메뉴 건너뛰기




Volumn 70, Issue 9, 2011, Pages 788-798

Accumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer disease

Author keywords

Alzheimer disease; Amyloid; Human; Immunoblot; Mild cognitive impairment; Tau; TDP 43

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; TAR DNA BINDING PROTEIN; TAU PROTEIN;

EID: 80052185880     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0b013e31822c62cf     Document Type: Review
Times cited : (75)

References (66)
  • 1
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregationprone and ALS-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, et al. TDP-43 is intrinsically aggregationprone and ALS-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 2009;284:20329-39
    • (2009) J Biol Chem , vol.284 , pp. 20329-39
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3
  • 6
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update
    • Mackenzie IR, Neumann M, Bigio EH, et al. Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update. Acta Neuropathol 2010;119:1-4
    • (2010) Acta Neuropathol , vol.119 , pp. 1-4
    • MacKenzie, I.R.1    Neumann, M.2    Bigio, E.H.3
  • 7
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis GS, Lee VMY, Trojanowski JQ. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum Mol Genet 2009;18:R156-62
    • (2009) Hum Mol Genet , vol.18
    • Pesiridis, G.S.1    Vmy, L.2    Trojanowski, J.Q.3
  • 8
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW. TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 2010;19:R46-64
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 9
    • 59649086176 scopus 로고    scopus 로고
    • Molecular neuropathology of TDP-43 proteinopathies
    • Neumann M. Molecular neuropathology of TDP-43 proteinopathies. Int J Mol Sci 2009;10:232-46
    • (2009) Int J Mol Sci , vol.10 , pp. 232-246
    • Neumann, M.1
  • 10
    • 60549117972 scopus 로고    scopus 로고
    • Clinical and pathological continuum of multisystem TDP-43 proteinopathies
    • Geser F, Martinez-Lage M, Robinson J, et al. Clinical and pathological continuum of multisystem TDP-43 proteinopathies. Arch Neurol 2009; 66:180-89
    • (2009) Arch Neurol , vol.66 , pp. 180-189
    • Geser, F.1    Martinez-Lage, M.2    Robinson, J.3
  • 11
    • 69549114542 scopus 로고    scopus 로고
    • The molecular links between TDP-43 dysfunction and neurodegeneration
    • Buratti E, Baralle FE. The molecular links between TDP-43 dysfunction and neurodegeneration. Adv Genet 2009;66:1-34
    • (2009) Adv Genet , vol.66 , pp. 1-34
    • Buratti, E.1    Baralle, F.E.2
  • 12
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • Geser F, Martinez-Lage M, Kwong LK, et al. Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases. J Neurol 2009;256:1205-14
    • (2009) J Neurol , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3
  • 13
    • 77951700391 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 can affect selected microRNA levels
    • Buratti E, De Conti L, Stuani C, et al. Nuclear factor TDP-43 can affect selected microRNA levels. FEBS J 2010;277:2268-81
    • (2010) FEBS J , vol.277 , pp. 2268-2281
    • Buratti, E.1    De Conti, L.2    Stuani, C.3
  • 14
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 poteinopathies
    • Igaz LM, Kwong LK, Chen-Plotkin A, et al. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 poteinopathies. J Biol Chem 2009;284:8516-24
    • (2009) J Biol Chem , vol.284 , pp. 8516-8524
    • Igaz, L.M.1    Kwong, L.K.2    Chen-Plotkin, A.3
  • 15
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein JD. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann Neurol 2009;65(Suppl 1):S3-9
    • (2009) Ann Neurol , vol.65 , Issue.SUPPL.1
    • Rothstein, J.D.1
  • 17
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • Zhang YJ, Xu YF, Cook C, et al. Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci USA 2009;106: 7607-12
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7607-7612
    • Zhang, Y.J.1    Xu, Y.F.2    Cook, C.3
  • 18
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T, et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 2008;64:60-70
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3
  • 19
    • 47949084000 scopus 로고    scopus 로고
    • Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease
    • Hu WT, Josephs KA, Knopman DS, et al. Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease. Acta Neuropathol 2008;116:215-20
    • (2008) Acta Neuropathol , vol.116 , pp. 215-220
    • Hu, W.T.1    Josephs, K.A.2    Knopman, D.S.3
  • 20
    • 70349308579 scopus 로고    scopus 로고
    • Regional distribution of TDP-43 inclusions in Alzheimer disease (AD) brains: Their relation to AD common pathology
    • Kadokura A, Yamazaki T, Lemere CA, et al. Regional distribution of TDP-43 inclusions in Alzheimer disease (AD) brains: Their relation to AD common pathology. Neuropathology 2009;29:566-73
    • (2009) Neuropathology , vol.29 , pp. 566-573
    • Kadokura, A.1    Yamazaki, T.2    Lemere, C.A.3
  • 22
    • 59249097160 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies
    • Arai T, Mackenzie IRA, Hasegawa M, et al. Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies. Acta Neuropathol 2009;117:125-36
    • (2009) Acta Neuropathol , vol.117 , pp. 125-136
    • Arai, T.1    Ira, M.2    Hasegawa, M.3
  • 25
    • 43249094487 scopus 로고    scopus 로고
    • Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype
    • Josephs KA, Whitwell JL, Knopman DS, et al. Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype. Neurology 2008;70:1850
    • (2008) Neurology , vol.70 , pp. 1850
    • Josephs, K.A.1    Whitwell, J.L.2    Knopman, D.S.3
  • 26
    • 79956214776 scopus 로고    scopus 로고
    • TAR-DNA binding protein-43 and alterations in the hippocampus
    • Rauramaa T, Pikkarainen M, Englund E, et al. TAR-DNA binding protein-43 and alterations in the hippocampus. J Neural Transm 2011; 118:683-89
    • (2011) J Neural Transm , vol.118 , pp. 683-689
    • Rauramaa, T.1    Pikkarainen, M.2    Englund, E.3
  • 27
    • 77954149731 scopus 로고    scopus 로고
    • Abnormal TDP-43 expression is identified in the neocortex in cases of dementia pugilistica, but is mainly confined to the limbic system when identified in high and moderate stages of Alzheimer's disease
    • King A, Sweeney F, Bodi I, et al. Abnormal TDP-43 expression is identified in the neocortex in cases of dementia pugilistica, but is mainly confined to the limbic system when identified in high and moderate stages of Alzheimer's disease. Neuropathology 2010;30:408-19
    • (2010) Neuropathology , vol.30 , pp. 408-419
    • King, A.1    Sweeney, F.2    Bodi, I.3
  • 28
    • 77953870289 scopus 로고    scopus 로고
    • TDP-43 pathology in primary progressive aphasia and frontotemporal dementia with pathologic Alzheimer disease
    • Bigio EH, Mishra M, Hatanpaa KJ, et al. TDP-43 pathology in primary progressive aphasia and frontotemporal dementia with pathologic Alzheimer disease. Acta Neuropathol 2010;120:43-54
    • (2010) Acta Neuropathol , vol.120 , pp. 43-54
    • Bigio, E.H.1    Mishra, M.2    Hatanpaa, K.J.3
  • 29
    • 49349104833 scopus 로고    scopus 로고
    • Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease
    • Rohn TT. Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease. Brain Res 2008;1228:189-98
    • (2008) Brain Res , vol.1228 , pp. 189-198
    • Rohn, T.T.1
  • 30
    • 73549109864 scopus 로고    scopus 로고
    • Transactive response DNAbinding protein 43 burden in familial Alzheimer disease and Down syndrome
    • Lippa CF, Rosso AL, Stutzbach LD, et al. Transactive response DNAbinding protein 43 burden in familial Alzheimer disease and Down syndrome. Arch Neurol 2009;66:1483-88
    • (2009) Arch Neurol , vol.66 , pp. 1483-1488
    • Lippa, C.F.1    Rosso, A.L.2    Stutzbach, L.D.3
  • 31
  • 32
    • 38049018185 scopus 로고    scopus 로고
    • Biochemical characterization of AA and tau pathologies in mild cognitive impairment and Alzheimer's disease
    • Tremblay C, Pilote M, Phivilay A, et al. Biochemical characterization of AA and tau pathologies in mild cognitive impairment and Alzheimer's disease. J Alzheimers Dis 2007;12:377-90
    • (2007) J Alzheimers Dis , vol.12 , pp. 377-390
    • Tremblay, C.1    Pilote, M.2    Phivilay, A.3
  • 33
    • 14644416500 scopus 로고    scopus 로고
    • Mild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions
    • Bennett DA, Schneider JA, Bienias JL, et al. Mild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions. Neurology 2005;64:834-41 (Pubitemid 40316322)
    • (2005) Neurology , vol.64 , Issue.5 , pp. 834-841
    • Bennett, D.A.1    Schneider, J.A.2    Bienias, J.L.3    Evans, D.A.4    Wilson, R.S.5
  • 34
    • 75149192348 scopus 로고    scopus 로고
    • Neuropathologic alterations in mild cognitive impairment: A review
    • Markesbery WR. Neuropathologic alterations in mild cognitive impairment: A review. J Alzheimers Dis 2010;19:221-28
    • (2010) J Alzheimers Dis , vol.19 , pp. 221-228
    • Markesbery, W.R.1
  • 36
    • 68949099364 scopus 로고    scopus 로고
    • Neuropathology-based risk scoring for dementia diagnosis in the elderly
    • Haneuse S, Larson E, Walker R, et al. Neuropathology-based risk scoring for dementia diagnosis in the elderly. J Alzheimers Dis 2009;17:875-85
    • (2009) J Alzheimers Dis , vol.17 , pp. 875-885
    • Haneuse, S.1    Larson, E.2    Walker, R.3
  • 37
    • 59349092999 scopus 로고    scopus 로고
    • Criteria for the neuropathological diagnosis of dementing disorders: Routes out of the swamp?
    • Jellinger KA. Criteria for the neuropathological diagnosis of dementing disorders: Routes out of the swamp? Acta Neuropathol 2009;117:101-10
    • (2009) Acta Neuropathol , vol.117 , pp. 101-110
    • Jellinger, K.A.1
  • 38
    • 64049098761 scopus 로고    scopus 로고
    • Neuropathology and cognitive impairment in Alzheimer disease: A complex but coherent relationship
    • Nelson PT, Braak H, Markesbery WR. Neuropathology and cognitive impairment in Alzheimer disease: A complex but coherent relationship. J Neuropathol Exp Neurol 2009;68:1-14
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 1-14
    • Nelson, P.T.1    Braak, H.2    Markesbery, W.R.3
  • 39
    • 40849101426 scopus 로고    scopus 로고
    • Epitope mapping of 2E2-D3, a monoclonal antibody directed against human TDP-43
    • Zhang HX, Tanji K, Mori F, et al. Epitope mapping of 2E2-D3, a monoclonal antibody directed against human TDP-43. Neurosci Lett 2008;434: 170-74
    • (2008) Neurosci Lett , vol.434 , pp. 170-174
    • Zhang, H.X.1    Tanji, K.2    Mori, F.3
  • 40
    • 33747613756 scopus 로고    scopus 로고
    • Postmortem indices linking risk factors to cognition: Results from the Religious Order Study and the Memory and Aging Project
    • DOI 10.1097/00002093-200607001-00009, PII 0000209320060700100009
    • Bennett DA. Postmortem indices linking risk factors to cognition: Results from the Religious Order Study and the Memory and Aging Project. Alzheimer Dis Assoc Disord 2006;20:S63-68 (Pubitemid 44265853)
    • (2006) Alzheimer Disease and Associated Disorders , vol.20 , Issue.SUPPL. 2
    • Bennett, D.A.1
  • 43
    • 79952590449 scopus 로고    scopus 로고
    • Cognitive decline in prodromal Alzheimer disease and mild cognitive impairment
    • Wilson RS, Leurgans SE, Boyle PA, et al. Cognitive decline in prodromal Alzheimer disease and mild cognitive impairment. Arch Neurol 2011;68: 351-56
    • (2011) Arch Neurol , vol.68 , pp. 351-356
    • Wilson, R.S.1    Leurgans, S.E.2    Boyle, P.A.3
  • 44
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991;82:239-59
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 47
    • 60349096101 scopus 로고    scopus 로고
    • Reduction of the cerebrovascular volume in a transgenic mouse model of Alzheimer's disease
    • Bourasset F, Ouellet M, Tremblay C, et al. Reduction of the cerebrovascular volume in a transgenic mouse model of Alzheimer's disease. Neuropharmacology 2009;56:808-13
    • (2009) Neuropharmacology , vol.56 , pp. 808-813
    • Bourasset, F.1    Ouellet, M.2    Tremblay, C.3
  • 48
    • 85040709233 scopus 로고    scopus 로고
    • Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments
    • Zhang YJ, Gendron TF, Xu YF, et al. Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments. Mol Neurodegener 2010;5:33
    • (2010) Mol Neurodegener , vol.5 , pp. 33
    • Zhang, Y.J.1    Gendron, T.F.2    Xu, Y.F.3
  • 50
    • 77953024802 scopus 로고    scopus 로고
    • Prevalence of dementia disorders in the oldestold: An autopsy study
    • Jellinger KA, Attems J. Prevalence of dementia disorders in the oldestold: An autopsy study. Acta Neuropathol 2010;119:421-33
    • (2010) Acta Neuropathol , vol.119 , pp. 421-433
    • Jellinger, K.A.1    Attems, J.2
  • 51
    • 77951879099 scopus 로고    scopus 로고
    • Thinking outside the box: Alzheimertype neuropathology that does not map directly onto current consensus recommendations
    • Nelson PT, Kukull WA, Frosch MP. Thinking outside the box: Alzheimertype neuropathology that does not map directly onto current consensus recommendations. J Neuropathol Exp Neurol 2010;69:449-54
    • (2010) J Neuropathol Exp Neurol , vol.69 , pp. 449-454
    • Nelson, P.T.1    Kukull, W.A.2    Frosch, M.P.3
  • 52
    • 48249111377 scopus 로고    scopus 로고
    • Decreased drebrin mRNA expression in Alzheimer disease: Correlation with tau pathology
    • Julien C, Tremblay C, Bendjelloul F, et al. Decreased drebrin mRNA expression in Alzheimer disease: Correlation with tau pathology. J Neurosci Res 2008;86:2292-302
    • (2008) J Neurosci Res , vol.86 , pp. 2292-302
    • Julien, C.1    Tremblay, C.2    Bendjelloul, F.3
  • 53
    • 1542268242 scopus 로고    scopus 로고
    • Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function
    • DOI 10.1001/archneur.61.3.378
    • Bennett DA, Schneider JA, Wilson RS, et al. Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function. Arch Neurol 2004;61:378-84 (Pubitemid 38327357)
    • (2004) Archives of Neurology , vol.61 , Issue.3 , pp. 378-384
    • Bennett, D.A.1    Schneider, J.A.2    Wilson, R.S.3    Bienias, J.L.4    Arnold, S.E.5
  • 55
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford NJ, Zhang YJ, Baker M, et al. Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 2008;4:e1000193
    • (2008) PLoS Genet , vol.4
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3
  • 56
    • 48749088629 scopus 로고    scopus 로고
    • Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
    • Inukai Y, Nonaka T, Arai T, et al. Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett 2008;582:2899-904
    • (2008) FEBS Lett , vol.582 , pp. 2899-904
    • Inukai, Y.1    Nonaka, T.2    Arai, T.3
  • 57
    • 77949908515 scopus 로고    scopus 로고
    • Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy
    • Arai T, Hasegawa M, Nonoka T, et al. Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy. Neuropathology 2010;30:170-81
    • (2010) Neuropathology , vol.30 , pp. 170-181
    • Arai, T.1    Hasegawa, M.2    Nonoka, T.3
  • 58
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann M, Kwong LK, Lee EB, et al. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol 2009;117:137-49
    • (2009) Acta Neuropathol , vol.117 , pp. 137-149
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3
  • 60
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-[beta] precursor protein and amyloidogenic A [beta] peptide formation
    • Gervais FG, Xu D, Robertson GS, et al. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-[beta] precursor protein and amyloidogenic A [beta] peptide formation. Cell 1999;97:395-406
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1    Xu, D.2    Robertson, G.S.3
  • 64
    • 24644453571 scopus 로고    scopus 로고
    • The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death
    • LeBlanc AC. The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death. Curr Alzheimer Res 2005;2:389-402
    • (2005) Curr Alzheimer Res , vol.2 , pp. 389-402
    • Leblanc, A.C.1
  • 65
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann D, Capell A, Carlson AM, et al. Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J Neurochem 2009;110:1082-94
    • (2009) J Neurochem , vol.110 , pp. 1082-1094
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3
  • 66
    • 78651408754 scopus 로고    scopus 로고
    • Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes
    • Sephton CF, Cenik C, Kucukural A, et al. Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes. J Biol Chem 2011;286:1204-15
    • (2011) J Biol Chem , vol.286 , pp. 1204-1215
    • Sephton, C.F.1    Cenik, C.2    Kucukural, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.