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Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: prevention by systemic passive immunization.

Journal article
Authors Igor Klyubin
Vicki Betts
Alfred T Welzel
Kaj Blennow
Henrik Zetterberg
Anders Wallin
Cynthia A Lemere
William K Cullen
Ying Peng
Thomas Wisniewski
Dennis J Selkoe
Roger Anwyl
Dominic M Walsh
Michael J Rowan
Published in The Journal of neuroscience : the official journal of the Society for Neuroscience
Volume 28
Issue 16
Pages 4231-7
ISSN 1529-2401
Publication year 2008
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 4231-7
Language en
Links dx.doi.org/10.1523/JNEUROSCI.5161-0...
Keywords Alzheimer Disease, immunology, metabolism, therapy, Amyloid beta-Protein, administration & dosage, cerebrospinal fluid, immunology, Animals, Antibodies, Monoclonal, administration & dosage, CHO Cells, Cricetinae, Cricetulus, Dimerization, Humans, Immunization, Passive, methods, Long-Term Potentiation, immunology, Male, Neuronal Plasticity, immunology, Rats, Rats, Wistar, Synapses, immunology
Subject categories Medical and Health Sciences

Abstract

The current development of immunotherapy for Alzheimer's disease is based on the assumption that human-derived amyloid beta protein (Abeta) can be targeted in a similar manner to animal cell-derived or synthetic Abeta. Because the structure of Abeta depends on its source and the presence of cofactors, it is of great interest to determine whether human-derived oligomeric Abeta species impair brain function and, if so, whether or not their disruptive effects can be prevented using antibodies. We report that untreated ex vivo human CSF that contains Abeta dimers rapidly inhibits hippocampal long-term potentiation in vivo and that acute systemic infusion of an anti-Abeta monoclonal antibody can prevent this disruption of synaptic plasticity. Abeta monomer isolated from human CSF did not affect long-term potentiation. These results strongly support a strategy of passive immunization against soluble Abeta oligomers in early Alzheimer's disease.

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