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The topic of cell stress proteins or molecular chaperones/heat shock proteins now pervades many branches of the biological science and biomedicine. These proteins interest biochemists, biophysicists and structural biologists because of the complexity of their structures and of their functions. They intrigue molecular and cellular biologists who are trying to ascertain how their synthesis is controlled and what their overall role in the normal and stressed cell. Immunologists have been trying to determine their role in immune regulation for three decades as have virologists, bacteriologists and parasitologists their role in infection. Indeed, the latest infecting agent, the prion, turns out to be a rogue molecular chaperone. In the medical profession, molecular chaperones have been invoked in the pathology of just about every human disease. This has interested the pharmacologists who are now seeking ways of modulating molecular chaperones for therapeutic purposes. In the last decade or so it has become clear that molecular chaperones are secreted proteins with a range of intercellular signalling functions. This is exciting interest from the whole biomedical community including physiologists, psychologists and systems biologists.
This short introduction, with its mention of most of the biological and biomedical specialities, shows that cell stress proteins are a very important topic in modern biology. Unfortunately, the literature on these proteins is: (i) voluminous; (ii) scattered throughout the biological and biomedical literature and (iii) because of terminology and the diversity of techniques used - very complex. The aim of the proposed volume is to cover the entire field of cell stress proteins - from their molecular structure to their epidemiology in human diseases - in a relatively short and easy-to-read textbook. This will be written for 3rd year undergraduates and for postgraduate scientists. It is proposed that if marketed at a reasonable price the proposed text will sell well simply because every biological scientist has to have some knowledge of these proteins and there is no textbook available.
The authors of this book cover the three main areas of molecular chaperone biology: (i) biochemistry and cell biology of molecular chaperones; (ii) immunology and immunomodulation and (iii) extracellular signalling and systems biology.
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Brian Henderson is Professor of Cell Biology in the Division of Microbial Diseases, Eastman Dental Institute and in the Division of Infection and Immunity, University College London. He has been working on the cell-cell signalling actions of molecular chaperones since 1994 when his group identified a potent bone-destroying protein produced by an oral bacterium as the cell stress protein, chaperonin (hsp)60. His studies have focused on the intercellular signalling actions of hsp60 and hsp10 proteins from various sources and on the anti-inflammatory activity of thioredoxin. In collaboration with Graham Pockley he has edited a postgraduate volume on the signalling activity of molecular chaperones entitled Molecular Chaperones and Cell Signalling, Cambridge University Press 2005.
Michael Cheetham is Professor of Molecular Cell Biology at the Institute of Ophthalmology, University College London and has worked on chaperones since he identified the first human Hsp70 cochaperone (HSJ1) in 1991. He has since worked on several cochaperones and has focused on the role of chaperones in the retina and nervous system and in degenerative disease.
A. Graham Pockley is Professor of Immunobiology in the University of Sheffield Medical School. His interests lie in the significance of extracellular molecular chaperones to inflammatory disease processes and his group has been working in this area since first discovering the presence of Hsp60 and Hsp70 in the peripheral circulation of healthy individuals in the late 1990s. Graham has published a number of reviews on circulating cell stress proteins in Lancet and Circulation and has edited a book on molecular chaperones as cell signalling molecules with Brian Henderson.
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