Abstract
α-Synuclein, a natively unfolded protein aggregation which is implicated in the pathogenesis of Parkinson's disease and several other neurodegenerative diseases, is known to interact with a great number of unrelated proteins. Some of these proteins, such as β-synuclein and DJ-1, were shown to inhibit α-synuclein aggregation in vitro and in vivo therefore acting as chaperones. Since calbindin-D28K is co-localized with Ca2+ neuronal membrane pumps, and since α-synuclein is also found in the membrane proximity, these two proteins can potentially interact in vivo. Here we show that calbindin-D28K interacts with α-synuclein and inhibits its fibrillation in a calcium-dependent manner, therefore potentially acting as a calcium-dependent chaperone.
Original language | English (US) |
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Pages (from-to) | 11-20 |
Number of pages | 10 |
Journal | Central European Journal of Biology |
Volume | 5 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 2010 |
Keywords
- Aggregation
- Fibrillation
- Intrinsically disordered protein
- Parkinson's disease
- α-synuclein