Tau Protein Methods and Protocols
This detailed volume gathers basic and advanced methods and protocols from in vitro assays and in vivo models to address the molecular and functional aspects of tau physiopathology. Divided into five parts that illustrate the underlying molecular mechanis
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Caroline Smet-Nocca Editor
Tau Protein Methods and Protocols
Methods
in
Molecular Biology
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Tau Protein Methods and Protocols
Edited by
Caroline Smet-Nocca UMR CNRS 8576, Villeneuve d’Ascq, France
Editor Caroline Smet-Nocca UMR CNRS 8576 Villeneuve d’Ascq, France
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-6596-0 ISBN 978-1-4939-6598-4 (eBook) DOI 10.1007/978-1-4939-6598-4 Library of Congress Control Number: 2016961536 © Springer Science+Business Media New York 2017 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. Cover illustration: Negative stain electron microscopy with a 200,000 × magnification of PHF-like fibrils made of recombinant Tau protein (longest human isoform) induced by heparin. Printed on acid-free paper This Humana Press imprint is published by Springer Nature The registered company is Springer Science+Business Media LLC The registered company address is: 233 Spring Street, New York, NY 10013, U.S.A.
Preface Isolated from a heat stable fraction of tubulin-bound proteins in 1975, Tau protein was associated a decade later with the paired helical filaments (PHFs) found in neurofibrillary tangles (NFTs) of Alzheimer’s disease (AD) brain. As the main constituent of PHFs, Tau has thus become a pharmacological target of interest. Although phosphorylation is involved in the regulation of Tau microtubule binding activity allowing for neuronal plasticity, Tau in AD brain is found in an abnormally hyperphosphorylated form which combines high level with abnormal phosphorylation (i.e., phosphorylation sites that are not detected in normal adult brains). Tau is mainly found in the axonal compartment of adult mature neurons under physiological conditions, separated from the somatodendritic compartment by a diffusion barrier in
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