Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells
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...
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doaj-04c9786b9560408b8ac0b65e4faa7ce62020-11-24T22:52:28ZengMDPI AGMolecules1420-30492017-08-01228129310.3390/molecules22081293molecules22081293Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 CellsJuan Zhao0Xiuling Zhi1Luanfeng Pan2Ping Zhou3State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Fudan University, Shanghai 200433, ChinaLaboratory of Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, ChinaLaboratory of Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, ChinaState Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Fudan University, Shanghai 200433, ChinaFibrillar 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.https://www.mdpi.com/1420-3049/22/8/1293α-synucleintrehalosetransduced PC12 cellParkinson’s disease |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Juan Zhao Xiuling Zhi Luanfeng Pan Ping Zhou |
spellingShingle |
Juan Zhao Xiuling Zhi Luanfeng Pan Ping Zhou Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells Molecules α-synuclein trehalose transduced PC12 cell Parkinson’s disease |
author_facet |
Juan Zhao Xiuling Zhi Luanfeng Pan Ping Zhou |
author_sort |
Juan Zhao |
title |
Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells |
title_short |
Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells |
title_full |
Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells |
title_fullStr |
Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells |
title_full_unstemmed |
Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells |
title_sort |
trehalose inhibits a53t mutant α-synuclein overexpression and neurotoxicity in transduced pc12 cells |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2017-08-01 |
description |
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. |
topic |
α-synuclein trehalose transduced PC12 cell Parkinson’s disease |
url |
https://www.mdpi.com/1420-3049/22/8/1293 |
work_keys_str_mv |
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