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Molecular Mechanism for the Suppression of Alpha Synuclein Membrane Toxicity by an Unconventional Extracellular Chaperone
- Source :
- Journal of the American Chemical Society. 142(21)
- Publication Year :
- 2020
-
Abstract
- Alpha synuclein (αS) oligomers are a key component of Lewy bodies implicated in Parkinson's disease (PD). Although primarily intracellular, extracellular αS exocytosed from neurons also contributes to PD pathogenesis through a prion-like transmission mechanism. Here, we show at progressive degrees of resolution that the most abundantly expressed extracellular protein, human serum albumin (HSA), inhibits αS oligomer (αS
- Subjects :
- Cell Survival
Serum albumin
Serum Albumin, Human
010402 general chemistry
01 natural sciences
Biochemistry
Catalysis
chemistry.chemical_compound
Colloid and Surface Chemistry
Cell Line, Tumor
Extracellular
Humans
Alpha-synuclein
biology
Chemistry
General Chemistry
nervous system diseases
3. Good health
0104 chemical sciences
Cell biology
Membrane
nervous system
Chaperone (protein)
Toxicity
biology.protein
Molecular mechanism
alpha-Synuclein
Hydrophobic and Hydrophilic Interactions
Intracellular
Molecular Chaperones
Subjects
Details
- ISSN :
- 15205126
- Volume :
- 142
- Issue :
- 21
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....366e482b481fd528ea59f3d744590f1f