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Heat shock proteins reduce α‐synuclein aggregation induced by MPP + in SK‐N‐SH cells
Author(s) -
Fan Guo-Hua,
Zhou Hai-Yan,
Yang Hui,
Chen Sheng-Di
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.057
Subject(s) - heat shock protein , chemistry , biophysics , shock (circulatory) , microbiology and biotechnology , biochemistry , biology , medicine , gene
α‐Synuclein has been implicated in the pathogenesis of Parkinson's disease (PD). Heat shock proteins (HSPs) can reduce protein misfolding and accelerate the degradation of misfolded proteins. 1‐methyl‐4‐phenylpyridinium ion (MPP + ) is the compound responsible for the PD‐like neurodegeneration caused by MPTP. In this study, we found that MPP + could increase the expression of α‐synuclein mRNA but could not elevate proteasome activity sufficiently, leading to α‐synuclein protein accumulation followed by aggregation. Both HSPs and HDJ‐1, a homologue of human Hsp40, can inhibit MPP + ‐induced α‐synuclein mRNA expression, promote ubiquitination and elevate proteasome activity. These findings suggest that HSPs may inhibit the MPP + ‐induced α‐synuclein expression, accelerate α‐synuclein degradation, thereby reducing the amount of α‐synuclein protein and accordingly preventing its aggregation.