Cellular Trafficking of Cell Stress Proteins in Health and Disease
Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between
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HEAT SHOCK PROTEINS Volume 6
Series Editors: A. A. A. Asea Department of Microbiology, Biochemistry and Immunology (MBI), Morehouse School of Medicine, 720 Westview Ave., SW, Atlanta, GA 30310, USA
S. K. Calderwood Division of Molecular and Cellular Radiation Oncology, Beth Israel Deaconness Medical Center and Harvard Medical School
For further volumes: http://www.springer.com/series/7515
Brian Henderson • A. Graham Pockley Editors
Cellular Trafficking of Cell Stress Proteins in Health and Disease
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Editors Prof. Brian Henderson Department of Microbial Diseases UCL-Eastman Dental Institute University College London United Kingdom
Prof. A. Graham Pockley John van Geest Cancer Research Centre Nottingham Trent University Nottingham United Kingdom
ISSN 1877-1246 ISSN 1877-1254 (Electronic) ISBN 978-94-007-4739-5 ISBN 978-94-007-4740-1 (eBook) DOI 10.1007/978-94-007-4740-1 Springer Dordrecht Heidelberg London NewYork Library of Congress Control Number: 2012951299 © Springer Science+Business Media Dordrecht 2012 No part of this work may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording or otherwise, without written permission from the Publisher, with the exception of any material supplied specifically for the purpose of being entered and executed on a computer system, for exclusive use by the purchaser of the work. Springer is part of Springer Science+Business Media (www.springer.com)
Preface
The establishment that cells responded to stress by the induction of specific gene expression led to the identification, in the 1980s, of heat shock or cell stress proteins and the realisation that these proteins are involved in the folding, re-folding, and prevention of aggregation, of client proteins. Such protein-folding proteins are now known as molecular chaperones, with the term protein-folding catalysts (PFCs) being applied to proteins such as thioredoxin and peptidyl prolyl isomerases that involve an enzymic step in the protein folding mechanism. Initially, these proteins were thought to be exclusively intracellular. However, in 1988 evidence was presented for the secretion and uptake of Hsp70 proteins by cultured cells suggesting that at least one molecular chaperone underwent aberrant cellular trafficking. Some years later the aberrant cytoplasmic and cell surface location of the mitochondrial Hsp60 protein began to be defined. These finding suggested a potentially wider remit for the function of molecular chaperones within the cell than had previously been considered. A growing number of reports in the 1990s established that a number of molecular chaperones and PFCs had cell signalling actions when applied externally to cultured cells, and this realisation has prompted a rapid expansion of work in this field. Despite being dogged by suggestions that the biological and immunological properties of extracellular stress proteins results from contaminants in the preparations used, it is now becoming accepted t
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