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Alpha-synuclein and the prion hypothesis in Parkinson's disease
1Institut François-Jacob, MIRCen, CEA, laboratory of Neurodegenerative Diseases, CNRS, 18, route du Panorama, 92265 Fontenay-aux-Roses cedex, France.
Revue Neurologique
|September 12, 2018
Summary
Misfolded alpha-synuclein protein aggregates spread between cells in the brain, similar to prion diseases. This propagation mechanism may explain the development of distinct synucleinopathies.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Protein intracellular inclusions in the central nervous system characterize neurodegenerative disorders.
- The spread of misfolded protein aggregates was previously thought to be unique to prion protein (PrP).
Purpose of the Study:
- To review experimental evidence for alpha-synuclein aggregate propagation.
- To explain how alpha-synuclein assemblies traffic, amplify, and cause distinct synucleinopathies.
Main Methods:
- Review of experimental evidence on alpha-synuclein mega-dalton assemblies.
- Analysis of cellular trafficking and amplification mechanisms of alpha-synuclein.
Main Results:
- Experimental data support the propagation of alpha-synuclein aggregates similarly to prion protein.
- Alpha-synuclein assemblies traffic between cells and amplify by recruiting endogenous monomers.
Conclusions:
- Alpha-synuclein aggregation and propagation contribute to distinct synucleinopathies.
- Understanding this mechanism is crucial for neurodegenerative disease research.