Format

Send to

Choose Destination
ScientificWorldJournal. 2014;2014:938348. doi: 10.1155/2014/938348. Epub 2014 Jun 23.

miR-16-1 promotes the aberrant α-synuclein accumulation in parkinson disease via targeting heat shock protein 70.

Author information

1
Department of Neurology, General Hospital of Tianjin Medical University, No. 154, Anshan road, Heping District, Tianjin 300071, China ; Department of Neurology, Affiliated Hospital of Inner Mongolia Medical University, No. 1 Tongdao North Street, Hohhot, Mongolia 010059, China.
2
Department of Neurology, General Hospital of Tianjin Medical University, No. 154, Anshan road, Heping District, Tianjin 300071, China.

Abstract

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.

PMID:
25054189
PMCID:
PMC4094852
DOI:
10.1155/2014/938348
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Hindawi Limited Icon for PubMed Central
Loading ...
Support Center