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Volumn 129, Issue 21, 2016, Pages 4118-4129

New links between SOD1 and metabolic dysfunction from a yeast model of amyotrophic lateral sclerosis

Author keywords

ALS; Metabolism; SOD1; Vacuole; Yeast

Indexed keywords

AMINO ACID; COPPER ZINC SUPEROXIDE DISMUTASE; LEUCINE; REACTIVE OXYGEN METABOLITE; ISOENZYME; MUTANT PROTEIN; PROTEIN AGGREGATE;

EID: 84995443036     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.190298     Document Type: Article
Times cited : (41)

References (51)
  • 2
    • 84952985148 scopus 로고    scopus 로고
    • Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathways
    • Ayers, J. I., Fromholt, S. E., O'Neal, V. M., Diamond, J. H. and Borchelt, D. R. (2016). Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathways. Acta Neuropathol. 131, 103-114.
    • (2016) Acta Neuropathol , vol.131 , pp. 103-114
    • Ayers, J.I.1    Fromholt, S.E.2    O'Neal, V.M.3    Diamond, J.H.4    Borchelt, D.R.5
  • 5
    • 0032579962 scopus 로고    scopus 로고
    • Glutamate uptake is decreased tardively in the spinal cord of FALS mice
    • Canton, T., Pratt, J., Stutzmann, J.-M., Imperato, A. and Boireau, A. (1998). Glutamate uptake is decreased tardively in the spinal cord of FALS mice. Neuroreport 9, 775-778.
    • (1998) Neuroreport , vol.9 , pp. 775-778
    • Canton, T.1    Pratt, J.2    Stutzmann, J.-M.3    Imperato, A.4    Boireau, A.5
  • 7
    • 84881275424 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis: an update
    • Chen, S., Sayana, P., Zhang, X. and Le, W. (2013). Genetics of amyotrophic lateral sclerosis: an update. Mol. Neurodegener. 8, 28.
    • (2013) Mol. Neurodegener , vol.8 , pp. 28
    • Chen, S.1    Sayana, P.2    Zhang, X.3    Le, W.4
  • 8
    • 80055071250 scopus 로고    scopus 로고
    • The role of tRNA and ribosome competition in coupling the expression of different mRNAs in Saccharomyces cerevisiae
    • Chu, D., Barnes, D. J. and von der Haar, T. (2011). The role of tRNA and ribosome competition in coupling the expression of different mRNAs in Saccharomyces cerevisiae. Nucleic Acids Res. 39, 6705-6714.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6705-6714
    • Chu, D.1    Barnes, D.J.2    von der Haar, T.3
  • 9
    • 84894646451 scopus 로고    scopus 로고
    • Translation elongation can control translation initiation on eukaryotic mRNAs
    • Chu, D., Kazana, E., Bellanger, N., Singh, T., Tuite, M. F. and von der Haar, T. (2014). Translation elongation can control translation initiation on eukaryotic mRNAs. EMBO J. 33, 21-34.
    • (2014) EMBO J , vol.33 , pp. 21-34
    • Chu, D.1    Kazana, E.2    Bellanger, N.3    Singh, T.4    Tuite, M.F.5    von der Haar, T.6
  • 11
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng, H.-X., Shi, Y., Furukawa, Y., Zhai, H., Fu, R., Liu, E., Gorrie, G. H., Khan, M. S., Hung, W.-Y., Bigio, E. H. et al. (2006). Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. USA 103, 7142-7147.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7142-7147
    • Deng, H.-X.1    Shi, Y.2    Furukawa, Y.3    Zhai, H.4    Fu, R.5    Liu, E.6    Gorrie, G.H.7    Khan, M.S.8    Hung, W.-Y.9    Bigio, E.H.10
  • 12
    • 0034602804 scopus 로고    scopus 로고
    • Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae
    • Eaglestone, S. S., Ruddock, L. W., Cox, B. S. and Tuite, M. F. (2000). Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97, 240-244.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 240-244
    • Eaglestone, S.S.1    Ruddock, L.W.2    Cox, B.S.3    Tuite, M.F.4
  • 14
    • 84957900504 scopus 로고    scopus 로고
    • Mice Overexpressing both non-mutated human SOD1 and mutated SOD1(G93A) genes: a competent experimental model for studying iron metabolism in amyotrophic lateral sclerosis
    • Gajowiak, A., Styś, A., Starzyński, R. R., Bednarz, A., Lenartowicz, M., Staroń, R. and Lipiński, P. (2015). Mice Overexpressing both non-mutated human SOD1 and mutated SOD1(G93A) genes: a competent experimental model for studying iron metabolism in amyotrophic lateral sclerosis. Front. Mol. Neurosci. 8, 82.
    • (2015) Front. Mol. Neurosci , vol.8 , pp. 82
    • Gajowiak, A.1    Styś, A.2    Starzyński, R.R.3    Bednarz, A.4    Lenartowicz, M.5    Staroń, R.6    Lipiński, P.7
  • 15
    • 84881337118 scopus 로고    scopus 로고
    • The impact of clinical factors, riluzole and therapeutic interventions on ALS survival: a population based study in Modena, Italy. Amyotroph. Lateral Scler
    • Georgoulopoulou, E., Fini, N., Vinceti, M., Monelli, M., Vacondio, P., Bianconi, G., Sola, P., Nichelli, P. and Mandrioli, J. (2013). The impact of clinical factors, riluzole and therapeutic interventions on ALS survival: a population based study in Modena, Italy. Amyotroph. Lateral Scler. Frontotemporal Degener. 14, 338-345.
    • (2013) Frontotemporal Degener , vol.14 , pp. 338-345
    • Georgoulopoulou, E.1    Fini, N.2    Vinceti, M.3    Monelli, M.4    Vacondio, P.5    Bianconi, G.6    Sola, P.7    Nichelli, P.8    Mandrioli, J.9
  • 16
    • 29144536703 scopus 로고    scopus 로고
    • Truncated wild-type SOD1 and FALS-linked mutant SOD1 cause neural cell death in the chick embryo spinal cord
    • Ghadge, G. D., Wang, L., Sharma, K., Monti, A. L., Bindokas, V., Stevens, F. J. and Roos, R. P. (2006). Truncated wild-type SOD1 and FALS-linked mutant SOD1 cause neural cell death in the chick embryo spinal cord. Neurobiol. Dis. 21, 194-205.
    • (2006) Neurobiol. Dis , vol.21 , pp. 194-205
    • Ghadge, G.D.1    Wang, L.2    Sharma, K.3    Monti, A.L.4    Bindokas, V.5    Stevens, F.J.6    Roos, R.P.7
  • 17
    • 77952544821 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 overexpression in NSC-34 cells: effect of trehalose on aggregation, TDP-43 localization and levels of co-expressed glycoproteins
    • Gomes, C., Escrevente, C. and Costa, J. (2010). Mutant superoxide dismutase 1 overexpression in NSC-34 cells: effect of trehalose on aggregation, TDP-43 localization and levels of co-expressed glycoproteins. Neurosci. Lett. 475, 145-149.
    • (2010) Neurosci. Lett , vol.475 , pp. 145-149
    • Gomes, C.1    Escrevente, C.2    Costa, J.3
  • 19
    • 84859454704 scopus 로고    scopus 로고
    • An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
    • Guareschi, S., Cova, E., Cereda, C., Ceroni, M., Donetti, E., Bosco, D. A., Trotti, D. and Pasinelli, P. (2012). An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc. Natl. Acad. Sci. USA 109, 5074-5079.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5074-5079
    • Guareschi, S.1    Cova, E.2    Cereda, C.3    Ceroni, M.4    Donetti, E.5    Bosco, D.A.6    Trotti, D.7    Pasinelli, P.8
  • 20
    • 0037088811 scopus 로고    scopus 로고
    • A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast
    • Gueldener, U., Heinisch, J., Koehler, G. J., Voss, D. and Hegemann, J. H. (2002). A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res. 30, e23.
    • (2002) Nucleic Acids Res , vol.30
    • Gueldener, U.1    Heinisch, J.2    Koehler, G.J.3    Voss, D.4    Hegemann, J.H.5
  • 21
    • 84919967635 scopus 로고    scopus 로고
    • Leucine as a treatment for muscle wasting: a critical review
    • Ham, D. J., Caldow, M. K., Lynch, G. S. and Koopman, R. (2014). Leucine as a treatment for muscle wasting: a critical review. Clin. Nutr. 33, 937-945.
    • (2014) Clin. Nutr , vol.33 , pp. 937-945
    • Ham, D.J.1    Caldow, M.K.2    Lynch, G.S.3    Koopman, R.4
  • 22
    • 84939983554 scopus 로고    scopus 로고
    • Metal-deficient SOD1 in amyotrophic lateral sclerosis
    • Hilton, J. B., White, A. R. and Crouch, P. J. (2015). Metal-deficient SOD1 in amyotrophic lateral sclerosis. J. Mol. Med. 93, 481-487.
    • (2015) J. Mol. Med , vol.93 , pp. 481-487
    • Hilton, J.B.1    White, A.R.2    Crouch, P.J.3
  • 23
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch, A. G. (2005). Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59, 407-450.
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 24
    • 84920716246 scopus 로고    scopus 로고
    • Assays for autophagy I: the Cvt pathway and nonselective autophagy
    • Huang, W.-P., Shintani, T. and Xie, Z. (2014). Assays for autophagy I: the Cvt pathway and nonselective autophagy. Methods Mol. Biol. 1163, 153-164.
    • (2014) Methods Mol. Biol , vol.1163 , pp. 153-164
    • Huang, W.-P.1    Shintani, T.2    Xie, Z.3
  • 25
    • 84952862051 scopus 로고    scopus 로고
    • Mutant SOD1 mediated pathogenesis of amyotrophic lateral sclerosis
    • Kaur, S. J., McKeown, S. R. and Rashid, S. (2016). Mutant SOD1 mediated pathogenesis of amyotrophic lateral sclerosis. Gene 577, 109-118.
    • (2016) Gene , vol.577 , pp. 109-118
    • Kaur, S.J.1    McKeown, S.R.2    Rashid, S.3
  • 26
    • 84893469844 scopus 로고    scopus 로고
    • Abnormal intracellular calcium signaling and SNARE-dependent exocytosis contributes to SOD1G93A astrocyte-mediated toxicity in amyotrophic lateral sclerosis
    • Kawamata, H., Ng, S. K., Diaz, N., Burstein, S., Morel, L., Osgood, A., Sider, B., Higashimori, H., Haydon, P. G., Manfredi, G. et al. (2014). Abnormal intracellular calcium signaling and SNARE-dependent exocytosis contributes to SOD1G93A astrocyte-mediated toxicity in amyotrophic lateral sclerosis. J. Neurosci. 34, 2331-2348.
    • (2014) J. Neurosci , vol.34 , pp. 2331-2348
    • Kawamata, H.1    Ng, S.K.2    Diaz, N.3    Burstein, S.4    Morel, L.5    Osgood, A.6    Sider, B.7    Higashimori, H.8    Haydon, P.G.9    Manfredi, G.10
  • 27
    • 84925748556 scopus 로고    scopus 로고
    • Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis
    • Kepp, K. P. (2015). Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis. PLoS ONE 10, e0118649.
    • (2015) PLoS ONE , vol.10
    • Kepp, K.P.1
  • 28
    • 84954467884 scopus 로고    scopus 로고
    • Dynamic relocation of the TORC1-Gtr1/2-Ego1/2/3 complex is regulated by Gtr1 and Gtr2
    • Kira, S., Kumano, Y., Ukai, H., Takeda, E., Matsuura, A. and Noda, T. (2016). Dynamic relocation of the TORC1-Gtr1/2-Ego1/2/3 complex is regulated by Gtr1 and Gtr2. Mol. Biol. Cell 27, 382-396.
    • (2016) Mol. Biol. Cell , vol.27 , pp. 382-396
    • Kira, S.1    Kumano, Y.2    Ukai, H.3    Takeda, E.4    Matsuura, A.5    Noda, T.6
  • 30
  • 31
    • 84957045630 scopus 로고    scopus 로고
    • Autophagy in motor neuron disease: key pathogenetic mechanisms and therapeutic targets
    • Mis, M. S. C., Brajkovic, S., Frattini, E., Di Fonzo, A. and Corti, S. (2016). Autophagy in motor neuron disease: key pathogenetic mechanisms and therapeutic targets. Mol. Cell. Neurosci. 72, 84-90.
    • (2016) Mol. Cell. Neurosci , vol.72 , pp. 84-90
    • Mis, M.S.C.1    Brajkovic, S.2    Frattini, E.3    Di Fonzo, A.4    Corti, S.5
  • 32
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Münch, C., O'Brien, J. and Bertolotti, A. (2011). Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. USA 108, 3548-3553.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3548-3553
    • Münch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 34
    • 84904648362 scopus 로고    scopus 로고
    • Mitochondria-targeted catalase reverts the neurotoxicity of hSOD1G93A astrocytes without extending the survival of ALS-linked mutant hSOD1 mice
    • Pehar, M., Beeson, G., Beeson, C. C., Johnson, J. A. and Vargas, M. R. (2014). Mitochondria-targeted catalase reverts the neurotoxicity of hSOD1G93A astrocytes without extending the survival of ALS-linked mutant hSOD1 mice. PLoS ONE 9, e103438.
    • (2014) PLoS ONE , vol.9
    • Pehar, M.1    Beeson, G.2    Beeson, C.C.3    Johnson, J.A.4    Vargas, M.R.5
  • 35
    • 0344465252 scopus 로고
    • Assay of vacuolar pH in yeast and identification of acidification-defective mutants
    • Preston, R. A., Murphy, R. F. and Jones, E. W. (1989). Assay of vacuolar pH in yeast and identification of acidification-defective mutants. Proc. Natl. Acad. Sci. USA 86, 7027-7031.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7027-7031
    • Preston, R.A.1    Murphy, R.F.2    Jones, E.W.3
  • 39
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • Sasaki, S. (2011). Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 70, 349-359.
    • (2011) J. Neuropathol. Exp. Neurol , vol.70 , pp. 349-359
    • Sasaki, S.1
  • 40
    • 0029435386 scopus 로고
    • Familial amyotrophic lateral sclerosis
    • Siddique, T. and Hentati, A. (1995-1996). Familial amyotrophic lateral sclerosis. Clin. Neurosci. 3, 338-347.
    • (1995) Clin. Neurosci , vol.3 , pp. 338-347
    • Siddique, T.1    Hentati, A.2
  • 43
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R. and Culotta, V. C. (2001). A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084-38089.
    • (2001) J. Biol. Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 45
    • 84955454731 scopus 로고    scopus 로고
    • Macrophage-mediated inflammation and glial response in the skeletal muscle of a rat model of familial amyotrophic lateral sclerosis (ALS)
    • Van Dyke, J. M., Smit-Oistad, I. M., Macrander, C., Krakora, D., Meyer, M. G. and Suzuki, M. (2016). Macrophage-mediated inflammation and glial response in the skeletal muscle of a rat model of familial amyotrophic lateral sclerosis (ALS). Exp. Neurol. 277, 275-282.
    • (2016) Exp. Neurol , vol.277 , pp. 275-282
    • Van Dyke, J.M.1    Smit-Oistad, I.M.2    Macrander, C.3    Krakora, D.4    Meyer, M.G.5    Suzuki, M.6
  • 46
    • 84901292105 scopus 로고    scopus 로고
    • Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis
    • Vehviläinen, P., Koistinaho, J. and Gundars, G. (2014). Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis. Front. Cell. Neurosci. 8, 126.
    • (2014) Front. Cell. Neurosci , vol.8 , pp. 126
    • Vehviläinen, P.1    Koistinaho, J.2    Gundars, G.3
  • 47
    • 0030714187 scopus 로고    scopus 로고
    • MRI and clinical features in amyotrophic lateral sclerosis
    • Waragai, M. (1997). MRI and clinical features in amyotrophic lateral sclerosis. Neuroradiology 39, 847-851.
    • (1997) Neuroradiology , vol.39 , pp. 847-851
    • Waragai, M.1
  • 48
    • 84919341594 scopus 로고    scopus 로고
    • Formation of hydrogen sulfide from cysteine in Saccharomyces cerevisiae BY4742: genome wide screen reveals a central role of the vacuole
    • Winter, G., Cordente, A. G. and Curtin, C. (2014). Formation of hydrogen sulfide from cysteine in Saccharomyces cerevisiae BY4742: genome wide screen reveals a central role of the vacuole. PLoS ONE 9, e113869.
    • (2014) PLoS ONE , vol.9
    • Winter, G.1    Cordente, A.G.2    Curtin, C.3
  • 49
    • 70349487306 scopus 로고    scopus 로고
    • Cytosolic superoxide dismutase (SOD1) is critical for tolerating the oxidative stress of zinc deficiency in yeast
    • Wu, C.-Y., Steffen, J. and Eide, D. J. (2009). Cytosolic superoxide dismutase (SOD1) is critical for tolerating the oxidative stress of zinc deficiency in yeast. PLoS ONE 4, e7061.
    • (2009) PLoS ONE , vol.4
    • Wu, C.-Y.1    Steffen, J.2    Eide, D.J.3
  • 50
    • 84947555603 scopus 로고    scopus 로고
    • Progressive endolysosomal deficits impair autophagic clearance beginning at early asymptomatic stages in fALS mice
    • Xie, Y., Zhou, B., Lin, M.-Y. and Sheng, Z.-H. (2015). Progressive endolysosomal deficits impair autophagic clearance beginning at early asymptomatic stages in fALS mice. Autophagy 11, 1934-1936.
    • (2015) Autophagy , vol.11 , pp. 1934-1936
    • Xie, Y.1    Zhou, B.2    Lin, M.-Y.3    Sheng, Z.-H.4
  • 51
    • 84922477400 scopus 로고    scopus 로고
    • Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice
    • Xu, G., Ayers, J. I., Roberts, B. L., Brown, H., Fromholt, S., Green, C. and Borchelt, D. R. (2015). Direct and indirect mechanisms for wild-type SOD1 to enhance the toxicity of mutant SOD1 in bigenic transgenic mice. Hum. Mol. Genet. 24, 1019-1035.
    • (2015) Hum. Mol. Genet , vol.24 , pp. 1019-1035
    • Xu, G.1    Ayers, J.I.2    Roberts, B.L.3    Brown, H.4    Fromholt, S.5    Green, C.6    Borchelt, D.R.7


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