Abstract
Alzheimer's disease (AD) is associated with pathological assembly states of amyloid-β protein (Aβ). Aβ-related synaptotoxicity can be blocked by anti-prion protein (PrP) antibodies, potentially allowing therapeutic targeting of this aspect of AD neuropathogenesis. Here, we show that intravascular administration of a high-affinity humanized anti-PrP antibody to rats can prevent the plasticity-disrupting effects induced by exposure to soluble AD brain extract. These results provide an in vivo proof of principle for such a therapeutic strategy.
Keywords:
Alzheimer's; drug discovery; immunotherapy; long-term potentiation; prion.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aged, 80 and over
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Alzheimer Disease / pathology*
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Amyloid beta-Peptides / pharmacology*
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Analysis of Variance
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Animals
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Antibodies, Monoclonal / administration & dosage*
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Biophysics
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CA1 Region, Hippocampal / drug effects*
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Drug Administration Routes
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Electric Stimulation
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Enzyme-Linked Immunosorbent Assay
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Female
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Humans
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Long-Term Potentiation / drug effects*
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Male
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Peptide Fragments / pharmacology*
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Prions / immunology*
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Prions / metabolism
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Rats
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Rats, Wistar
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Temporal Lobe / chemistry
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Temporal Lobe / metabolism
Substances
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Amyloid beta-Peptides
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Antibodies, Monoclonal
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Peptide Fragments
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Prions
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amyloid beta-protein (1-42)