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Updated: Dec 7, 2025
11:29
Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
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Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction
Hajar Miranzadeh Mahabadi1, Changiz Taghibiglou1
1Department of Anatomy, Physiology, Pharmacology, College of Medicine, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada.
International Journal of Molecular Sciences
|September 30, 2020
Summary
Cellular prion protein (PrPc) interacts with various partners, influencing its function and disease roles. Understanding these interactions is key to deciphering prion protein
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Cellular prion protein (PrPc) is a GPI-anchored protein abundant in the CNS.
- PrPc misfolding is linked to neurodegenerative prion diseases.
- PrPc's intrinsically disordered N-terminus facilitates interactions with numerous protein partners.
Purpose of the Study:
- To review intracellular and extracellular interacting partners of PrPc.
- To explore the consequences of PrPc binding to its partners.
- To briefly discuss prion disease-related mutations.
Main Methods:
- Literature review of studies on PrPc interactions.
- Analysis of biochemical and functional consequences of PrPc binding.
- Summary of identified PrPc interacting partners.
Main Results:
- PrPc interacts with a diverse range of intracellular and extracellular proteins.
- These interactions influence PrPc's biochemical characteristics and biological functions.
- Identifying essential binding partners for physiological function remains a challenge.
Conclusions:
- PrPc interactions are crucial for its physiological roles and involvement in prion diseases.
- Further research is needed to validate the necessity of specific PrPc-ligand interactions in cellular function and malfunction.
- Understanding these interactions may offer therapeutic insights for prion diseases.
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