The prion protein as a receptor for amyloid-[Beta]/Laurén et al. reply

Amyloid-β(1242) peptides (Aβ42) formoligomers, and when exogenously applied they produced a similar loss of dendritic spines in slices prepared from either wildtype or PrPC-lacking mice (Fig. 1c). [...] the loss of dendritic spines produced by oligomeric Aβ42 exposure does not depend on PrPC. [.....

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Bibliographic Details
Published inNature (London) Vol. 466; no. 7308; p. E3
Main Authors Kessels, Helmut W, Nguyen, Louis N, Nabavi, Sadegh, Malinow, Roberto, Laurén, Juha, Gimbel, David A, Nygaard, Haakon B, Gilbert, John W, Strittmatter, Stephen M
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group 12.08.2010
Subjects
Alzheimer's disease
Embargoes & blockades
Neurons
Prions
Proteins
Rodents
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Summary:Amyloid-β(1242) peptides (Aβ42) formoligomers, and when exogenously applied they produced a similar loss of dendritic spines in slices prepared from either wildtype or PrPC-lacking mice (Fig. 1c). [...] the loss of dendritic spines produced by oligomeric Aβ42 exposure does not depend on PrPC. [...] Kessels et al.7 overexpressed carboxy-terminal amyloid precursor protein (APP) in cultured neurons. To our knowledge, there is no evidence that local viral expression produces pathological amyloid-b oligomers. Because PrPC shows little affinity for amyloid-b monomer4, it follows that the effects of viral APP will be unaltered in Prnp-/- neurons.
ISSN:0028-0836
1476-4687