegeneration
    • in (Friedmann T., Dunlap J. C. and Goodwin S. F., eds), Vol., pp. Elsevier Inc., Amsterdam.
    • Buratti E., and, Baralle F.,. (2009) The molecular links between TDP-43 dysfunction and neurodegeneration, in Advances in Genetics (, Friedmann T., Dunlap J. C., and, Goodwin S. F., eds), Vol. 66, pp. 1-34. Elsevier Inc., Amsterdam.
    • (2009) Advances in Genetics , vol.66 , pp. 1-34
    • Buratti, E.1    Baralle, F.2
  • 6
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • et al.
    • Hasegawa M., Arai T., Nonaka T., et al. (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 64, 60-70.
    • (2008) Ann. Neurol. , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3
  • 7
    • 0037436884 scopus 로고    scopus 로고
    • Some glial progenitors in the neonatal subventricular zone migrate through the corpus callosum to the contralateral cerebral hemisphere
    • DOI 10.1002/cne.10597
    • Kakita A., Zerlin M., Takahashi H., and, Goldman J. E., (2003) Some glial progenitors in the neonatal subventricular zone migrate through the corpus callosum to the contralateral cerebral hemisphere. J. Comp. Neurol. 458, 381-388. (Pubitemid 36337054)
    • (2003) Journal of Comparative Neurology , vol.458 , Issue.4 , pp. 381-388
    • Kakita, A.1    Zerlin, M.2    Takahashi, H.3    Goldman, J.E.4
  • 10
    • 39749083266 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system
    • Lee E. B., Lee V. M., Trojanowski J. Q., and, Neumann M., (2008) TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system. Acta Neuropathol. 115, 305-311.
    • (2008) Acta Neuropathol. , vol.115 , pp. 305-311
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3    Neumann, M.4
  • 11
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update
    • et al.
    • Mackenzie I. R., Neumann M., Bigio E. H., et al. (2010) Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update. Acta Neuropathol. 119, 1-4.
    • (2010) Acta Neuropathol. , vol.119 , pp. 1-4
    • MacKenzie, I.R.1    Neumann, M.2    Bigio, E.H.3
  • 12
    • 0026598564 scopus 로고
    • Penumbral tissues salvaged by reperfusion following middle cerebral artery occlusion in rats
    • Memezawa H., Smith M. L., and, Siesjo B. K., (1992) Penumbral tissues salvaged by reperfusion following middle cerebral artery occlusion in rats. Stroke 23, 552-559.
    • (1992) Stroke , vol.23 , pp. 552-559
    • Memezawa, H.1    Smith, M.L.2    Siesjo, B.K.3
  • 13
    • 58049221032 scopus 로고    scopus 로고
    • Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: Implications for TDP-43 in the physiological response to neuronal injury
    • Moisse K., Volkening K., Leystra-Lantz C., Welch I., Hill T., and, Strong M. J., (2009a) Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury. Brain Res. 1249, 202-211.
    • (2009) Brain Res. , vol.1249 , pp. 202-211
    • Moisse, K.1    Volkening, K.2    Leystra-Lantz, C.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 14
    • 70349292075 scopus 로고    scopus 로고
    • Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL-/- mice: Support for a role for TDP-43 in the physiological response to neuronal injury
    • Moisse K., Mepham J., Volkening K., Welch I., Hill T., and, Strong M. J., (2009b) Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL-/- mice: support for a role for TDP-43 in the physiological response to neuronal injury. Brain Res. 1296, 176-186.
    • (2009) Brain Res. , vol.1296 , pp. 176-186
    • Moisse, K.1    Mepham, J.2    Volkening, K.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 16
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Nonaka T., Arai T., Buratti E., Baralle F. E., Akiyama H., and, Hasegawa M., (2009a) Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett. 583, 394-400.
    • (2009) FEBS Lett. , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5    Hasegawa, M.6
  • 17
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka T., Kametani F., Arai T., Akiyama H., and, Hasegawa M., (2009b) Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum. Mol. Genet. 18, 3353-3364.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 18
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis G. S., Lee V. M., and, Trojanowski J. Q., (2009) Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet. 18, R156-R162.
    • (2009) Hum. Mol. Genet. , vol.18
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 19
    • 0032898735 scopus 로고    scopus 로고
    • Non-specific effects of methyl ketone peptide inhibitors of caspases
    • DOI 10.1016/S0014-5793(98)01640-8, PII S0014579398016408
    • Schotte P., Declercq W., Van Huffel S., Vandenabeele P., and, Beyaert R., (1999) Non-specific effects of methyl ketone peptide inhibitors of caspases. FEBS Lett. 442, 117-121. (Pubitemid 29065390)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 117-121
    • Schotte, P.1    Declercq, W.2    Van Huffel, S.3    Vandenabeele, P.4    Beyaert, R.5
  • 20
    • 34547111785 scopus 로고    scopus 로고
    • Suppression of δPKC activation after focal cerebral ischemia contributes to the protective effect of hypothermia
    • DOI 10.1038/sj.jcbfm.9600450, PII 9600450
    • Shimohata T., Zhao H., Sung J. H., Sun G., Mochly-Rosen D., and, Steinberg G. K., (2007) Suppression of δPKC activation after focal cerebral ischemia contributes to the protective effect of hypothermia. J. Cereb. Blood Flow Metab. 27, 1463-1475. (Pubitemid 47106606)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.8 , pp. 1463-1475
    • Shimohata, T.1    Zhao, H.2    Sung, J.H.3    Sun, G.4    Mochly-Rosen, D.5    Steinberg, G.K.6
  • 21
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • et al.
    • Sreedharan J., Blair I. P., Tripathi V. B., et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1668-16672.
    • (2008) Science , vol.319 , pp. 1668-16672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3
  • 23
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • DOI 10.1016/S0888-7543(03)00214-3
    • Wang H. Y., Wang I. F., Bose J., and, Shen C. K., (2004) Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 83, 130-139. (Pubitemid 37518267)
    • (2004) Genomics , vol.83 , Issue.1 , pp. 130-139
    • Wang, H.-Y.1    Wang, I.-F.2    Bose, J.3    Shen, C.-K.J.4
  • 24
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang I. F., Wu L. S., Chang H. Y., and, Shen C. K., (2008) TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 105, 797-806.
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 25
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redisturbance, sequestration, and aggregate formation
    • Winton M. J., Igaz L. M., Wong M. M., Kwong L. K., Trojanowski J. Q., and, Lee V. M., (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redisturbance, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 28
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • et al.
    • Zhang Y. J., Xu Y. F., Cook C., et al. (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc. Natl Acad. Sci. USA 106, 7607-7612.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7607-7612
    • Zhang, Y.J.1    Xu, Y.F.2    Cook, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.