Same Protein, With Different Structure, Causes Parkinson's And MSA


Same Protein, With Different Structure, Causes Parkinson's And MSA
Several neurodegenerative disorders are caused by aggregates of a single protein known as alpha-synuclein. Researchers have now discovered that the shape of these aggregates - 'cylinders' or 'ribbons' - determines whether a patient develops Parkinson's disease or Multiple System Atrophy (MSA), respectively. The research was published in the journal Nature.
 
Typical of neurodegenerative disorders is the disrupted communication between brain cells together with a loss of cells in specific brain regions. For some brain diseases this phenomenon is linked to a protein known as alpha-synuclein. The exact function of this protein remains unclear, but it may play a role in the communication between brain cells. However, in the case of specific diseases, including Parkinson's disease, Multiple System Atrophy, and dementia with Lewy bodies (DLB), this protein forms aggregates that cause neurodegeneration. However, up to now, nobody understood how these aggregates of the same protein could induce different pathologies.
 
In 2013, the researchers isolated several forms of fibres called 'strains'. The two most important strains were cylinder-shaped fibres and broad ribbons. They then injected these fibres separately into the brain and blood stream of rats, and noticed that the rats developed different symptoms. While the 'cylinders' induced Parkinson's disease, the 'ribbons' caused MSA symptoms. This clearly demonstrates that distinct diseases result from alpha-synuclein fibres that are structurally different.
 
The findings open up possibilities for the development of new treatments. A drug that counteracts the development of aggregates could be used to treat a whole range of brain diseases. The researchers also suspect that more fibres with different shapes and effects are waiting to be discovered, apart from the two that they examined in this study. 
 
Based on material originally posted by KU Leuven.
If you appreciate our work, consider making a contribution