메뉴 건너뛰기




Volumn 1386, Issue , 2011, Pages 191-199

β-Amyloid triggers ALS-associated TDP-43 pathology in AD models

Author keywords

amyloid; Synuclein; AD; ALS; FTLD; PD; Tau; TDP 43

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; CASEIN KINASE; LENTIVIRUS VECTOR; TAR DNA BINDING PROTEIN; TAU PROTEIN;

EID: 79953882939     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2011.02.052     Document Type: Article
Times cited : (53)

References (63)
  • 3
    • 0035377241 scopus 로고    scopus 로고
    • Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7
    • Ardley, H.C., Tan, N.G., Rose, S.A., Markham, A.F., Robinson, P.A., 2001. Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. J. Biol. Chem. 276, 19640-19647.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19640-19647
    • Ardley, H.C.1    Tan, N.G.2    Rose, S.A.3    Markham, A.F.4    Robinson, P.A.5
  • 6
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti, E., Brindisi, A., Giombi, M., Tisminetzky, S., Ayala, Y.M., Baralle, F.E., 2005. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J. Biol. Chem. 280, 37572-37584.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5    Baralle, F.E.6
  • 7
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti, E., Baralle, F.E., 2008. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci. 13, 867-878.
    • (2008) Front. Biosci. , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 9
    • 70350454798 scopus 로고    scopus 로고
    • Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability
    • Caccamo, A., Majumder, S., Deng, J.J., Bai, Y., Thornton, F.B., Oddo, S., 2009. Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability. J. Biol. Chem. 284, 27416-27424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27416-27424
    • Caccamo, A.1    Majumder, S.2    Deng, J.J.3    Bai, Y.4    Thornton, F.B.5    Oddo, S.6
  • 10
    • 78149318021 scopus 로고    scopus 로고
    • Age-dependent changes in TDP-43 levels in a mouse model of Alzheimer disease are linked to Abeta oligomers accumulation
    • Caccamo, A., Magri, A., Oddo, S., 2010. Age-dependent changes in TDP-43 levels in a mouse model of Alzheimer disease are linked to Abeta oligomers accumulation. Mol. Neurodegener. 5, 51.
    • (2010) Mol. Neurodegener. , vol.5 , pp. 51
    • Caccamo, A.1    Magri, A.2    Oddo, S.3
  • 11
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook, D.G., Forman, M.S., Sung, J.C., Leight, S., Kolson, D.L., Iwatsubo, T., Lee, V.M., Doms, R.W., 1997. Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3, 1021-1023.
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.7    Doms, R.W.8
  • 12
    • 34247625005 scopus 로고    scopus 로고
    • Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43
    • DOI 10.1007/s00401-006-0189-y
    • Davidson, Y., Kelley, T., Mackenzie, I.R., Pickering-Brown, S., Du Plessis, D., Neary, D., Snowden, J.S., Mann, D.M., 2007. Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43. Acta Neuropathol. 113, 521-533. (Pubitemid 46672598)
    • (2007) Acta Neuropathologica , vol.113 , Issue.5 , pp. 521-533
    • Davidson, Y.1    Kelley, T.2    Mackenzie, I.R.A.3    Pickering-Brown, S.4    Du, P.D.5    Neary, D.6    Snowden, J.S.7    Mann, D.M.A.8
  • 18
    • 33751250197 scopus 로고    scopus 로고
    • Genetics of familial and sporadic amyotrophic lateral sclerosis
    • Gros-Louis, F., Gaspar, C., Rouleau, G.A., 2006. Genetics of familial and sporadic amyotrophic lateral sclerosis. Biochim. Biophys. Acta 1762, 956-972.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 956-972
    • Gros-Louis, F.1    Gaspar, C.2    Rouleau, G.A.3
  • 21
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J., Selkoe, D.J., 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 22
    • 34249709931 scopus 로고    scopus 로고
    • TDP-43 is deposited in the Guam parkinsonism-dementia complex brains
    • DOI 10.1093/brain/awm065
    • Hasegawa, M., Arai, T., Akiyama, H., Nonaka, T., Mori, H., Hashimoto, T., Yamazaki, M., Oyanagi, K., 2007. TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 130, 1386-1394. (Pubitemid 47355958)
    • (2007) Brain , vol.130 , Issue.5 , pp. 1386-1394
    • Hasegawa, M.1    Arai, T.2    Akiyama, H.3    Nonaka, T.4    Mori, H.5    Hashimoto, T.6    Yamazaki, M.7    Oyanagi, K.8
  • 24
    • 0026721235 scopus 로고
    • Distribution of cortical neurofibrillary tangles in progressive supranuclear palsy: A quantitative analysis of six cases
    • Hof, P.R., Delacourte, A., Bouras, C., 1992. Distribution of cortical neurofibrillary tangles in progressive supranuclear palsy: a quantitative analysis of six cases. Acta Neuropathol. 84, 45-51.
    • (1992) Acta Neuropathol. , vol.84 , pp. 45-51
    • Hof, P.R.1    Delacourte, A.2    Bouras, C.3
  • 25
    • 0037047311 scopus 로고    scopus 로고
    • Effect of wild-type or mutant Parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome
    • Hyun, D.H., Lee, M., Hattori, N., Kubo, S., Mizuno, Y., Halliwell, B., Jenner, P., 2002. Effect of wild-type or mutant Parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome. J. Biol. Chem. 277, 28572-28577.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28572-28577
    • Hyun, D.H.1    Lee, M.2    Hattori, N.3    Kubo, S.4    Mizuno, Y.5    Halliwell, B.6    Jenner, P.7
  • 26
    • 43649103517 scopus 로고    scopus 로고
    • Astrocytic tau pathology positively correlates with neurofibrillary tangle density in progressive supranuclear palsy
    • Ito, K., Arai, K., Yoshiyama, Y., Kashiwado, K., Sakakibara, Y., Hattori, T., 2008. Astrocytic tau pathology positively correlates with neurofibrillary tangle density in progressive supranuclear palsy. Acta Neuropathol. 115, 623-628.
    • (2008) Acta Neuropathol. , vol.115 , pp. 623-628
    • Ito, K.1    Arai, K.2    Yoshiyama, Y.3    Kashiwado, K.4    Sakakibara, Y.5    Hattori, T.6
  • 28
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E.H., Squazzo, S.L., 1994. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 31
    • 0037044240 scopus 로고    scopus 로고
    • The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
    • Lomen-Hoerth, C., Anderson, T., Miller, B., 2002. The overlap of amyotrophic lateral sclerosis and frontotemporal dementia. Neurology 59, 1077-1079.
    • (2002) Neurology , vol.59 , pp. 1077-1079
    • Lomen-Hoerth, C.1    Anderson, T.2    Miller, B.3
  • 35
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett, E., Bork, P., 1999. A novel transactivation domain in parkin. Trends Biochem. Sci. 24, 229-231.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 37
    • 23844445158 scopus 로고    scopus 로고
    • Clinicopathological features of the tauopathies
    • Murray, B., Lynch, T., Farrell, M., 2005. Clinicopathological features of the tauopathies. Biochem. Soc. Trans. 33, 595-599.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 595-599
    • Murray, B.1    Lynch, T.2    Farrell, M.3
  • 40
    • 0034528007 scopus 로고    scopus 로고
    • Classification and description of frontotemporal dementias
    • Neary, D., Snowden, J.S., Mann, D.M., 2000. Classification and description of frontotemporal dementias. Ann. NY Acad. Sci. 920, 46-51.
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 46-51
    • Neary, D.1    Snowden, J.S.2    Mann, D.M.3
  • 42
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: Protein misfolding diseases without amyloidosis
    • Neumann, M., Kwong, L.K., Sampathu, D.M., Trojanowski, J.Q., Lee, V.M., 2007a. TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis. Arch. Neurol. 64, 1388-1394.
    • (2007) Arch. Neurol. , vol.64 , pp. 1388-1394
    • Neumann, M.1    Kwong, L.K.2    Sampathu, D.M.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 44
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli, P., Brown, R.H., 2006. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7, 710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 45
    • 0037062609 scopus 로고    scopus 로고
    • The prevalence of frontotemporal dementia
    • Ratnavalli, E., Brayne, C., Dawson, K., Hodges, J.R., 2002. The prevalence of frontotemporal dementia. Neurology 58, 1615-1621. (Pubitemid 34602891)
    • (2002) Neurology , vol.58 , Issue.11 , pp. 1615-1621
    • Ratnavalli, E.1    Brayne, C.2    Dawson, K.3    Hodges, J.R.4
  • 46
    • 77951226607 scopus 로고    scopus 로고
    • Beta-Amyloid1-42 gene transfer model exhibits intraneuronal amyloid, gliosis, tau phosphorylation, and neuronal loss
    • Rebeck, G.W., Hoe, H.S., Moussa, C.E., 2010. beta]-Amyloid1-42 gene transfer model exhibits intraneuronal amyloid, gliosis, tau phosphorylation, and neuronal loss. J. Biol. Chem.
    • (2010) J. Biol. Chem.
    • Rebeck, G.W.1    Hoe, H.S.2    Moussa, C.E.3
  • 47
    • 40749134969 scopus 로고    scopus 로고
    • Parkin polymorphisms in progressive supranuclear palsy
    • Ros, R., Ampuero, I., Garcia de Yebenes, J., 2008. Parkin polymorphisms in progressive supranuclear palsy. J. Neurol. Sci. 268, 176-178.
    • (2008) J. Neurol. Sci. , vol.268 , pp. 176-178
    • Ros, R.1    Ampuero, I.2    Garcia De Yebenes, J.3
  • 48
    • 0027164824 scopus 로고
    • Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis (Nature (1993) 362 (59-62))
    • Rosen, D.R., 1993. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364, 362. (Pubitemid 23265284)
    • (1993) Nature , vol.364 , Issue.6435 , pp. 362
    • Rosen, D.R.1
  • 49
    • 0036812559 scopus 로고    scopus 로고
    • Progressive supranuclear palsy and tau hyperphosphorylation in a patient with a C212Y parkin mutation
    • Sanchez, M.P., Gonzalo, I., Avila, J., De Yebenes, J.G., 2002. Progressive supranuclear palsy and tau hyperphosphorylation in a patient with a C212Y parkin mutation. J. Alzheimers Dis. 4, 399-404. (Pubitemid 35397805)
    • (2002) Journal of Alzheimer's Disease , vol.4 , Issue.5 , pp. 399-404
    • Sanchez, M.P.1    Gonzalo, I.2    Avila, J.3    De Yebenes, J.G.4
  • 50
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture
    • DOI 10.1083/jcb.141.4.1031
    • Skovronsky, D.M., Doms, R.W., Lee, V.M., 1998. Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J. Cell Biol. 141, 1031-1039. (Pubitemid 28243969)
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.-Y.3
  • 53
    • 33749002522 scopus 로고    scopus 로고
    • Recent advances in the genetics of amyotrophic lateral sclerosis and frontotemporal dementia: Common pathways in neurodegenerative disease
    • Talbot, K., Ansorge, O., 2006. Recent advances in the genetics of amyotrophic lateral sclerosis and frontotemporal dementia: common pathways in neurodegenerative disease. Hum. Mol. Genet. 15 Spec No 2, R182-R187.
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.SPEC NO 2
    • Talbot, K.1    Ansorge, O.2
  • 54
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • DOI 10.1007/s00401-007-0206-9
    • Tan, C.F., Eguchi, H., Tagawa, A., Onodera, O., Iwasaki, T., Tsujino, A., Nishizawa, M., Kakita, A., Takahashi, H., 2007. TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol. 113, 535-542. (Pubitemid 46672599)
    • (2007) Acta Neuropathologica , vol.113 , Issue.5 , pp. 535-542
    • Tan, C.-F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 55
    • 0035976835 scopus 로고    scopus 로고
    • alpha-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • DOI 10.1016/S0014-5793(01)03115-5, PII S0014579301031155
    • Tofaris, G.K., Layfield, R., Spillantini, M.G., 2001. alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509, 22-26. (Pubitemid 33153074)
    • (2001) FEBS Letters , vol.509 , Issue.1 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 57
    • 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., 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
  • 58
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., Bell, S., Cairns, N.J., Miller, T.M., Baloh, R.H., 2009. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 106, 18809-18814.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 59
    • 0032800818 scopus 로고    scopus 로고
    • Intracellular APP processing and A beta production in Alzheimer disease
    • Wilson, C.A., Doms, R.W., Lee, V.M., 1999. Intracellular APP processing and A beta production in Alzheimer disease. J. Neuropathol. Exp. Neurol. 58, 787-794.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 787-794
    • Wilson, C.A.1    Doms, R.W.2    Lee, V.M.3
  • 60
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M.J., Igaz, L.M., Wong, M.M., Kwong, L.K., Trojanowski, J.Q., Lee, V.M., 2008. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, 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
  • 61
    • 0030963605 scopus 로고    scopus 로고
    • Generation of Alzheimer beta-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
    • Xu, H., Sweeney, D., Wang, R., Thinakaran, G., Lo, A.C., Sisodia, S.S., Greengard, P., Gandy, S., 1997. Generation of Alzheimer beta-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation. Proc. Natl Acad. Sci. USA 94, 3748-3752.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3748-3752
    • Xu, H.1    Sweeney, D.2    Wang, R.3    Thinakaran, G.4    Lo, A.C.5    Sisodia, S.S.6    Greengard, P.7    Gandy, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.