메뉴 건너뛰기




Volumn 226, Issue 5, 2012, Pages 693-702

The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies

Author keywords

Endoplasmic reticulum stress; Frontotemporal lobar degeneration; Tau; Unfolded protein response

Indexed keywords

PANCREATIC ENDOPLASMIC RETICULUM KINASE; PHOSPHOTRANSFERASE; PROTEIN IRE1; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84858000638     PISSN: 00223417     EISSN: 10969896     Source Type: Journal    
DOI: 10.1002/path.3969     Document Type: Article
Times cited : (149)

References (29)
  • 1
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74: 739-789. (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 2
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • DOI 10.1038/nrn2194, PII NRN2194
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nature Rev Neurosci 2007; 8: 663-672. (Pubitemid 47283144)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 3
    • 5044235577 scopus 로고    scopus 로고
    • The role of tau (MAPT) in frontotemporal dementia and related tauopathies
    • DOI 10.1002/humu.20086
    • Rademakers R, Cruts M, Van Broeckhoven C. The role of tau (MAPT) in frontotemporal dementia and related tauopathies. Hum Mutat 2004; 24: 277-295. (Pubitemid 39336634)
    • (2004) Human Mutation , vol.24 , Issue.4 , pp. 277-295
    • Rademakers, R.1    Cruts, M.2    Van Broeckhoven, C.3
  • 4
    • 65349093893 scopus 로고    scopus 로고
    • The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus
    • Hoozemans JJ, Van Haastert ES, Nijholt DA, et al . The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus. Am J Pathol 2009; 174: 1241-1251.
    • (2009) Am J Pathol , vol.174 , pp. 1241-1251
    • Hoozemans, J.J.1    Van Haastert, E.S.2    Nijholt, D.A.3
  • 5
    • 77956288847 scopus 로고    scopus 로고
    • Activation of PERK signaling attenuates Aβ-mediated ER stress
    • Lee dY, Lee KS, Lee HJ, et al . Activation of PERK signaling attenuates Aβ-mediated ER stress. PLoS One 2010; 5: e10489.
    • (2010) PLoS One , vol.5
    • Lee, D.Y.1    Lee, K.S.2    Lee, H.J.3
  • 6
    • 84856951448 scopus 로고    scopus 로고
    • Amyloid beta-induced ER stress is enhanced under mitochondrial dysfunction conditions
    • doi:10.1016/j.neurobiolaging.2011.04.011
    • Costa RO, Ferreiro E, Martins I, et al . Amyloid beta-induced ER stress is enhanced under mitochondrial dysfunction conditions. Neurobiol Aging doi:10.1016/j.neurobiolaging.2011.04.011
    • Neurobiol Aging
    • Costa, R.O.1    Ferreiro, E.2    Martins, I.3
  • 7
    • 35848951621 scopus 로고    scopus 로고
    • 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner
    • DOI 10.1089/ars.2007.1797
    • Chafekar SM, Hoozemans JJ, Zwart R, et al . Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antioxid Redox Signal 2007; 9: 2245-2254. (Pubitemid 350059019)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2245-2254
    • Chafekar, S.M.1    Hoozemans, J.J.M.2    Zwart, R.3    Baas, F.4    Scheper, W.5
  • 9
    • 77951937629 scopus 로고    scopus 로고
    • Depletion of oxidative and endoplasmic reticulum stress regulators in Pick disease
    • Ilieva EV, Naudi A, Kichev A, et al . Depletion of oxidative and endoplasmic reticulum stress regulators in Pick disease. Free Radic Biol Med 2010; 48: 1302-1310.
    • (2010) Free Radic Biol Med , vol.48 , pp. 1302-1310
    • Ilieva, E.V.1    Naudi, A.2    Kichev, A.3
  • 10
    • 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
  • 11
    • 77953516041 scopus 로고    scopus 로고
    • Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction
    • Spatara ML, Robinson AS. Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction. J Neurosci Res 2010; 88: 1951-1961.
    • (2010) J Neurosci Res , vol.88 , pp. 1951-1961
    • Spatara, M.L.1    Robinson, A.S.2
  • 12
    • 78650469377 scopus 로고    scopus 로고
    • LiCl attenuates thapsigargin-induced tau hyperphosphorylation by inhibiting GSK-3β in vivo and in vitro
    • Fu ZQ, Yang Y, Song J, et al . LiCl attenuates thapsigargin-induced tau hyperphosphorylation by inhibiting GSK-3β in vivo and in vitro. J Alzheimers Dis 2010; 21: 1107-1117.
    • (2010) J Alzheimers Dis , vol.21 , pp. 1107-1117
    • Fu, Z.Q.1    Yang, Y.2    Song, J.3
  • 13
    • 68149164274 scopus 로고    scopus 로고
    • Isoflavones prevent endoplasmic reticulum stress-mediated neuronal degeneration by inhibiting tau hyperphosphorylation in SH-SY5Y cells
    • Park YJ, Jang YM, Kwon YH. Isoflavones prevent endoplasmic reticulum stress-mediated neuronal degeneration by inhibiting tau hyperphosphorylation in SH-SY5Y cells. J Med Food 2009; 12: 528-535.
    • (2009) J Med Food , vol.12 , pp. 528-535
    • Park, Y.J.1    Jang, Y.M.2    Kwon, Y.H.3
  • 14
    • 48249157930 scopus 로고    scopus 로고
    • ER stress is involved in Aβ-induced GSK-3β activation and tau phosphorylation
    • Resende R, Ferreiro E, Pereira C, et al . ER stress is involved in Aβ-induced GSK-3β activation and tau phosphorylation. J Neurosci Res 2008; 86: 2091-2099.
    • (2008) J Neurosci Res , vol.86 , pp. 2091-2099
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3
  • 15
    • 14044261099 scopus 로고    scopus 로고
    • Valproate protects cells fom ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3
    • DOI 10.1242/jcs.01562
    • Kim AJ, Shi Y, Austin RC, et al . Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3. J Cell Sci 2005; 118: 89-99. (Pubitemid 40277107)
    • (2005) Journal of Cell Science , vol.118 , Issue.1 , pp. 89-99
    • Kim, A.J.1    Shi, Y.2    Austin, R.C.3    Werstuck, G.H.4
  • 16
    • 0037160134 scopus 로고    scopus 로고
    • Central role of glycogen synthase kinase-3β in endoplasmic reticulum stress-induced caspase-3 activation
    • DOI 10.1074/jbc.M206047200
    • Song L, De Sarno P, Jope RS. Central role of glycogen synthase kinase-3β in endoplasmic reticulum stress-induced caspase-3 activation. J Biol Chem 2002; 277: 44701-44708. (Pubitemid 36159060)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44701-44708
    • Song, L.1    De Sarno, P.2    Jope, R.S.3
  • 17
    • 79959689333 scopus 로고    scopus 로고
    • Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy
    • Hoglinger GU, Melhem NM, Dickson DW, et al . Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy. Nature Genet 2011; 43: 699-705.
    • (2011) Nature Genet , vol.43 , pp. 699-705
    • Hoglinger, G.U.1    Melhem, N.M.2    Dickson, D.W.3
  • 18
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, Neumann M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 2010; 9: 995-1007.
    • (2010) Lancet Neurol , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 19
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import
    • Dormann D, Rodde R, Edbauer D, et al . ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 2010; 29: 2841-2857.
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3
  • 21
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue
    • Liu-Yesucevitz L, Bilgutay A, Zhang YJ, et al . Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS One 2010; 5: e13250.
    • (2010) PLoS One , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3
  • 22
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch WE, Morimoto RI, Dillin A, et al . Adapting proteostasis for disease intervention. Science 2008; 319: 916-919. (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 24
    • 0026454255 scopus 로고
    • Granulovacuolar degeneration in the hippocampal cortex of aging and demented patients - A quantitative study
    • Xu M, Shibayama H, Kobayashi H, et al . Granulovacuolar degeneration in the hippocampal cortex of aging and demented patients - a quantitative study. Acta Neuropathol (Berlin) 1992; 85: 1-9.
    • (1992) Acta Neuropathol (Berlin) , vol.85 , pp. 1-9
    • Xu, M.1    Shibayama, H.2    Kobayashi, H.3
  • 25
    • 0038326624 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment
    • DOI 10.1001/archneur.60.5.729
    • Guillozet AL, Weintraub S, Mash DC, et al . Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment. Arch Neurol 2003; 60: 729-736. (Pubitemid 36569891)
    • (2003) Archives of Neurology , vol.60 , Issue.5 , pp. 729-736
    • Guillozet, A.L.1    Weintraub, S.2    Mash, D.C.3    Marsel, M.M.4
  • 26
    • 0034622242 scopus 로고    scopus 로고
    • Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases
    • DOI 10.1016/S0197-4580(00)00110-X, PII S019745800000110X
    • Schwab C, DeMaggio AJ, Ghoshal N, et al . Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiol Aging 2000; 21: 503-510. (Pubitemid 30621488)
    • (2000) Neurobiology of Aging , vol.21 , Issue.4 , pp. 503-510
    • Schwab, C.1    Demaggio, A.J.2    Ghoshal, N.3    Binder, L.I.4    Kuret, J.5    McGeer, P.L.6
  • 28
    • 79961124071 scopus 로고    scopus 로고
    • The unfolded protein response and proteostasis in Alzheimer disease: Preferential activation of autophagy by endoplasmic reticulum stress
    • Scheper W, Nijholt DA, Hoozemans JJ. The unfolded protein response and proteostasis in Alzheimer disease: preferential activation of autophagy by endoplasmic reticulum stress. Autophagy 2011; 7: 910-911.
    • (2011) Autophagy , vol.7 , pp. 910-911
    • Scheper, W.1    Nijholt, D.A.2    Hoozemans, J.J.3
  • 29
    • 79955804227 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates autophagy but not the proteasome in neuronal cells: Implications for Alzheimer's disease
    • Nijholt DA, de Graaf TR, Van Haastert ES, et al . Endoplasmic reticulum stress activates autophagy but not the proteasome in neuronal cells: implications for Alzheimer's disease. Cell Death Differ 2011; 18: 1071-1081.
    • (2011) Cell Death Differ , vol.18 , pp. 1071-1081
    • Nijholt, D.A.1    De Graaf, T.R.2    Van Haastert, E.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.