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Updated: Jul 15, 2026
12:57
Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
The cellular prion protein (PrP(C)): its physiological function and role in disease
Laura Westergard1, Heather M Christensen, David A Harris
1Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO 63110, USA.
Biochimica Et Biophysica Acta
|April 25, 2007
Summary
Prion diseases involve normal prion protein (PrP(C)) converting to an infectious form (PrP(Sc)). This review explores PrP(C)
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Prion diseases stem from the misfolding of cellular prion protein (PrP(C)) into infectious PrP(Sc) isoforms.
- While PrP(Sc)'s role in prion propagation is studied, the normal function of PrP(C) remains less understood.
- Understanding PrP(C) function is crucial for deciphering prion disease pathogenesis.
Purpose of the Study:
- To review proposed physiological functions of the cellular prion protein (PrP(C)).
- To explore the potential contribution of PrP(C) dysfunction to prion disease pathology.
- To link PrP(C) mechanisms to other neurodegenerative disorders.
Main Methods:
- Literature review and synthesis of existing research on PrP(C) function.
- Analysis of proposed roles including cytoprotection, copper binding, signaling, and synaptic functions.
- Examination of the link between PrP(C) loss-of-function and neurodegeneration.
Main Results:
- PrP(C) is implicated in protecting cells from apoptosis and oxidative stress.
- Proposed functions include copper ion uptake/binding, transmembrane signaling, and synaptic maintenance.
- PrP(C) may also play a role in cell adhesion to the extracellular matrix.
Conclusions:
- Loss or alteration of PrP(C)'s normal functions may drive prion disease pathogenesis.
- Mechanisms involving PrP(C) dysfunction are likely relevant to other neurodegenerative conditions.
- Further research into PrP(C) physiology is essential for understanding and treating prion and related disorders.
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