Abstract
Alzheimer disease (AD) is the most prevalent cause of dementia. Amyloid-β (Aβ) oligomers are potent synaptotoxins thought to mediate AD-related phenotypes. Cellular prion protein (PrPc) has been identified as a high-affinity receptor for Aβ oligomers. Herein, we review the functional consequences of Aβ oligomer binding to PrPc on the neuronal surface. We highlight recent evidence that Fyn kinase mediates signal transduction downstream of the PrPc-Aβ oligomer complex. These studies suggest that PrPC has a central role in AD pathogenesis and may provide a target for therapeutic intervention in AD.
| Original language | English |
|---|---|
| Pages (from-to) | 37-41 |
| Number of pages | 5 |
| Journal | Prion |
| Volume | 7 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2013 |
Bibliographical note
Funding Information:We acknowledge support from the National Institutes of Health, the Falk Medical Research Trust and the Alzheimer Association to S.M.S. S.M.S. is a member of the Kavli Institute for Neuroscience at Yale University. S.M.S. is a co-founder of Axerion Therapeutics, seeking to develop NgR-and PrP-based therapeutics.
Keywords
- Alzheimer disease
- Cellular prion protein
- Fyn kinase
- PrP
- Prion
