期刊
JOURNAL OF NEUROSCIENCE
卷 31, 期 20, 页码 7259-7263出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.6500-10.2011
关键词
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资金
- Science Foundation Ireland [08/IN. 1/B2033, 06/IN. 1/B88, 10/IN. 1/B3001]
- Health Research Board
- European Commission [200611, 201159]
- Science Foundation Ireland (SFI) [06/IN.1/B88, 08/IN.1/B2033, 10/IN.1/B3001] Funding Source: Science Foundation Ireland (SFI)
Synthetic amyloid-beta protein (A beta) 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 beta in vitro is controversial. Here we report that intracerebroventricular injection of A beta-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 A beta. Importantly, intracerebroventricular administration of antigen-binding antibody fragment D13, directed to a putative A beta-binding site on PrPC, prevented the inhibition of LTP by AD brain-derived A beta. In contrast, R1, a Fab directed to the C terminus of PrPC, a region not implicated in binding of A beta, did not significantly affect the A beta-mediatedinhibition of LTP. These data support the pathophysiological significance of SDS-stable A beta dimer and the role of PrPC in mediating synaptic plasticity disruption by soluble A beta.
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