Amyloid-beta oligomer detection by ELISA in cerebrospinal fluid and brain tissue
Publication year
2013Source
Analytical Biochemistry, 433, 2, (2013), pp. 112-20ISSN
Publication type
Article / Letter to editor
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Organization
Neurology
Laboratory of Genetic, Endocrine and Metabolic Diseases
Geriatrics
Journal title
Analytical Biochemistry
Volume
vol. 433
Issue
iss. 2
Page start
p. 112
Page end
p. 20
Subject
DCN MP - Plasticity and memory; DCN NN - Brain networks and neuronal communication; DCN PAC - Perception action and control NCEBP 11: Alzheimer Centre; NCEBP 14: Cardiovascular diseases; Laboratory Medicine - Radboud University Medical CenterAbstract
Amyloid-beta (Abeta) deposits are important pathological hallmarks of Alzheimer's disease (AD). Abeta aggregates into fibrils; however, the intermediate oligomers are believed to be the most neurotoxic species and, therefore, are of great interest as potential biomarkers. Here, we have developed an enzyme-linked immunosorbent assay (ELISA) specific for Abeta oligomers by using the same capture and (labeled) detection antibody. The ELISA predominantly recognizes relatively small oligomers (10-25 kDa) and not monomers. In brain tissue of APP/PS1 transgenic mice, we found that Abeta oligomer levels increase with age. However, for measurements in human samples, pretreatment to remove human anti-mouse antibodies (HAMAs) was required. In HAMA-depleted human hippocampal extracts, the Abeta oligomer concentration was significantly increased in AD compared with nondemented controls. Abeta oligomer levels could also be quantified in pretreated cerebrospinal fluid (CSF) samples; however, no difference was detected between AD and control groups. Our data suggest that levels of small oligomers might not be suitable as biomarkers for AD. In addition, we demonstrate the importance of avoiding HAMA interference in assays to quantify Abeta oligomers in human body fluids.
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- Faculty of Medical Sciences [93209]
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