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Volumn 12, Issue 9, 2003, Pages 985-994

Raised intracellular glucose concentrations reduce aggredation and cell death caused by mutant huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLGLUCOSE; ADENINE; CYTOSINE; DEOXYGLUCOSE; GLUCOSE; GLUCOSE 6 PHOSPHATE; GLUCOSE TRANSPORTER 1; GUANINE; HUNTINGTIN; POLYGLUTAMINE; PROTEIN KINASE B; RAPAMYCIN; REGULATOR PROTEIN; S6 KINASE;

EID: 0038364056     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/ddg109     Document Type: Review
Times cited : (111)

References (30)
  • 1
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Huntington's disease
    • Rubinsztein, D.C. (2002) Lessons from animal models of Huntington's disease. Trends. Genet., 18, 202-209.
    • (2002) Trends Genet. , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 2
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes, A., Lindenberg, K.S., Ben-Haiem, L., Weber, C., Devys, D., Landwehrmeyer, G.B., Mandel, J.L. and Trottier, Y. (2002) Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell, 10, 259-269.
    • (2002) Mol. Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6    Mandel, J.L.7    Trottier, Y.8
  • 4
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R. and Rubinsztein, D.C. (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet., 11, 1107-1117.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 5
    • 0033791650 scopus 로고    scopus 로고
    • Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells
    • Kim, J. and Klionsky, D.J. (2000) Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells. A. Rev. Biochem., 69, 303-342.
    • (2000) A. Rev. Biochem. , vol.69 , pp. 303-342
    • Kim, J.1    Klionsky, D.J.2
  • 6
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomallysosomal activity, endosomal tubulation and autophagy
    • Kegel, K.B., Kim, M., Sapp, E., McIntyre, C., Castano, J.G., Aronin, N. and DiFiglia, M. (2000) Huntingtin expression stimulates endosomallysosomal activity, endosomal tubulation and autophagy. J. Neurosci., 20, 7268-7278.
    • (2000) J. Neurosci. , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6    DiFiglia, M.7
  • 7
    • 0036792019 scopus 로고    scopus 로고
    • Involvement of lysosomes in the pathogenesis of CAG repeat diseases
    • Yamada, M., Tsuji, S. and Takahashi, H. (2002) Involvement of lysosomes in the pathogenesis of CAG repeat diseases. Ann. Neurol., 52, 498-503.
    • (2002) Ann. Neurol. , vol.52 , pp. 498-503
    • Yamada, M.1    Tsuji, S.2    Takahashi, H.3
  • 8
    • 0036569331 scopus 로고    scopus 로고
    • Yeast autophagosomes: De novo formation of a membrane structure
    • Noda, T., Suzuki, K. and Ohsumi, Y. (2002) Yeast autophagosomes: de novo formation of a membrane structure. Trends Cell Biol., 12, 231-235.
    • (2002) Trends Cell Biol. , vol.12 , pp. 231-235
    • Noda, T.1    Suzuki, K.2    Ohsumi, Y.3
  • 9
    • 0034703021 scopus 로고    scopus 로고
    • Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway
    • Mordier, S., Deval, C., Bechet, D., Tassa, A. and Ferrara, M. (2000) Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway. J. Biol. Chem., 275, 29900-29906.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29900-29906
    • Mordier, S.1    Deval, C.2    Bechet, D.3    Tassa, A.4    Ferrara, M.5
  • 10
    • 0017816161 scopus 로고
    • Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy
    • Pfeifer, U. (1978) Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy. J. Cell Biol., 78, 152-167.
    • (1978) J. Cell Biol. , vol.78 , pp. 152-167
    • Pfeifer, U.1
  • 11
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • Hara, K., Yonezawa, K., Weng, Q.P., Kozlowski, M.T., Belham, C. and Avruch, J. (1998) Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem., 273, 14484-14494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 12
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle, T. and Hall, M.N. (2000) TOR, a central controller of cell growth. Cell, 103, 253-262.
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 13
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B.T., Ouwens, D.M., Withers, D.J., Alessi, D.R. and Shepherd, P.R. (1999) Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J., 344, 427-431.
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, D.M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 14
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signalling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulic, A., Hudson, C.C., Homme, J.L., Yin, P., Otterness, D.M., Karnitz, L.M. and Abraham, R.T. (2000) A direct linkage between the phosphoinositide 3-kinase-AKT signalling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res., 60, 3504-3513.
    • (2000) Cancer Res. , vol.60 , pp. 3504-3513
    • Sekulic, A.1    Hudson, C.C.2    Homme, J.L.3    Yin, P.4    Otterness, D.M.5    Karnitz, L.M.6    Abraham, R.T.7
  • 15
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, A., Raught, B. and Sonenberg, N. (2001) Regulation of translation initiation by FRAP/mTOR. Genes Dev., 15, 807-826.
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.1    Raught, B.2    Sonenberg, N.3
  • 18
    • 0033607531 scopus 로고    scopus 로고
    • Immunopurified mammalian target of rapamycin phosphorylates and activates p7O S6 kinase alpha in vitro
    • Isotani, S., Hara, K., Tokunaga, C., Inoue, H., Avruch, J. and Yonezawa, K. (1999) Immunopurified mammalian target of rapamycin phosphorylates and activates p7O S6 kinase alpha in vitro. J. Biol. Chem., 274, 34493-34498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34493-34498
    • Isotani, S.1    Hara, K.2    Tokunaga, C.3    Inoue, H.4    Avruch, J.5    Yonezawa, K.6
  • 19
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart, E.F., Luiken, J.J., Blommaart, P.J., van Woerkom, G.M. and Meijer, A.J. (1995) Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem., 270, 2320-2326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    van Woerkom, G.M.4    Meijer, A.J.5
  • 20
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky, D.J. and Emr, S.D. (2000) Autophagy as a regulated pathway of cellular degradation. Science, 290, 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 22
    • 0034662915 scopus 로고    scopus 로고
    • Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease
    • Carmichael, J., Chatellier, J., Woolfson, A., Milstein, C., Fersht, A.R. and Rubinsztein, D.C. (2000) Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease. Proc. Natl Acad. Sci. USA, 97, 9701-9705.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9701-9705
    • Carmichael, J.1    Chatellier, J.2    Woolfson, A.3    Milstein, C.4    Fersht, A.R.5    Rubinsztein, D.C.6
  • 23
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • Wyttenbach, A., Swartz, J., Kita, H., Thykjaer, T., Carmichael, J., Bradley, J., Brown, R., Maxwell, M., Schapira, A., Orntoft, T.F. et al. (2001) Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum. Mol. Genet., 10, 1829-1845.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3    Thykjaer, T.4    Carmichael, J.5    Bradley, J.6    Brown, R.7    Maxwell, M.8    Schapira, A.9    Orntoft, T.F.10
  • 24
    • 0035395894 scopus 로고    scopus 로고
    • Glucose regulates protein catabolism in ras-transformed fibroblasts through a lysosomal-dependent proteolytic pathway
    • Tournu, C., Obled, A., Roux, M.P., Ferrara, M., Omura, S. and Bechet, D.M. (2001) Glucose regulates protein catabolism in ras-transformed fibroblasts through a lysosomal-dependent proteolytic pathway. Biochem. J., 357, 255-261.
    • (2001) Biochem. J. , vol.357 , pp. 255-261
    • Tournu, C.1    Obled, A.2    Roux, M.P.3    Ferrara, M.4    Omura, S.5    Bechet, D.M.6
  • 25
    • 0028836002 scopus 로고
    • Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles
    • Biederbick, A., Kern, H.F. and Elsasser, H.P. (1995) Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles. Eur. J. Cell Biol., 66, 3-14.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 26
    • 0033997045 scopus 로고    scopus 로고
    • The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe
    • Niemann, A., Takatsuki, A. and Elsasser, H.P. (2000) The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe. J. Histochem. Cytochem., 48, 251-258.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 251-258
    • Niemann, A.1    Takatsuki, A.2    Elsasser, H.P.3
  • 27
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafo, D.B. and Colombo, M.I. (2001) A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation. J. Cell Sci., 114, 3619-3629.
    • (2001) J. Cell Sci. , vol.114 , pp. 3619-3629
    • Munafo, D.B.1    Colombo, M.I.2
  • 29
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species causes by Huntingtin
    • Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A.P. and Rubinsztein, D.C. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species causes by Huntingtin. Hum. Mol. Genet., 11, 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
  • 30
    • 0030783009 scopus 로고    scopus 로고
    • Dense core lysosomes can fuse with late endosomes and are re-formed from the resultant hybrid organelles
    • Bright, N.A., Reaves, B.J., Mullock, B.M. and Luzio, J.P. (1997) Dense core lysosomes can fuse with late endosomes and are re-formed from the resultant hybrid organelles. J. Cell Sci., 110, 2027-2040.
    • (1997) J. Cell Sci. , vol.110 , pp. 2027-2040
    • Bright, N.A.1    Reaves, B.J.2    Mullock, B.M.3    Luzio, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.