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Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
Laura Urrea1,2,3,4, Miriam Segura-Feliu1,2,3,4, Masami Masuda-Suzukake5
1Molecular and Cellular Neurobiotechnology, Institute of Bioengineering of Catalonia (IBEC), Parc Científic de Barcelona, Baldiri Reixac 15-21, E-08028, Barcelona, Spain.
Molecular Neurobiology
|February 24, 2017
Summary
The cellular prion protein (PrPC) is not essential for α-synuclein spreading. However, PrPC can accelerate α-synuclein expansion and bind to α-synuclein fibrils, suggesting a role in modulating its effects.
Area of Science:
- Neuroscience
- Molecular Biology
- Protein Misfolding Diseases
Background:
- The cellular prion protein (PrPC), encoded by the Prnp gene, acts as a receptor for β-amyloid, mediating its neurotoxicity.
- Understanding the role of PrPC in the propagation of other misfolded proteins is crucial for neurodegenerative disease research.
Purpose of the Study:
- To investigate the potential involvement of PrPC in the cell-to-cell spreading of α-synuclein.
- To determine if PrPC influences the rate and extent of pathological α-synuclein propagation.
Main Methods:
- Utilizing mouse models with varying levels of PrPC expression.
- Assessing the spreading of α-synuclein pathology in vivo.
- Investigating the binding interactions between α-synuclein and PrPC-expressing cells.
Main Results:
- Prnp gene expression is not mandatory for the initiation or progression of α-synuclein spreading.
- α-synuclein spreading occurred, albeit at a slower rate, in the absence of Prnp.
- α-synuclein exhibited faster spreading in mice overexpressing PrPC.
- Strong binding of α-synuclein to PrPC-expressing cells was observed.
Conclusions:
- PrPC is not required for α-synuclein spreading but can modulate its rate.
- The interaction between α-synuclein and PrPC suggests a potential role for PrPC in influencing the pathological effects of α-synuclein fibrils.
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