Lack of direct role of parkin in the steady-state level and aggregation of alpha-synuclein and the clearance of pre-formed aggregates |
| |
Authors: | Kim Yoon Suk Patel Smita Lee Seung-Jae |
| |
Affiliation: | The Parkinson's Institute, 1170 Morse Avenue, Sunnyvale, CA 94089, USA. |
| |
Abstract: | Mutations in parkin and alpha-synuclein (alpha-syn) are linked to heritable forms of Parkinson's disease (PD). Recently, it has been shown that parkin mitigates alpha-syn-induced neuronal cell death in animal and tissue culture models, suggesting that there is a functional relationship between these two proteins. Although the mechanism by which parkin protects cells from alpha-syn-induced cytotoxicity remains elusive, it is tempting to speculate that parkin might directly regulate the normal metabolism and aggregation of alpha-syn. In the current study, we show that neither the suppression of endogenous parkin expression nor ectopic overexpression affects the steady-state levels of endogenous alpha-syn expression, overall aggregation of this protein, or breakdown of pre-formed aggregates in human neuroblastoma cells. These results suggest that parkin is not directly involved in the metabolism of alpha-syn, its aggregation, or the clearance of pre-formed aggregates. |
| |
Keywords: | Parkin α -synuclein Protein aggregation RNA interference Adenoviral vector Parkinson's disease |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|