miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70

There is striking evidence that heat shock protein 70 (Hsp70) negatively regulates α-synuclein aggregation, which plays a significant role in the formation and progression of Parkinson disease (PD). However, how the Hsp70 in neurons fails to prevent or even reverse α-synuclein aggregation and toxici...

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Main Authors: Zhelin Zhang, Yan Cheng
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1155/2014/938348
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author Zhelin Zhang
Yan Cheng
author_facet Zhelin Zhang
Yan Cheng
author_sort Zhelin Zhang
collection DOAJ
description There is striking evidence that heat shock protein 70 (Hsp70) negatively regulates α-synuclein aggregation, which plays a significant role in the formation and progression of Parkinson disease (PD). However, how the Hsp70 in neurons fails to prevent or even reverse α-synuclein aggregation and toxicity in PD still remains to be determined. In the present study, we constructed an α-synuclein-overexpressed human neuroblastoma cell line, SH-SY5Y-Syn, in which the blockage of Hsp70 promoted α-synuclein aggregation. And we also found that miR-16-1 downregulated Hsp70 and promoted α-synuclein aggregation in the SH-SY5Y-Syn cells. This study revealed a novel regulatory mechanism of Hsp70 expression, which might contribute to the PD development.
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institution Kabale University
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language English
publishDate 2014-01-01
publisher Wiley
record_format Article
series The Scientific World Journal
spelling doaj-art-fcf4dea1bc93467cba9c8d6b557236b32025-02-03T05:43:37ZengWileyThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/938348938348miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70Zhelin Zhang0Yan Cheng1Department of Neurology, General Hospital of Tianjin Medical University, No. 154, Anshan road, Heping District, Tianjin 300071, ChinaDepartment of Neurology, General Hospital of Tianjin Medical University, No. 154, Anshan road, Heping District, Tianjin 300071, ChinaThere is striking evidence that heat shock protein 70 (Hsp70) negatively regulates α-synuclein aggregation, which plays a significant role in the formation and progression of Parkinson disease (PD). However, how the Hsp70 in neurons fails to prevent or even reverse α-synuclein aggregation and toxicity in PD still remains to be determined. In the present study, we constructed an α-synuclein-overexpressed human neuroblastoma cell line, SH-SY5Y-Syn, in which the blockage of Hsp70 promoted α-synuclein aggregation. And we also found that miR-16-1 downregulated Hsp70 and promoted α-synuclein aggregation in the SH-SY5Y-Syn cells. This study revealed a novel regulatory mechanism of Hsp70 expression, which might contribute to the PD development.http://dx.doi.org/10.1155/2014/938348
spellingShingle Zhelin Zhang
Yan Cheng
miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
The Scientific World Journal
title miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
title_full miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
title_fullStr miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
title_full_unstemmed miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
title_short miR-16-1 Promotes the Aberrant α-Synuclein Accumulation in Parkinson Disease via Targeting Heat Shock Protein 70
title_sort mir 16 1 promotes the aberrant α synuclein accumulation in parkinson disease via targeting heat shock protein 70
url http://dx.doi.org/10.1155/2014/938348
work_keys_str_mv AT zhelinzhang mir161promotestheaberrantasynucleinaccumulationinparkinsondiseaseviatargetingheatshockprotein70
AT yancheng mir161promotestheaberrantasynucleinaccumulationinparkinsondiseaseviatargetingheatshockprotein70