title: miR-16-1 promotes the aberrant α-synuclein accumulation in parkinson disease via targeting heat shock protein 70.
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.
authors: 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.
authors: Zhelin
authors: Z
authors: Zhang
authors: Department of Neurology, General Hospital of Tianjin Medical University, No. 154, Anshan road, Heping District, Tianjin 300071, China.
authors: Yan
authors: Y
authors: Cheng
mesh_terms: D045744:Cell Line, Tumor; D015536:Down-Regulation; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D035683:MicroRNAs / Q000235:genetics / Q000378:metabolism*; D010300:Parkinson Disease / Q000378:metabolism*; D066263:Protein Aggregation, Pathological / Q000378:metabolism*; D051844:alpha-Synuclein / Q000235:genetics / Q000378:metabolism*
chemical_list: D018840:HSP70 Heat-Shock Proteins; C505362:MIRN16 microRNA, human; D035683:MicroRNAs; C497604:SNCA protein, human; D051844:alpha-Synuclein