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Open AccessArticle

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

1
State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Fudan University, Shanghai 200433, China
2
Laboratory of Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, China
*
Authors to whom correspondence should be addressed.
Molecules 2017, 22(8), 1293; https://doi.org/10.3390/molecules22081293
Received: 6 July 2017 / Accepted: 1 August 2017 / Published: 8 August 2017
(This article belongs to the Special Issue Neuroprotective Agents)
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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MDPI and ACS Style

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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