메뉴 건너뛰기




Volumn 454, Issue 2, 2009, Pages 152-156

Decreased protein synthesis of Hsp27 associated with cellular toxicity in a cell model of Machado-Joseph disease

Author keywords

Heat shock protein 27; Machado Joseph disease; Mutant ataxin 3; Protease inhibitor; Protein synthesis

Indexed keywords

ATAXIN 3; HEAT SHOCK PROTEIN 27; METHIONINE; PROTEASOME; SULFUR 35;

EID: 62949154852     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2009.03.004     Document Type: Article
Times cited : (24)

References (23)
  • 1
    • 0033624419 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative disease
    • Albers D.S., and Beal M.F. Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative disease. J. Neural. Transm. Suppl. 59 (2000) 133-154
    • (2000) J. Neural. Transm. Suppl. , vol.59 , pp. 133-154
    • Albers, D.S.1    Beal, M.F.2
  • 2
    • 11844257596 scopus 로고    scopus 로고
    • Cytotoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression
    • Arrigo A.P., Firdaus W.J., Mellier G., Moulin M., Paul C., Diaz-latoud C., and Kretz-remy C. Cytotoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression. Methods 35 (2005) 126-138
    • (2005) Methods , vol.35 , pp. 126-138
    • Arrigo, A.P.1    Firdaus, W.J.2    Mellier, G.3    Moulin, M.4    Paul, C.5    Diaz-latoud, C.6    Kretz-remy, C.7
  • 3
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B., Li F., and Pittman R.N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 12 (2003) 3195-3205
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 5
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding W.X., Ni H.M., Gao W., Yoshimori T., Stolz D.B., Ron D., and Yin X.M. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am. J. Pathol. 171 (2007) 513-524
    • (2007) Am. J. Pathol. , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 6
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • Doss-Pepe E.W., Stenroos E.S., Johnson W.G., and Madura K. Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol. Cell Biol. 23 (2003) 6469-6483
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 7
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graber S., Gaestel M., and Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16 (1997) 221-229
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 8
    • 34547129609 scopus 로고    scopus 로고
    • Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3
    • Haacke A., Hartl F.U., and Breuer P. Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. J. Biol. Chem. 282 (2007) 18851-18856
    • (2007) J. Biol. Chem. , vol.282 , pp. 18851-18856
    • Haacke, A.1    Hartl, F.U.2    Breuer, P.3
  • 9
  • 12
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel K.B., Kim M., Sapp E., McIntyre C., Castaño J.G., Aronin N., and DiFiglia M. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J. Neurosci. 20 (2000) 7268-7278
    • (2000) J. Neurosci. , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castaño, J.G.5    Aronin, N.6    DiFiglia, M.7
  • 13
    • 34547581106 scopus 로고    scopus 로고
    • Regulation of adipocyte lipolysis by degradation of the perilipin protein: nelfinavir enhances lysosome-mediated perilipin proteolysis
    • Kovsan J., Ben-Romano R., Souza S.C., Greenberg A.S., and Rudich A. Regulation of adipocyte lipolysis by degradation of the perilipin protein: nelfinavir enhances lysosome-mediated perilipin proteolysis. J. Biol. Chem. 282 (2007) 21704-21711
    • (2007) J. Biol. Chem. , vol.282 , pp. 21704-21711
    • Kovsan, J.1    Ben-Romano, R.2    Souza, S.C.3    Greenberg, A.S.4    Rudich, A.5
  • 14
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells
    • Mehlen P., Hickey E., Weber L.A., and Arrigo A.P. Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells. Biochem. Biophys. Res. Commun. 241 (1997) 187-192
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 15
    • 23044507689 scopus 로고    scopus 로고
    • Decreased expression of Hsp27 and Hsp70 in transformed lymphoblastoid cells from patients with spinocerebellar ataxia type 7
    • Tsai H.F., Lin S.J., Li C., and Hsieh M. Decreased expression of Hsp27 and Hsp70 in transformed lymphoblastoid cells from patients with spinocerebellar ataxia type 7. Biochem. Biophys. Res. Commun. 334 (2005) 1279-1286
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1279-1286
    • Tsai, H.F.1    Lin, S.J.2    Li, C.3    Hsieh, M.4
  • 16
    • 14344262672 scopus 로고    scopus 로고
    • Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells
    • Tsai H.F., Tsai H.J., and Hsieh M. Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells. Biochem. Biophys. Res. Commun. 324 (2004) 1274-1282
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1274-1282
    • Tsai, H.F.1    Tsai, H.J.2    Hsieh, M.3
  • 20
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3
    • Wen F.C., Li Y.H., Tsai H.F., Lin C.H., Li C., Liu C.S., Lii C.K., Nukina N., and Hsieh M. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. FEBS Lett. 546 (2003) 307-314
    • (2003) FEBS Lett. , vol.546 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3    Lin, C.H.4    Li, C.5    Liu, C.S.6    Lii, C.K.7    Nukina, N.8    Hsieh, M.9
  • 21
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by Huntingtin
    • Wyttenbach A., Sauvageot O., Carmichael J., Diaz-Latoud C., Arrigo A.P., and Rubinsztein D.C. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by Huntingtin. Hum. Mol. Genet. 11 (2002) 1137-1151
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 23
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi H.Y., and Orr H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23 (2000) 217-247
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.