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Characterization of tau in cerebrospinal fluid using mass spectrometry.

Journal article
Authors Erik Portelius
Sara Folkesson Hansson
Ai Jun Tran
Henrik Zetterberg
Pierre Grognet
Eugeen Vanmechelen
Kina Höglund
Gunnar Brinkmalm
Ann Brinkmalm-Westman
Eckhard Nordhoff
Kaj Blennow
Johan Gobom
Published in Journal of proteome research
Volume 7
Issue 5
Pages 2114-20
ISSN 1535-3893
Publication year 2008
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 2114-20
Language en
Links dx.doi.org/10.1021/pr7008669
Keywords Alzheimer Disease, metabolism, Amino Acid Sequence, Brain Chemistry, Chromatography, Liquid, methods, Humans, Immunoprecipitation, methods, Mass Spectrometry, methods, Molecular Sequence Data, Peptide Fragments, cerebrospinal fluid, chemistry, Protein Isoforms, cerebrospinal fluid, chemistry, genetics, tau Proteins, cerebrospinal fluid, chemistry, genetics
Subject categories Medical and Health Sciences

Abstract

The neurodegenerative disorder Alzheimer's disease (AD) is the most common cause of dementia in the elderly. The presence of neurofibrillary tangles, consisting of hyperphosphorylated tau protein, is one of the major neuropathologic characteristics of the disease, making this protein an attractive biomarker for AD and a possible target for therapy. Here, we describe an optimized immunoprecipitation mass spectrometry method that enables, for the first time, detailed characterization of tau in human cerebrospinal fluid. The identities of putative tau fragments were confirmed using nanoflow liquid chromatography and tandem mass spectrometry. Nineteen tryptic fragments of tau were detected, of which 16 are found in all tau isoforms while 3 represented unique tau isoforms. These results pave the way for clinical CSF studies on the tauopathies.

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