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Title: Alzheimer's disease brain-derived amyloid-ß-mediated inhibition of LTP In Vivo is prevented by immunotargeting cellular prion protein
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Keywords: Alzheimer’s disease
Issue Date: 2011
Citation: Barry, A.E., Klyubin, I., McDonald, J.M., Mably, A.J., Farrell, M.A., Scott, M., Walsh, D.M., Rowan, M.J., Alzheimer's disease brain-derived amyloid-ß-mediated inhibition of LTP In Vivo is prevented by immunotargeting cellular prion protein, Journal of Neuroscience, 31, 20, 2011, 7259-7263
Series/Report no.: Journal of Neuroscience
Abstract: Synthetic amyloid- protein (A ) oligomers bind with high affinity to cellular prion protein (PrPC), but the role of this interaction in mediating the disruption of synaptic plasticity by such soluble A in vitro is controversial. Here we report that intracerebroventricular injection of A -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 immunodepletionofA . Importantly, intracerebroventricular administration of antigen-binding antibody fragment D13, directed to a putative A -binding site on PrPC, prevented the inhibition of LTP by AD brain-derived A . In contrast, R1, a Fab directed to the C terminus of PrPC, a regionnotimplicatedinbindingofA ,didnotsignificantly affect theA -mediatedinhibition ofLTP.These data support the pathophysiological significance of SDS-stable A dimer and the role of PrPC in mediating synaptic plasticity disruption by soluble A .
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Appears in Collections:Pharmacology & Therapeutics (Scholarly Publications)

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