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Determination of beta-amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry.

Journal article
Authors Erik Portelius
Ann Brinkmalm-Westman
Henrik Zetterberg
Kaj Blennow
Published in Journal of proteome research
Volume 5
Issue 4
Pages 1010-6
ISSN 1535-3893
Publication year 2006
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 1010-6
Language en
Links dx.doi.org/10.1021/pr050475v
Keywords Amino Acid Sequence, Amyloid beta-Protein, cerebrospinal fluid, chemistry, Humans, Mass Spectrometry, methods, Models, Biological, Molecular Sequence Data, Molecular Weight, Peptides, analysis, cerebrospinal fluid, Precipitin Tests, Sensitivity and Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Subject categories Neurochemistry

Abstract

Early pathogenic events in Alzheimer's disease (AD) involve increased production and/or reduced clearance of beta-amyloid (Abeta), especially the 42 amino acid fragment Abeta1-42. The Abeta1-42 peptide is generated through cleavage of the amyloid precursor protein by beta- and gamma-secretase and is catabolised by a variety of proteolytic enzymes such as insulin-degrading enzyme and neprilysin. Here, we describe a method that employs immunoprecipitation combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to determine the pattern of C-terminally truncated Abeta peptides in cerebrospinal fluid (CSF). Using antibodies coupled to magnetic beads, we have detected 18 C-terminally and 2 N-terminally truncated Abeta peptides in CSF. By determining the identity and profile of the truncated Abeta peptides, more insight may be gained about differences in the metabolism and structural properties of Abeta in AD. Finally, the Abeta fragment signatures may prove useful as a diagnostic test for AD.

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