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

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.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro ; volume:5 ; number:1 ; year:2010 ; pages:11-20 ; extent:10 ; Open life sciences ; 5, Heft 1 (2010), 11-20 (gesamt 10)

Contributors, Places and Time

• Creator: Zhou, Wenbo ; Long, Chunmei ; Fink, Anthony ; Uversky, Vladimir

Further information

• DOI: 10.2478/s11535-009-0071-8
• URN: urn:nbn:de:101:1-2409201850569.358794111874
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 15.08.2025, 7:32 AM CEST