Heat shock proteins reduce alpha-synuclein aggregation induced by MPP+ in SK-N-SH cells.
FEBS Lett
; 580(13): 3091-8, 2006 May 29.
Article
en En
| MEDLINE
| ID: mdl-16678164
ABSTRACT
Alpha-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 alpha-synuclein mRNA but could not elevate proteasome activity sufficiently, leading to alpha-synuclein protein accumulation followed by aggregation. Both HSPs and HDJ-1, a homologue of human Hsp40, can inhibit MPP+-induced alpha-synuclein mRNA expression, promote ubiquitination and elevate proteasome activity. These findings suggest that HSPs may inhibit the MPP+-induced alpha-synuclein expression, accelerate alpha-synuclein degradation, thereby reducing the amount of alpha-synuclein protein and accordingly preventing its aggregation.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Enfermedad de Parkinson
/
Proteínas del Choque Térmico HSP40
/
Alfa-Sinucleína
/
Proteínas de Choque Térmico
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2006
Tipo del documento:
Article
País de afiliación:
China