Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro
| Autor: | Anthony L. Fink, Vladimir N. Uversky, Wenbo Zhou, Chunmei Long |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Parkinson's disease
parkinson’s disease QH301-705.5 Protein aggregation General Biochemistry Genetics and Molecular Biology Pathogenesis α-synuclein In vivo mental disorders medicine fibrillation Biology (General) Fibrillation General Immunology and Microbiology biology General Neuroscience aggregation intrinsically disordered protein medicine.disease In vitro nervous system diseases Cell biology Membrane nervous system Biochemistry Chaperone (protein) biology.protein medicine.symptom General Agricultural and Biological Sciences |
| Zdroj: | Open Life Sciences, Vol 5, Iss 1, Pp 11-20 (2010) |
| ISSN: | 2391-5412 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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