RGD Reference Report - Alzheimer's disease brain-derived amyloid-ß-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. - Rat Genome Database

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Alzheimer's disease brain-derived amyloid-ß-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein.

Authors: Barry, Andrew E  Klyubin, Igor  Mc Donald, Jessica M  Mably, Alexandra J  Farrell, Michael A  Scott, Michael  Walsh, Dominic M  Rowan, Michael J 
Citation: Barry AE, etal., J Neurosci. 2011 May 18;31(20):7259-63. doi: 10.1523/JNEUROSCI.6500-10.2011.
RGD ID: 12790639
Pubmed: PMID:21593310   (View Abstract at PubMed)
PMCID: PMC6622598   (View Article at PubMed Central)
DOI: DOI:10.1523/JNEUROSCI.6500-10.2011   (Journal Full-text)

Synthetic amyloid-ß protein (Aß) oligomers bind with high affinity to cellular prion protein (PrP(C)), but the role of this interaction in mediating the disruption of synaptic plasticity by such soluble Aß in vitro is controversial. Here we report that intracerebroventricular injection of Aß-containing aqueous extracts of Alzheimer's disease (AD) brain robustly inhibits long-term potentiation (LTP) without significantly affecting baseline excitatory synaptic transmission in the rat hippocampus in vivo. Moreover, the disruption of LTP was abrogated by immunodepletion of Aß. Importantly, intracerebroventricular administration of antigen-binding antibody fragment D13, directed to a putative Aß-binding site on PrP(C), prevented the inhibition of LTP by AD brain-derived Aß. In contrast, R1, a Fab directed to the C terminus of PrP(C), a region not implicated in binding of Aß, did not significantly affect the Aß-mediated inhibition of LTP. These data support the pathophysiological significance of SDS-stable Aß dimer and the role of PrP(C) in mediating synaptic plasticity disruption by soluble Aß.



Gene Ontology Annotations    

Biological Process

Objects Annotated

Genes (Rattus norvegicus)
Prnp  (prion protein)


Additional Information