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Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease

Tanaka, Motomasa, Machida, Yoko, Niu, Sanyong, Ikeda, Tetsurou, Jana, Nihar R, Doi, Hiroshi, Kurosawa, Masaru, Nekooki, Munenori, Nukina, Nobuyuki·2004·Nature Medicine

DOI 10.1038/nm985

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Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
Mangiarini, L., Sathasivam, K., Seller, M., Cozens, B., Harper, A., Hetherington, C., Lawton, M., Trottier, Y., Lehrach, H., Davies, S. W., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81369-0 · Cited by 3,073
Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., & Aronin, N. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,439
Formation of Neuronal Intranuclear Inclusions Underlies the Neurological Dysfunction in Mice Transgenic for the HD Mutation
Davies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., Ross, C. A., Scherzinger, E., Wanker, E. E., Mangiarini, L., & Bates, G. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80513-9 · Cited by 2,181
Glutamine Repeats and Neurodegeneration
Zoghbi, H. Y., & Orr, H. T. (2000) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.23.1.217 · Cited by 1,309
Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291
Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
Chen, M., Ona, V. O., Li, M., Ferrante, R. J., Fink, K. B., Zhu, S., Bian, J., Guo, L., Farrell, L. A., Hersch, S. M., et al. (2000) · Nature Medicine · doi:10.1038/77528 · Cited by 1,051
Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits in a mouse model of Huntington's disease
Hockly, E., Richon, V. M., Woodman, B., Smith, D. L., Zhou, X., Rosa, E., Sathasivam, K., Ghazi-Noori, S., Mahal, A., Lowden, P. A. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437870100 · Cited by 845
Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
Cummings, C. J., Mancini, M. A., Antalffy, B., DeFranco, D. B., Orr, H. T., & Zoghbi, H. Y. (1998) · Nature Genetics · doi:10.1038/502 · Cited by 744
Multiple Effects of Trehalose on Protein Folding In Vitro and In Vivo
Singer, M. A., & Lindquist, S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80064-7 · Cited by 698
Expanded Polyglutamine Protein Forms Nuclear Inclusions and Causes Neural Degeneration in Drosophila
Warrick, J. M., Paulson, H. L., Gray-Board, G. L., Bui, Q. T., Fischbeck, K. H., Pittman, R. N., & Bonini, N. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81200-3 · Cited by 668

Show all 38 references

Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134
Trehalose, a Novel mTOR-independent Autophagy Enhancer, Accelerates the Clearance of Mutant Huntingtin and α-Synuclein
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142
Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
Molecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
RNA interference improves motor and neuropathological abnormalities in a Huntington's disease mouse model
Harper, S. Q., Staber, P. D., He, X., Eliason, S. L., Martins, I. H., Mao, Q., Yang, L., Kotin, R. M., Paulson, H. L., & Davidson, B. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501507102 · Cited by 682
Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
Sarkar, S., Ravikumar, B., Floto, R. A., & Rubinsztein, D. C. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.110 · Cited by 578
Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
Tai, H.-C., & Schuman, E. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2499 · Cited by 532
Trehalose: Current Use and Future Applications
Ohtake, S., & Wang, Y. J. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22458 · Cited by 487
Formation of nucleoplasmic protein aggregates impairs nuclear function in response to SiO nanoparticles
CHEN, M., & VONMIKECZ, A. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.12.021 · Cited by 493
Repeat expansion disease: progress and puzzles in disease pathogenesis
La Spada, A. R., & Taylor, J. P. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2748 · Cited by 488
Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
Shibata, M., Lu, T., Furuya, T., Degterev, A., Mizushima, N., Yoshimori, T., MacDonald, M., Yankner, B., & Yuan, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600364200 · Cited by 458
The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective
Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436
Control of autophagy as a therapy for neurodegenerative disease
Harris, H., & Rubinsztein, D. C. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.200 · Cited by 447
Autophagy in neurodegenerative diseases: pathogenesis and therapy
Guo, F., Liu, X., Cai, H., & Le, W. (2018) · Brain Pathology · doi:10.1111/bpa.12545 · Cited by 444
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration
Rusmini, P., Cortese, K., Crippa, V., Cristofani, R., Cicardi, M. E., Ferrari, V., Vezzoli, G., Tedesco, B., Meroni, M., Messi, E., et al. (2019) · Autophagy · doi:10.1080/15548627.2018.1535292 · Cited by 436
Huntington's disease: from pathology and genetics to potential therapies
Imarisio, S., Carmichael, J., Korolchuk, V., Chen, C.-W., Saiki, S., Rose, C., Krishna, G., Davies, J. E., Ttofi, E., Underwood, B. R., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071619 · Cited by 409
mTORC1-independent TFEB activation via Akt inhibition promotes cellular clearance in neurodegenerative storage diseases
Palmieri, M., Pal, R., Nelvagal, H. R., Lotfi, P., Stinnett, G. R., Seymour, M. L., Chaudhury, A., Bajaj, L., Bondar, V. V., Bremner, L., et al. (2017) · Nature Communications · doi:10.1038/ncomms14338 · Cited by 383
Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease
Giordano, S., Darley-Usmar, V., & Zhang, J. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.013 · Cited by 366
Exploiting macrophage autophagy-lysosomal biogenesis as a therapy for atherosclerosis
Sergin, I., Evans, T. D., Zhang, X., Bhattacharya, S., Stokes, C. J., Song, E., Ali, S., Dehestani, B., Holloway, K. B., Micevych, P. S., et al. (2017) · Nature Communications · doi:10.1038/ncomms15750 · Cited by 351
Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection
Nedelsky, N. B., Todd, P. K., & Taylor, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.002 · Cited by 351
Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343
Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons
Castillo, K., Nassif, M., Valenzuela, V., Rojas, F., Matus, S., Mercado, G., Court, F. A., van Zundert, B., & Hetz, C. (2013) · Autophagy · doi:10.4161/auto.25188 · Cited by 340
Autophagy and Microglia: Novel Partners in Neurodegeneration and Aging
Plaza-Zabala, A., Sierra-Torre, V., & Sierra, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030598 · Cited by 323
Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
Ignatova, Z., & Gierasch, L. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603772103 · Cited by 320
Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation
Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297
Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
Vidal, R. L., Figueroa, A., Court, F. A., Thielen, P., Molina, C., Wirth, C., Caballero, B., Kiffin, R., Segura-Aguilar, J., Cuervo, A. M., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds040 · Cited by 285
Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
Bauer, P. O., Goswami, A., Wong, H. K., Okuno, M., Kurosawa, M., Yamada, M., Miyazaki, H., Matsumoto, G., Kino, Y., Nagai, Y., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1608 · Cited by 280
Self-citation
Trehalose transporter 1, a facilitated and high-capacity trehalose transporter, allows exogenous trehalose uptake into cells
Kikawada, T., Saito, A., Kanamori, Y., Nakahara, Y., Iwata, K.-I., Tanaka, D., Watanabe, M., & Okuda, T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702538104 · Cited by 268
Gene regulation by the glucocorticoid receptor: structure:function relationship
Kumar, R., & Thompson, E. B. (2005) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.12.046 · Cited by 261
The ubiquitin–proteasome pathway in Parkinson's disease and other neurodegenerative diseases
Ross, C. A., & Pickart, C. M. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.10.006 · Cited by 261
The therapeutic potential of chemical chaperones in protein folding diseases
Cortez, L., & Sim, V. (2014) · Prion · doi:10.4161/pri.28938 · Cited by 254
Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
Davies, J. E., Sarkar, S., & Rubinsztein, D. C. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi422 · Cited by 207
VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington’s disease
Guo, X., Sun, X., Hu, D., Wang, Y.-J., Fujioka, H., Vyas, R., Chakrapani, S., Joshi, A. U., Luo, Y., Mochly-Rosen, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms12646 · Cited by 200
Autophagy for tissue homeostasis and neuroprotection
Mariño, G., Madeo, F., & Kroemer, G. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.10.001 · Cited by 195
The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies
Bauer, P. O., & Nukina, N. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06302.x · Cited by 178
Self-citation
Current Advances in The Development of Novel Polymeric Nanoparticles for The Treatment of Neurodegenerative Diseases
Cano, A., Sánchez-López, E., Ettcheto, M., López-Machado, A., Espina, M., Souto, E. B., Galindo, R., Camins, A., García, M. L., & Turowski, P. (2020) · Nanomedicine · doi:10.2217/nnm-2019-0443 · Cited by 144
The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells
Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., de Yébenes, J. G., & Mena, M. A. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.01.008 · Cited by 114
Trehalose reduces retinal degeneration, neuroinflammation and storage burden caused by a lysosomal hydrolase deficiency
Lotfi, P., Tse, D. Y., Di Ronza, A., Seymour, M. L., Martano, G., Cooper, J. D., Pereira, F. A., Passafaro, M., Wu, S. M., & Sardiello, M. (2018) · Autophagy · doi:10.1080/15548627.2018.1474313 · Cited by 106
The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease
Fox, J. H., Connor, T., Chopra, V., Dorsey, K., Kama, J. A., Bleckmann, D., Betschart, C., Hoyer, D., Frentzel, S., DiFiglia, M., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-26 · Cited by 94
“Discussion R6/2 HD mice have been used extensively in pre-clinical drug trials and numerous compounds, including one that promotes macroautophagy, have shown neuroprotective effects [9,27].”
Background
Dysregulation of C/EBPα by mutant Huntingtin causes the urea cycle deficiency in Huntington's disease
Chiang, M.-C., Chen, H.-M., Lee, Y.-H., Chang, H.-H., Wu, Y.-C., Soong, B.-W., Chen, C.-M., Wu, Y.-R., Liu, C.-S., Niu, D.-M., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl481 · Cited by 95
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79
Loss of dopaminergic neurons and resulting behavioural deficits in mouse model of Angelman syndrome
Mulherkar, S. A., & Jana, N. R. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.002 · Cited by 71
Self-citation
Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases
Takeuchi, T., & Nagai, Y. (2017) · Brain Sciences · doi:10.3390/brainsci7100128 · Cited by 71
Y-27632 improves rotarod performance and reduces huntingtin levels in R6/2 mice
Li, M., Huang, Y., Ma, A. A. K., Lin, E., & Diamond, M. I. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.06.011 · Cited by 68
Trehalose induced antidepressant-like effects and autophagy enhancement in mice
Kara, N. Z., Toker, L., Agam, G., Anderson, G. W., Belmaker, R. H., & Einat, H. (2013) · Psychopharmacology · doi:10.1007/s00213-013-3119-4 · Cited by 64
Targeting the unfolded protein response for disease intervention.
Rivas, A., Vidal, R. L., & Hetz, C. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2015.1053869 · Cited by 62
Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway
Nassif, M., Matus, S., Castillo, K., & Hetz, C. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2991 · Cited by 60
Autophagy preferentially degrades non-fibrillar polyQ aggregates
(2024) · doi:10.1016/j.molcel.2024.04.018 · Cited by 51
Chemical Screening Approaches Enabling Drug Discovery of Autophagy Modulators for Biomedical Applications in Human Diseases
Panda, P. K., Fahrner, A., Vats, S., Seranova, E., Sharma, V., Chipara, M., Desai, P., Torresi, J., Rosenstock, T., Kumar, D., et al. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00038 · Cited by 50
Trehalose does not improve neuronal survival on exposure to alpha-synuclein pre-formed fibrils
Redmann, M., Wani, W. Y., Volpicelli-Daley, L., Darley-Usmar, V., & Zhang, J. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.032 · Cited by 46
Spinocerebellar ataxias caused by polyglutamine expansions: A review of therapeutic strategies
Underwood, B. R., & Rubinsztein, D. C. (2008) · The Cerebellum · doi:10.1007/s12311-008-0026-z · Cited by 44
Lanosterol Suppresses the Aggregation and Cytotoxicity of Misfolded Proteins Linked with Neurodegenerative Diseases
Upadhyay, A., Amanullah, A., Mishra, R., Kumar, A., & Mishra, A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-016-0377-2 · Cited by 39
Neuroprotective Effects of Trehalose and Sodium Butyrate on Preformed Fibrillar Form of α-Synuclein-Induced Rat Model of Parkinson’s Disease
Kakoty, V., K C, S., Dubey, S. K., Yang, C.-H., & Taliyan, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00144 · Cited by 33
The regulation of the small heat shock protein B8 in misfolding protein diseases causing motoneuronal and muscle cell death
Cristofani, R., Rusmini, P., Galbiati, M., Cicardi, M. E., Ferrari, V., Tedesco, B., Casarotto, E., Chierichetti, M., Messi, E., Piccolella, M., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00796 · Cited by 35
An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors
Fuentealba, R. A., Marasa, J., Diamond, M. I., Piwnica-Worms, D., & Weihl, C. C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr500 · Cited by 28
Autophagy preferentially degrades non-fibrillar polyQ aggregates
Zhao, D. Y., Bäuerlein, F. J. B., Saha, I., Hartl, F. U., Baumeister, W., & Wilfling, F. (2023) · doi:10.1101/2023.08.08.552291 · Cited by 3

Authors: Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N. R., Doi, H., Kurosawa, M., Nekooki, M., & Nukina, N.
Venue: Nature Medicine
Publisher: Springer Science and Business Media LLC
Published: 2004-01-18
Volume: 10
Issue: 2
Pages: 148-154
ISSN: 1078-8956 (ISSN-L)
1546-170X
DOI: 10.1038/nm985
OpenAlex: W2014520750
Cited by: 782
References: 38
FWCI: 12.13
Type: journal article
Language: en
Open access: closed

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Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease

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