메뉴 건너뛰기




Volumn 19, Issue 17, 2010, Pages 3372-3382

Increased energy metabolism rescues glia-induced pathology in a Drosophila model of Huntington's disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CATALASE; GLUCOSE TRANSPORTER 1; MANGANESE SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 5;

EID: 77955376527     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddq249     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 0033007867 scopus 로고    scopus 로고
    • Expression of the Huntington's disease gene is regulated in astrocytes in the arcuate nucleus of the hypothalamus of postpartum rats
    • Hebb, M.O., Denovan-Wright, E.M. and Robertson, H.A. (1999) Expression of the Huntington's disease gene is regulated in astrocytes in the arcuate nucleus of the hypothalamus of postpartum rats. FASEB J., 13, 1099-1106.
    • (1999) FASEB J. , vol.13 , pp. 1099-1106
    • Hebb, M.O.1    Denovan-Wright, E.M.2    Robertson, H.A.3
  • 2
    • 29144460321 scopus 로고    scopus 로고
    • Expression of mutant Huntingtin in glial cells contributes to neuronal excitotoxicity
    • Shin, J.Y., Fang, Z.H., Yu, Z.X., Wang, C.E., Li, S.H. and Li, X.J. (2005) Expression of mutant Huntingtin in glial cells contributes to neuronal excitotoxicity. J. Cell Biol., 171, 1001-1012.
    • (2005) J. Cell Biol. , vol.171 , pp. 1001-1012
    • Shin, J.Y.1    Fang, Z.H.2    Yu, Z.X.3    Wang, C.E.4    Li, S.H.5    Li, X.J.6
  • 3
    • 40549084657 scopus 로고    scopus 로고
    • AKT-sensitive or insensitive pathways of toxicity in glial cells and neurons in Drosophila models of Huntington's disease
    • Liévens, J.C., Iché, M., Laval, M., Faivre-Sarrailh, C. and Birman, S. (2008) AKT-sensitive or insensitive pathways of toxicity in glial cells and neurons in Drosophila models of Huntington's disease. Hum. Mol. Genet., 17, 882-894.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 882-894
    • Liévens, J.C.1    Iché, M.2    Laval, M.3    Faivre-Sarrailh, C.4    Birman, S.5
  • 4
    • 59249101029 scopus 로고    scopus 로고
    • Glial cell lineage expression of mutant ataxin-1 and Huntingtin induces developmental and late-onset neuronal pathologies in Drosophila models
    • Tamura, T., Sone, M., Yamashita, M., Wanker, E.E. and Okazawa, H. (2009) Glial cell lineage expression of mutant ataxin-1 and Huntingtin induces developmental and late-onset neuronal pathologies in Drosophila models. PLoS ONE, 4, e4262.
    • (2009) PLoS ONE , vol.4
    • Tamura, T.1    Sone, M.2    Yamashita, M.3    Wanker, E.E.4    Okazawa, H.5
  • 5
    • 76049118058 scopus 로고    scopus 로고
    • Expression of mutant Huntingtin in mouse brain astrocytes causes age-dependent neurological symptoms
    • Bradford, J., Shin, J.Y., Roberts, M., Wang, C.E., Li, X.J. and Li, S. (2009) Expression of mutant Huntingtin in mouse brain astrocytes causes age-dependent neurological symptoms. Proc. Natl Acad. Sci. USA, 106, 22480-22485.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 22480-22485
    • Bradford, J.1    Shin, J.Y.2    Roberts, M.3    Wang, C.E.4    Li, X.J.5    Li, S.6
  • 7
    • 0036345741 scopus 로고    scopus 로고
    • Impaired glutamate transport and glutamate-glutamine cycling: downstream effects of the Huntington mutation
    • Behrens, P.F., Franz, P., Woodman, B., Lindenberg, K.S. and Landwehrmeyer, G.B. (2002) Impaired glutamate transport and glutamate-glutamine cycling: downstream effects of the Huntington mutation. Brain, 125, 1908-1922.
    • (2002) Brain , vol.125 , pp. 1908-1922
    • Behrens, P.F.1    Franz, P.2    Woodman, B.3    Lindenberg, K.S.4    Landwehrmeyer, G.B.5
  • 8
    • 0030708576 scopus 로고    scopus 로고
    • Changes of NMDA receptor subunit (NR1, NR2B) and glutamate transporter (GLT1) mRNA expression in Huntington's disease-an in situ hybridization study
    • Arzberger, T., Krampfl, K., Leimgruber, S. and Weindl, A. (1997) Changes of NMDA receptor subunit (NR1, NR2B) and glutamate transporter (GLT1) mRNA expression in Huntington's disease-an in situ hybridization study. J. Neuropathol. Exp. Neurol., 56, 440-454.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 440-454
    • Arzberger, T.1    Krampfl, K.2    Leimgruber, S.3    Weindl, A.4
  • 9
    • 38349101590 scopus 로고    scopus 로고
    • Glutamate uptake is reduced in prefrontal cortex in Huntington's disease
    • Hassel, B., Tessler, S., Faull, R.L. and Emson, P.C. (2007) Glutamate uptake is reduced in prefrontal cortex in Huntington's disease. Neurochem. Res., 33, 232-237.
    • (2007) Neurochem. Res. , vol.33 , pp. 232-237
    • Hassel, B.1    Tessler, S.2    Faull, R.L.3    Emson, P.C.4
  • 10
    • 14644430451 scopus 로고    scopus 로고
    • Expanded polyglutamine peptides disrupt EGF receptor signaling and glutamate transporter expression in Drosophila
    • Liévens, J.C., Rival, T., Iche, M., Chneiweiss, H. and Birman, S. (2005) Expanded polyglutamine peptides disrupt EGF receptor signaling and glutamate transporter expression in Drosophila. Hum. Mol. Genet., 14, 713-724.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 713-724
    • Liévens, J.C.1    Rival, T.2    Iche, M.3    Chneiweiss, H.4    Birman, S.5
  • 12
    • 74449087772 scopus 로고    scopus 로고
    • Deciphering neuronglia compartmentalization in cortical energy metabolism
    • Jolivet, R., Magistretti, P.J. and Weber, B. (2009) Deciphering neuronglia compartmentalization in cortical energy metabolism. Front. Neuroenergetics, 1,4.
    • (2009) Front. Neuroenergetics , vol.1 , pp. 4
    • Jolivet, R.1    Magistretti, P.J.2    Weber, B.3
  • 14
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models
    • Browne, S.E. (2008) Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models. Ann. N. Y. Acad. Sci., 1147, 358-382.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 15
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia
    • Browne, S.E., Bowling, A.C., MacGarvey, U., Baik, M.J., Berger, S.C., Muqit, M.M., Bird, E.D. and Beal, M.F. (1997) Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia. Ann. Neurol., 41, 646-653.
    • (1997) Ann. Neurol. , vol.41 , pp. 646-653
    • Browne, S.E.1    Bowling, A.C.2    MacGarvey, U.3    Baik, M.J.4    Berger, S.C.5    Muqit, M.M.6    Bird, E.D.7    Beal, M.F.8
  • 21
    • 0021917344 scopus 로고
    • Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases
    • Butterworth, J., Yates, C.M. and Reynolds, G.P. (1985) Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and gamma-glutamyl transpeptidase in post-mortem brain from Huntington's disease and agonal cases. J. Neurol. Sci., 67, 161-171.
    • (1985) J. Neurol. Sci. , vol.67 , pp. 161-171
    • Butterworth, J.1    Yates, C.M.2    Reynolds, G.P.3
  • 22
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • Sorbi, S., Bird, E.D. and Blass, J.P. (1983) Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Ann. Neurol., 13, 72-78.
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 23
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • Browne, S.E. and Beal, M.F. (2006) Oxidative damage in Huntington's disease pathogenesis. Antioxid. Redox Signal., 8, 2061-2073.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 24
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. and Perrimon, N. (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development, 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 25
    • 65549105815 scopus 로고    scopus 로고
    • UCP2, not a physiologically relevant uncoupler but a glucose sparing switch impacting ROS production and glucose sensing
    • Bouillaud, F. (2009) UCP2, not a physiologically relevant uncoupler but a glucose sparing switch impacting ROS production and glucose sensing. Biochim. Biophys. Acta, 1787, 377-383.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 377-383
    • Bouillaud, F.1
  • 26
    • 27644448810 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the CNS: in support of function and survival
    • Andrews, Z.B., Diano, S. and Horvath, T.L. (2005) Mitochondrial uncoupling proteins in the CNS: in support of function and survival. Nat. Rev. Neurosci., 6, 829-840.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 829-840
    • Andrews, Z.B.1    Diano, S.2    Horvath, T.L.3
  • 27
    • 24144475250 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the central nervous system
    • Kim-Han, J.S. and Dugan, L.L. (2005) Mitochondrial uncoupling proteins in the central nervous system. Antioxid. Redox Signal., 7, 1173-1181.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1173-1181
    • Kim-Han, J.S.1    Dugan, L.L.2
  • 28
    • 0035986608 scopus 로고    scopus 로고
    • Possible physiological roles of mitochondrial uncoupling proteins-UCPn
    • Jezek, P. (2002) Possible physiological roles of mitochondrial uncoupling proteins-UCPn. Int. J. Biochem. Cell Biol., 34, 1190-1206.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1190-1206
    • Jezek, P.1
  • 30
    • 1842816630 scopus 로고    scopus 로고
    • Decreasing glutamate buffering capacity triggers oxidative stress and neuropil degeneration in the Drosophila brain
    • Rival, T., Soustelle, L., Strambi, C., Besson, M.T., Iche, M. and Birman, S. (2004) Decreasing glutamate buffering capacity triggers oxidative stress and neuropil degeneration in the Drosophila brain. Curr. Biol., 14, 599-605.
    • (2004) Curr. Biol. , vol.14 , pp. 599-605
    • Rival, T.1    Soustelle, L.2    Strambi, C.3    Besson, M.T.4    Iche, M.5    Birman, S.6
  • 31
    • 33645243792 scopus 로고    scopus 로고
    • Involvement of Drosophila uncoupling protein 5 in metabolism and aging
    • Sanchez-Blanco, A., Fridell, Y.W. and Helfand, S.L. (2006) Involvement of Drosophila uncoupling protein 5 in metabolism and aging. Genetics, 172, 1699-1710.
    • (2006) Genetics , vol.172 , pp. 1699-1710
    • Sanchez-Blanco, A.1    Fridell, Y.W.2    Helfand, S.L.3
  • 33
    • 30844445369 scopus 로고    scopus 로고
    • Structure of the mushroom bodies of the insect brain
    • Fahrbach, S.E. (2006) Structure of the mushroom bodies of the insect brain. Annu. Rev. Entomol., 51, 209-232.
    • (2006) Annu. Rev. Entomol. , vol.51 , pp. 209-232
    • Fahrbach, S.E.1
  • 34
    • 23944494249 scopus 로고    scopus 로고
    • Targeted expression of the human uncoupling protein 2 (hUCP2) to adult neurons extends life span in the fly
    • Fridell, Y.W., Sanchez-Blanco, A., Silvia, B.A. and Helfand, S.L. (2005) Targeted expression of the human uncoupling protein 2 (hUCP2) to adult neurons extends life span in the fly. Cell. Metab., 1, 145-152.
    • (2005) Cell. Metab. , vol.1 , pp. 145-152
    • Fridell, Y.W.1    Sanchez-Blanco, A.2    Silvia, B.A.3    Helfand, S.L.4
  • 37
    • 27444442915 scopus 로고    scopus 로고
    • Enhanced catabolism of mitochondrial superoxide/hydrogen peroxide and aging in transgenic Drosophila
    • Bayne, A.C., Mockett, R.J., Orr, W.C. and Sohal, R.S. (2005) Enhanced catabolism of mitochondrial superoxide/hydrogen peroxide and aging in transgenic Drosophila. Biochem. J., 391, 277-284.
    • (2005) Biochem. J. , vol.391 , pp. 277-284
    • Bayne, A.C.1    Mockett, R.J.2    Orr, W.C.3    Sohal, R.S.4
  • 38
    • 0345713188 scopus 로고    scopus 로고
    • The Drosophila glucose transporter gene: cDNA sequence, phylogenetic comparisons, analysis of functional sites and secondary structures
    • Escher, S.A. and Rasmuson-Lestander, A. (1999) The Drosophila glucose transporter gene: cDNA sequence, phylogenetic comparisons, analysis of functional sites and secondary structures. Hereditas, 130, 95-103.
    • (1999) Hereditas , vol.130 , pp. 95-103
    • Escher, S.A.1    Rasmuson-Lestander, A.2
  • 39
    • 3543111486 scopus 로고    scopus 로고
    • Cellular bases of activity-dependent paralysis in Drosophila stress-sensitive mutants
    • Trotta, N., Rodesch, C.K., Fergestad, T. and Broadie, K. (2004) Cellular bases of activity-dependent paralysis in Drosophila stress-sensitive mutants. J. Neurobiol., 60, 328-347.
    • (2004) J. Neurobiol. , vol.60 , pp. 328-347
    • Trotta, N.1    Rodesch, C.K.2    Fergestad, T.3    Broadie, K.4
  • 40
    • 33746384132 scopus 로고    scopus 로고
    • Metabolic disruption in Drosophila bang-sensitive seizure mutants
    • Fergestad, T., Bostwick, B. and Ganetzky, B. (2006) Metabolic disruption in Drosophila bang-sensitive seizure mutants. Genetics, 173, 1357-1364.
    • (2006) Genetics , vol.173 , pp. 1357-1364
    • Fergestad, T.1    Bostwick, B.2    Ganetzky, B.3
  • 41
    • 0033778866 scopus 로고    scopus 로고
    • Effects of 2-G exposure on temperature regulation, circadian rhythms, and adiposity in UCP2/3 transgenic mice
    • Fuller, P.M., Warden, C.H., Barry, S.J. and Fuller, C.A. (2000) Effects of 2-G exposure on temperature regulation, circadian rhythms, and adiposity in UCP2/3 transgenic mice. J. Appl. Physiol., 89, 1491-1498.
    • (2000) J. Appl. Physiol. , vol.89 , pp. 1491-1498
    • Fuller, P.M.1    Warden, C.H.2    Barry, S.J.3    Fuller, C.A.4
  • 43
    • 0242468451 scopus 로고    scopus 로고
    • Uncoupling protein 2 prevents neuronal death including that occurring during seizures: a mechanism for preconditioning
    • Diano, S., Matthews, R.T., Patrylo, P., Yang, L., Beal, M.F., Barnstable, C.J. and Horvath, T.L. (2003) Uncoupling protein 2 prevents neuronal death including that occurring during seizures: a mechanism for preconditioning. Endocrinology, 144, 5014-5021.
    • (2003) Endocrinology , vol.144 , pp. 5014-5021
    • Diano, S.1    Matthews, R.T.2    Patrylo, P.3    Yang, L.4    Beal, M.F.5    Barnstable, C.J.6    Horvath, T.L.7
  • 47
    • 38049120264 scopus 로고    scopus 로고
    • Uncoupling protein-2 controls proliferation by promoting fatty acid oxidation and limiting glycolysis-derived pyruvate utilization
    • Pecqueur, C., Bui, T., Gelly, C., Hauchard, J., Barbot, C., Bouillaud, F., Ricquier, D., Miroux, B. and Thompson, C.B. (2008) Uncoupling protein-2 controls proliferation by promoting fatty acid oxidation and limiting glycolysis-derived pyruvate utilization. Faseb J., 22, 9-18.
    • (2008) Faseb J. , vol.22 , pp. 9-18
    • Pecqueur, C.1    Bui, T.2    Gelly, C.3    Hauchard, J.4    Barbot, C.5    Bouillaud, F.6    Ricquier, D.7    Miroux, B.8    Thompson, C.B.9
  • 48
    • 0025930608 scopus 로고
    • Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
    • Skulachev, V.P. (1991) Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation. FEBS Lett., 294, 158-162.
    • (1991) FEBS Lett , vol.294 , pp. 158-162
    • Skulachev, V.P.1
  • 49
    • 0030039607 scopus 로고    scopus 로고
    • On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein
    • Garlid, K.D., Orosz, D.E., Modriansky, M., Vassanelli, S. and Jezek, P. (1996) On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein. J. Biol. Chem., 271, 2615-2620.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2615-2620
    • Garlid, K.D.1    Orosz, D.E.2    Modriansky, M.3    Vassanelli, S.4    Jezek, P.5
  • 50
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg, O. (1956) On the origin of cancer cells. Science, 123, 309-314.
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 51
    • 33745230018 scopus 로고    scopus 로고
    • Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress
    • Liu, D., Chan, S.L., de Souza-Pinto, N.C., Slevin, J.R., Wersto, R.P., Zhan, M., Mustafa, K., de Cabo, R. and Mattson, M.P. (2006) Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress. Neuromolecular Med., 8, 389-414.
    • (2006) Neuromolecular Med , vol.8 , pp. 389-414
    • Liu, D.1    Chan, S.L.2    de Souza-Pinto, N.C.3    Slevin, J.R.4    Wersto, R.P.5    Zhan, M.6    Mustafa, K.7    de Cabo, R.8    Mattson, M.P.9
  • 52
    • 0035918162 scopus 로고    scopus 로고
    • Uncoupling protein 3 (UCP3) stimulates glucose uptake in muscle cells through a phosphoinositide 3-kinase-dependent mechanism
    • Huppertz, C., Fischer, B.M., Kim, Y.B., Kotani, K., Vidal-Puig, A., Slieker, L.J., Sloop, K.W., Lowell, B.B. and Kahn, B.B. (2001) Uncoupling protein 3 (UCP3) stimulates glucose uptake in muscle cells through a phosphoinositide 3-kinase-dependent mechanism. J. Biol. Chem., 276, 12520-12529.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12520-12529
    • Huppertz, C.1    Fischer, B.M.2    Kim, Y.B.3    Kotani, K.4    Vidal-Puig, A.5    Slieker, L.J.6    Sloop, K.W.7    Lowell, B.B.8    Kahn, B.B.9
  • 53
    • 0035462612 scopus 로고    scopus 로고
    • Overexpression of UCP3 in cultured human muscle lowers mitochondrial membrane potential, raises ATP/ADP ratio, and favors fatty acid vs. glucose oxidation
    • Garcia-Martinez, C., Sibille, B., Solanes, G., Darimont, C., Mace, K., Villarroya, F. and Gomez-Foix, A.M. (2001) Overexpression of UCP3 in cultured human muscle lowers mitochondrial membrane potential, raises ATP/ADP ratio, and favors fatty acid vs. glucose oxidation. Faseb J., 15, 2033-2035.
    • (2001) Faseb J. , vol.15 , pp. 2033-2035
    • Garcia-Martinez, C.1    Sibille, B.2    Solanes, G.3    Darimont, C.4    Mace, K.5    Villarroya, F.6    Gomez-Foix, A.M.7
  • 54
    • 0028080101 scopus 로고
    • Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization
    • Pellerin, L. and Magistretti, P.J. (1994) Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization. Proc. Natl Acad. Sci. USA, 91, 10625-10629.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10625-10629
    • Pellerin, L.1    Magistretti, P.J.2
  • 55
    • 0038364056 scopus 로고    scopus 로고
    • Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant Huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy
    • Ravikumar, B., Stewart, A., Kita, H., Kato, K., Duden, R. and Rubinsztein, D.C. (2003) Raised intracellular glucose concentrations reduce aggregation and cell death caused by mutant Huntingtin exon 1 by decreasing mTOR phosphorylation and inducing autophagy. Hum. Mol. Genet., 12, 985-994.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 985-994
    • Ravikumar, B.1    Stewart, A.2    Kita, H.3    Kato, K.4    Duden, R.5    Rubinsztein, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.