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Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance
Julia Hernandez-Rapp1, Séverine Martin-Lannerée2, Théo Z Hirsch2
1INSERM UMR-S1124 Paris, France ; Sorbonne Paris Cité, UMR-S1124, Université Paris Descartes Paris, France ; Université Paris Sud 11, ED419 Biosigne Orsay, France.
Frontiers in Aging Neuroscience
|March 5, 2014
Summary
The cellular prion protein (PrP(c)) acts as a receptor for amyloid-beta (Aβ) peptides, potentially worsening neurotoxicity. Prion diseases impair Aβ clearance by hijacking PrP(c)-mediated signaling pathways.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Cellular prion protein (PrP(c)) is the normal form of the scrapie prion protein (PrP(Sc)), linked to transmissible spongiform encephalopathies.
- PrP(c) functions as a receptor for amyloid-beta (Aβ) peptides, mediating their neurotoxic effects.
- PrP(Sc) and Aβ can disrupt PrP(c)-dependent signaling pathways, contributing to disease pathogenesis.
Purpose of the Study:
- To summarize the link between PrP-mediated signaling and Aβ clearance.
- To discuss the pathological implications of this interaction.
Main Methods:
- Literature review and synthesis of existing research on PrP(c), Aβ, and neurodegenerative pathways.
- Analysis of studies investigating Aβ clearance mechanisms in prion-infected cells.
Main Results:
- PrP(c) acts as a crucial mediator in the neurotoxicity of Aβ.
- Prion infection leads to impaired Aβ clearance in neuronal cells.
- Disease-associated PrP(Sc) exploits PrP(c) signaling to initiate pathogenic events.
Conclusions:
- The interplay between PrP(c) and Aβ is complex and involves PrP(c)-mediated signaling.
- Dysregulation of Aβ clearance is a pathological consequence of prion infection, linked to PrP(c) signaling.
- Understanding this connection offers insights into neurodegenerative disease mechanisms.
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