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Volumn 377, Issue 2, 2008, Pages 550-555

ER stress is the initial response to polyglutamine toxicity in PC12 cells

Author keywords

ER stress; PC12 cells; Polyglutamine; Proteasome; Ubiquitin; UPS

Indexed keywords

CASPASE 3; HYBRID PROTEIN; LACTACYSTIN; POLYGLUTAMINE; PROTEASOME; STRESS ACTIVATED PROTEIN KINASE; UBIQUITIN;

EID: 55649099810     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.006     Document Type: Article
Times cited : (13)

References (23)
  • 2
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. ER stress and diseases. FEBS J. 274 (2007) 630-658
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 3
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr H.Y., and Zoghbi H.Y. Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30 (2007) 575-621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.Y.1    Zoghbi, H.Y.2
  • 4
    • 12144280807 scopus 로고    scopus 로고
    • Polyglutamine disease and transport problems
    • Gunawardena S., and Goldstein L.S.B. Polyglutamine disease and transport problems. Arch. Neurol. 62 (2005) 46-51
    • (2005) Arch. Neurol. , vol.62 , pp. 46-51
    • Gunawardena, S.1    Goldstein, L.S.B.2
  • 5
    • 33747359908 scopus 로고    scopus 로고
    • Polyglutamine neurodegenerative diseases and regulation of transcription: assembling the puzzle
    • Riley B.E., and Orr H.T. Polyglutamine neurodegenerative diseases and regulation of transcription: assembling the puzzle. Genes Dev. 20 (2006) 2183-2192
    • (2006) Genes Dev. , vol.20 , pp. 2183-2192
    • Riley, B.E.1    Orr, H.T.2
  • 6
    • 34548331451 scopus 로고    scopus 로고
    • Is the ubiquitin-proteasome system impaired in Huntington's disease?
    • Ortega Z., Díaz-Hernández M., and Lucas J.J. Is the ubiquitin-proteasome system impaired in Huntington's disease?. Cell. Mol. Life Sci. 64 (2007) 2245-2257
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2245-2257
    • Ortega, Z.1    Díaz-Hernández, M.2    Lucas, J.J.3
  • 7
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef L.G., Lindsten K., Masucci M.G., and Dantuma N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11 (2002) 2689-2700
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 8
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., and Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16 (2002) 1345-1355
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 9
    • 29644433718 scopus 로고    scopus 로고
    • Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGγ as a therapeutic target
    • Bett J.S., Goellner G.M., Woodman B., Pratt G., Rechsteiner M., and Bates G.P. Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGγ as a therapeutic target. Hum. Mol. Genet. 15 (2005) 33-44
    • (2005) Hum. Mol. Genet. , vol.15 , pp. 33-44
    • Bett, J.S.1    Goellner, G.M.2    Woodman, B.3    Pratt, G.4    Rechsteiner, M.5    Bates, G.P.6
  • 10
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman A.B., Yoo S.Y., Dantuma N.P., and Zoghbi H.Y. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet. 14 (2005) 679-691
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 13
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen S., Putkonen N., Norremolle A., Lindholm D., and Korhornen L. Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp. Cell Res. 314 (2008) 950-960
    • (2008) Exp. Cell Res. , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhornen, L.5
  • 14
    • 0034615932 scopus 로고    scopus 로고
    • Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening
    • Nagai Y., Tucker T., Ren H., Kenan D.J., Henderson B.S., Keene J.D., Strittmatter W.J., and Burke J.R. Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J. Biol. Chem. 275 (2000) 10437-10442
    • (2000) J. Biol. Chem. , vol.275 , pp. 10437-10442
    • Nagai, Y.1    Tucker, T.2    Ren, H.3    Kenan, D.J.4    Henderson, B.S.5    Keene, J.D.6    Strittmatter, W.J.7    Burke, J.R.8
  • 15
    • 22244459510 scopus 로고    scopus 로고
    • Humanin attenuates apoptosis induced by DRPLA proteins with expanded polyglutamine stretches
    • Kariya S., Hirano M., Nagai Y., Furuya Y., Fujikake N., Toda T., and Ueno S. Humanin attenuates apoptosis induced by DRPLA proteins with expanded polyglutamine stretches. J. Mol. Neurosci. 25 (2005) 165-169
    • (2005) J. Mol. Neurosci. , vol.25 , pp. 165-169
    • Kariya, S.1    Hirano, M.2    Nagai, Y.3    Furuya, Y.4    Fujikake, N.5    Toda, T.6    Ueno, S.7
  • 16
    • 0034763702 scopus 로고    scopus 로고
    • Nicotine-induced phosphorylation of extracellular signal-regulated protein kinase and CREB in PC12h cells
    • Nakayama H., Numakawa T., Ikeuchi T., and Hatanaka H. Nicotine-induced phosphorylation of extracellular signal-regulated protein kinase and CREB in PC12h cells. J. Neurochem. 79 (2001) 489-498
    • (2001) J. Neurochem. , vol.79 , pp. 489-498
    • Nakayama, H.1    Numakawa, T.2    Ikeuchi, T.3    Hatanaka, H.4
  • 18
    • 20444378891 scopus 로고    scopus 로고
    • The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor
    • Thomas M., Yu Z., Dadgar N., Varambally S., Yu J., Chinnaiyan A.M., and Lieberman A.P. The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor. J. Biol. Chem. 280 (2005) 21264-21271
    • (2005) J. Biol. Chem. , vol.280 , pp. 21264-21271
    • Thomas, M.1    Yu, Z.2    Dadgar, N.3    Varambally, S.4    Yu, J.5    Chinnaiyan, A.M.6    Lieberman, A.P.7
  • 22
    • 33747891213 scopus 로고    scopus 로고
    • Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
    • Zhong X., and Pittman R.N. Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Hum. Mol. Genet. 15 (2006) 2409-2420
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2409-2420
    • Zhong, X.1    Pittman, R.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.