کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2052591 | 1074234 | 2006 | 8 صفحه PDF | دانلود رایگان |
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.
Journal: FEBS Letters - Volume 580, Issue 13, 29 May 2006, Pages 3091–3098