Laurén et al. reply

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
David A. Gimbel: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine
Haakon B. Nygaard: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine
John W. Gilbert: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine
Stephen M. Strittmatter: Cellular Neuroscience, Neurodegeneration and Repair Program, Yale University School of Medicine

Nature, 2010, vol. 466, issue 7308, E4-E5

Abstract: Abstract Replying to: H. W. Kessels, L. N. Nguyen, S. Nabavi & R. Malinow Nature 466, 10.1038/nature09217 (2010) Amyloid-β oligomers are correlated with Alzheimer’s disease progression and suppress synaptic plasticity1,2,3. Through unbiased expression cloning, we identified cellular prion protein (PrPC) as an amyloid-β oligomer binding protein4. PrPC was necessary for acute amyloid-β(1−42) (Aβ42) oligomer suppression of synaptic plasticity4; thus, it becomes critical to explore the importance of PrPC in a range of Alzheimer’s-disease-related deficits. Transgenic Alzheimer’s disease model mice show deficits of spatial learning and memory5, so the most direct assessment of PrPC will monitor memory in transgenic Alzheimer’s disease model mice deficient for PrPC. In this paradigm, amyloid-β species are produced endogenously and the brain is exposed chronically over months. Recently, we have found that deletion of PrPC from APPswe/PSen1ΔE9 transgenic mice restores spatial learning and memory without altering amyloid-β6. Furthermore, the early death, synapse loss and serotonin axonal degeneration of transgenic Alzheimer’s disease mice require PrPC (ref. 6). Kessels et al. 7 examine PrPC in alternative paradigms.

Date: 2010
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature09218 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:466:y:2010:i:7308:d:10.1038_nature09218

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

DOI: 10.1038/nature09218

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 ().