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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.

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