Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro

• Published in: Central European journal of biology Vol. 5; no. 1; pp. 11 - 20
• Main Authors: Zhou, Wenbo, Long, Chunmei, Fink, Anthony L., Uversky, Vladimir N.
• Format: Journal Article
• Language: English
• Published: Heidelberg SP Versita 01.02.2010; Versita; De Gruyter
• Subjects: Aggregation; Biochemistry; Biomedical and Life Sciences; Biotechnology; Cell Biology; Fibrillation; Human Genetics; Immunology; Intrinsically disordered protein; Life Sciences; Parkinson’s disease; Research Article; α-synuclein; Aggregation; Fibrillation; Intrinsically disordered protein; Parkinson’s disease; α-synuclein
• ISSN: 1895-104X; 2391-5412; 1644-3632; 2391-5412
• DOI: 10.2478/s11535-009-0071-8

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-D 28K is co-localized with Ca 2+ 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.