메뉴 건너뛰기




Volumn 390, Issue 4, 2009, Pages 1294-1298

Overexpression of F0F1-ATP synthase α suppresses mutant huntingtin aggregation and toxicity in vitro

Author keywords

ATP synthase ; HSP; Huntingtin; Overexpression

Indexed keywords

HUNTINGTIN; POLYGLUTAMINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE ALPHA; UNCLASSIFIED DRUG;

EID: 70450253167     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.139     Document Type: Article
Times cited : (18)

References (42)
  • 2
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations
    • Wanker E. Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations. Biol Chem 381 (2000) 937-942
    • (2000) Biol Chem , vol.381 , pp. 937-942
    • Wanker, E.1
  • 4
    • 52049095054 scopus 로고    scopus 로고
    • Suppression of mutant huntingtin aggregate formation by Cdk5/p35 through the effect on microtubule stability
    • Kaminosono S., Saito T., Oyama F., Ohshima T., Asada A., Nagai Y., Nukina N., and Hisanaga S. Suppression of mutant huntingtin aggregate formation by Cdk5/p35 through the effect on microtubule stability. J. Neurosci. 28 (2008) 8747-8755
    • (2008) J. Neurosci. , vol.28 , pp. 8747-8755
    • Kaminosono, S.1    Saito, T.2    Oyama, F.3    Ohshima, T.4    Asada, A.5    Nagai, Y.6    Nukina, N.7    Hisanaga, S.8
  • 5
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • Lee W., Yoshihara M., and Littleton J. Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc. Natl. Acad. Sci. USA 101 (2004) 3224-3229
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3224-3229
    • Lee, W.1    Yoshihara, M.2    Littleton, J.3
  • 6
    • 0032897760 scopus 로고    scopus 로고
    • Impaired synaptic plasticity in mice carrying the Huntington's disease mutation
    • Usdin M., Shelbourne P., Myers R., and Madison D. Impaired synaptic plasticity in mice carrying the Huntington's disease mutation. Hum. Mol. Genet. 8 (1999) 839-846
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 839-846
    • Usdin, M.1    Shelbourne, P.2    Myers, R.3    Madison, D.4
  • 7
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross C. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 35 (2002) 819-822
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.1
  • 9
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K., Davies S., Bates G., Vonsattel J., and Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3    Davies, S.4    Bates, G.5    Vonsattel, J.6    Aronin, N.7
  • 10
    • 0034571171 scopus 로고    scopus 로고
    • Huntington's disease: the challenge for cell biologists
    • Tobin A., and Signer E. Huntington's disease: the challenge for cell biologists. Trends Cell Biol. 10 (2000) 531-536
    • (2000) Trends Cell Biol. , vol.10 , pp. 531-536
    • Tobin, A.1    Signer, E.2
  • 11
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: interaction partners tell many different stories
    • Harjes P., and Wanker E. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem. Sci. 28 (2003) 425-433
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.2
  • 13
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li S., and Li X. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet. 20 (2004) 146-154
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.1    Li, X.2
  • 14
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: an alternative approach to Huntington's disease
    • Cattaneo E., Zuccato C., and Tartari M. Normal huntingtin function: an alternative approach to Huntington's disease. Nat. Rev. Neurosci. 6 (2005) 919-930
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 17
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sánchez I., Mahlke C., and Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421 (2003) 373-379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sánchez, I.1    Mahlke, C.2    Yuan, J.3
  • 19
    • 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., Henderson B., Keene J., Strittmatter W., and Burke J. 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.4    Henderson, B.5    Keene, J.6    Strittmatter, W.7    Burke, J.8
  • 21
    • 0034738058 scopus 로고    scopus 로고
    • Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation
    • Futai M., Omote H., Sambongi Y., and Wada Y. Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation. Biochim. Biophys. Acta 1458 (2000) 276-288
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 276-288
    • Futai, M.1    Omote, H.2    Sambongi, Y.3    Wada, Y.4
  • 22
    • 0025349203 scopus 로고
    • The alpha regulatory subunit of the mitochondrial F1-ATPase complex is a heat-shock protein. Identification of two highly conserved amino acid sequences among the alpha-subunits and molecular chaperones
    • Luis A., Alconada A., and Cuezva J. The alpha regulatory subunit of the mitochondrial F1-ATPase complex is a heat-shock protein. Identification of two highly conserved amino acid sequences among the alpha-subunits and molecular chaperones. J. Biol. Chem. 265 (1990) 7713-7716
    • (1990) J. Biol. Chem. , vol.265 , pp. 7713-7716
    • Luis, A.1    Alconada, A.2    Cuezva, J.3
  • 23
    • 0025341052 scopus 로고
    • Identification of a 66 kDa protein associated with yeast mitochondrial ATP synthase as heat shock protein hsp60
    • Gray R., Grasso D., Maxwell R., Finnegan P., Nagley P., and Devenish R. Identification of a 66 kDa protein associated with yeast mitochondrial ATP synthase as heat shock protein hsp60. FEBS Lett. 268 (1990) 265-268
    • (1990) FEBS Lett. , vol.268 , pp. 265-268
    • Gray, R.1    Grasso, D.2    Maxwell, R.3    Finnegan, P.4    Nagley, P.5    Devenish, R.6
  • 24
    • 33947205041 scopus 로고    scopus 로고
    • Abnormal levels of prohibitin and ATP synthase in the substantia nigra and frontal cortex in Parkinson's disease
    • Ferrer I., Perez E., Dalfó E., and Barrachina M. Abnormal levels of prohibitin and ATP synthase in the substantia nigra and frontal cortex in Parkinson's disease. Neurosci. Lett. 415 (2007) 205-209
    • (2007) Neurosci. Lett. , vol.415 , pp. 205-209
    • Ferrer, I.1    Perez, E.2    Dalfó, E.3    Barrachina, M.4
  • 26
    • 51949099008 scopus 로고    scopus 로고
    • Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells
    • Schmidt C., Lepsverdize E., Chi S., Das A., Pizzo S., Dityatev A., and Schachner M. Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells. Mol. Psychiatry 13 (2008) 953-969
    • (2008) Mol. Psychiatry , vol.13 , pp. 953-969
    • Schmidt, C.1    Lepsverdize, E.2    Chi, S.3    Das, A.4    Pizzo, S.5    Dityatev, A.6    Schachner, M.7
  • 27
    • 13844266044 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondria from primary neuron cultures treated with amyloid beta peptide
    • Lovell M., Xiong S., Markesbery W., and Lynn B. Quantitative proteomic analysis of mitochondria from primary neuron cultures treated with amyloid beta peptide. Neurochem. Res. 30 (2005) 113-122
    • (2005) Neurochem. Res. , vol.30 , pp. 113-122
    • Lovell, M.1    Xiong, S.2    Markesbery, W.3    Lynn, B.4
  • 29
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana N., Tanaka M., Wang G., and Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9 (2000) 2009-2018
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 30
    • 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., and Rubinsztein D. 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.5    Rubinsztein, D.6
  • 31
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y., Kume A., Li M., Doyu M., Hata M., Ohtsuka K., and Sobue G. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J. Biol. Chem. 275 (2000) 8772-8778
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 32
    • 34548608465 scopus 로고    scopus 로고
    • Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine
    • Rujano M., Kampinga H., and Salomons F. Modulation of polyglutamine inclusion formation by the Hsp70 chaperone machine. Exp. Cell Res. 313 (2007) 3568-3578
    • (2007) Exp. Cell Res. , vol.313 , pp. 3568-3578
    • Rujano, M.1    Kampinga, H.2    Salomons, F.3
  • 33
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings C., Sun Y., Opal P., Antalffy B., Mestril R., Orr H., Dillmann W., and Zoghbi H. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10 (2001) 1511-1518
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.6    Dillmann, W.7    Zoghbi, H.8
  • 34
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick J., Chan H., Gray-Board G., Chai Y., Paulson H., and Bonini N. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 23 (1999) 425-428
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.1    Chan, H.2    Gray-Board, G.3    Chai, Y.4    Paulson, H.5    Bonini, N.6
  • 35
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y., Koppenhafer S., Bonini N., and Paulson H. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 19 (1999) 10338-10347
    • (1999) J. Neurosci. , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.2    Bonini, N.3    Paulson, H.4
  • 36
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan H., Warrick J., Gray-Board G., Paulson H., and Bonini N. Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet. 9 (2000) 2811-2820
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.1    Warrick, J.2    Gray-Board, G.3    Paulson, H.4    Bonini, N.5
  • 37
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H., Katsuno M., Minamiyama M., Sang C., Pagoulatos G., Angelidis C., Kusakabe M., Yoshiki A., Kobayashi Y., Doyu M., and Sobue G. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. 23 (2003) 2203-2211
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10    Sobue, G.11
  • 40
    • 32644481227 scopus 로고    scopus 로고
    • Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction
    • Goswami A., Dikshit P., Mishra A., Mulherkar S., Nukina N., and Jana N. Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction. Biochem. Biophys. Res. Commun. 342 (2006) 184-190
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 184-190
    • Goswami, A.1    Dikshit, P.2    Mishra, A.3    Mulherkar, S.4    Nukina, N.5    Jana, N.6
  • 41
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana N., Dikshit P., Goswami A., Kotliarova S., Murata S., Tanaka K., and Nukina N. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 280 (2005) 11635-11640
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.