期刊
SCIENTIFIC WORLD JOURNAL
卷 -, 期 -, 页码 -出版社
HINDAWI LTD
DOI: 10.1155/2014/938348
关键词
-
资金
- Natural Science Foundation of China, Inner Mongolia [2011MS1102]
There is striking evidence that heat shock protein 70 (Hsp70) negatively regulates alpha-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 alpha-synuclein aggregation and toxicity in PD still remains to be determined. In the present study, we constructed an alpha-synuclein overexpressed human neuroblastoma cell line, SH-SY5Y-Syn, in which the blockage of Hsp70 promoted alpha-synuclein aggregation. And we also found that miR-16-1 downregulated Hsp70 and promoted alpha-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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