Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Juha Laurén, David A. Gimbel, Haakon B. Nygaard, John W. Gilbert and Stephen M. Strittmatter ()
Additional contact information
Juha Laurén: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine, New Haven, Connecticut 06536, USA
David A. Gimbel: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine, New Haven, Connecticut 06536, USA
Haakon B. Nygaard: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine, New Haven, Connecticut 06536, USA
John W. Gilbert: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine, New Haven, Connecticut 06536, USA
Stephen M. Strittmatter: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine, New Haven, Connecticut 06536, USA

Nature, 2009, vol. 457, issue 7233, 1128-1132

Abstract: Prion link to Alzheimer's The hypothesis that soluble amyloid-β peptide oligomer plays a central role in Alzheimer's disease is well established, yet no mechanistic basis for Aβ oligomer effects on neurons has been described. Several lines of evidence point to the existence of a high-affinity cell-surface receptor for soluble Aβ oligomers on neurons as central to Alzheimer's disease pathology and now cellular prion protein PrPC has been identified as a candidate for that role. PrP, a plasma membrane glycoprotein associated with lipid rafts, binds Aβ oligomers selectively with high affinity and mediates the deleterious effects of the peptide. These data raise the possibility that PrPC-specific drugs might have therapeutic potential in Alzheimer's, and point to an unexpected link between infectious prion diseases and Alzheimer's disease.

Date: 2009
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature07761 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:457:y:2009:i:7233:d:10.1038_nature07761

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature07761

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().