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An integrated workflow for multiplex CSF proteomics and peptidomics - identification of candidate cerebrospinal fluid biomarkers of Alzheimer's disease.

Journal article
Authors Mikko Hölttä
Lennart Minthon
Oscar Hansson
Jessica Holmén Larsson
Ian Pike
Malcolm Ward
Karsten Kuhn
Ulla Rüetschi
Henrik Zetterberg
Kaj Blennow
Johan Gobom
Published in Journal of proteome research
Volume 14
Issue 2
Pages 654-663
ISSN 1535-3907
Publication year 2015
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 654-663
Language en
Links dx.doi.org/10.1021/pr501076j
Subject categories Neurochemistry

Abstract

Many disease processes in the brain are reflected in the protein composition of the cerebrospinal fluid (CSF). In addition to proteins, CSF also contains a large number of endogenous peptides whose potential as disease biomarkers largely remains to be explored. We have developed a novel workflow in which multiplex isobaric labeling is used for simultaneous quantification of endogenous CSF peptides and proteins by LC-MS. After labeling of CSF samples, endogenous peptides are separated from proteins by ultrafiltration. The proteins retained on the filters are trypsinized and the tryptic peptides collected separately. We evaluated this technique in a comparative pilot study of CSF peptide and protein profiles in eight patients with Alzheimer's disease (AD) and eight non-demented controls. We identified several differences between the AD and control group among endogenous peptides derived from proteins known to be associated with AD, including neurosecretory protein VGF (ratios AD/controls 0.45-0.81), integral membrane protein 2B (ratios AD/controls 0.72-0.84), and metallothionein-3 (ratios AD/controls 0.51-0.61). Analysis of tryptic peptides identified several proteins that were altered in the AD group, some of which have previously been reported as changed in AD, e.g. VGF (ratio AD/controls 0.70).

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