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• W2898873142 abstract "Genetic studies have revealed that rare mutations and multiplications of the gene locus in α-synuclein (α-syn) are implicated in the pathogenesis of Parkinson's disease (PD). However, the pathological effects of α-syn are still obscure. The neurotoxicity of α-syn is mainly determined by its protein levels, which depend on a balance between synthesis and degradation. Therefore, verifying the possible routes contributing to the clearance of α-syn is important for PD therapy. In this study, we established stable lines overexpressing human wild-type (WT) and E46K mutant α-syn in rat PC12 cells and investigated the degradation pathways of α-syn by using a panel of inhibitors and inducers of lysosome and proteasome function. We also monitored the degradation kinetics of α-syn by using cycloheximide to block protein synthesis. Our data showed that both proteasome and chaperon-mediated autophagy (CMA) are responsible for the degradation of the WT α-syn. Meanwhile, E46K mutant α-syn is mainly degraded by the proteasome and macroautophagy pathway. Compared with the WT protein, E46K mutant α-syn turned over more slowly in PC12 cells. In addition, overexpression of E46K mutant α-syn increased vulnerability of PC12 cells to apoptosis insults when compared with WT α-syn. Our findings may verify the possible routes contributing to the degradation of the E46K mutant α-syn." @default.
• W2898873142 created "2018-11-09" @default.
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• W2898873142 date "2018-11-01" @default.
• W2898873142 modified "2023-10-01" @default.
• W2898873142 title "E46K Mutant α-Synuclein Is Degraded by Both Proteasome and Macroautophagy Pathway" @default.
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• W2898873142 doi "https://doi.org/10.3390/molecules23112839" @default.
• W2898873142 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6278282" @default.
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• W2898873142 hasPublicationYear "2018" @default.
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