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Molecules 2017, 22(8), 1293;

Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells

State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Fudan University, Shanghai 200433, China
Laboratory of Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, China
Authors to whom correspondence should be addressed.
Received: 6 July 2017 / Accepted: 1 August 2017 / Published: 8 August 2017
(This article belongs to the Special Issue Neuroprotective Agents)
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Fibrillar accumulation of A53T mutant α-synuclein (A53T-AS) in Lewy bodies is a symptom of Parkinsonism. Inhibitions of the overexpression and fibrillar aggregation of α-synuclein (AS) in vivo could be a promising strategy for treating Parkinson’s disease (PD). In this study, at concentrations lower than 1 mM, trehalose decreased the A53T-AS expression level in transduced PC12 cells. Although H2O2 and aluminum ions increased the expression level and neurotoxicity of A53T-AS in cells, proper trehalose concentrations inhibited the event. These studies adequately prove that trehalose at an appropriate dose would be potentially useful for PD treatment. View Full-Text
Keywords: α-synuclein; trehalose; transduced PC12 cell; Parkinson’s disease α-synuclein; trehalose; transduced PC12 cell; Parkinson’s disease

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Zhao, J.; Zhi, X.; Pan, L.; Zhou, P. Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells. Molecules 2017, 22, 1293.

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