Document Type
Article
Publication Date
2010
Keywords
Parkinson's Disease, α-synuclein, Fibrillation, Aggregation, Intrinsically Disordered Protein
Digital Object Identifier (DOI)
https://doi.org/10.2478/s11535-009-0071-8
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 ß-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
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Open Life Sciences, v. 5, issue 1, p. 11-20
Scholar Commons Citation
Zhou, Wenbo; Long, Chunmei; Fink, Anthony L.; and Uversky, Vladimir N., "Calbindin-d28k Acts as a Calcium-dependent Chaperone Suppressing α-synuclein Fibrillation in Vitro" (2010). Molecular Medicine Faculty Publications. 546.
https://digitalcommons.usf.edu/mme_facpub/546
