Biology of Cell Stress Proteins

Chapter 1 A brief history of the cell stress response and molecular chaperones.
A brief overview of the history of the science of physiological and psychological stress and the discovery of the heat shock response and molecular chaperones. This chapter will provide an introduction and links to the other sections of the book..
Chapter 2 The cell stress response.
A current synthesis of the response of cells to stress with emphasis on the regulation of the cell stress response at the cellular level and it role in homeostatic regulation..
Chapter 3 An introduction to molecular chaperones.
This first chapter devoted to the classic chaperone proteins will provide information on the function of these proteins, their numbers, cellular location, oligomeric states, enzymic activity and structure and mechanism of action of exemplars..
Chapter 4 Protein folding, quality control and degradation.
A similar coverage will be provided for the various enzymes such a protein-disulphide isomerase and thioredoxin which aid in protein folding by catalysing specific biochemical modifications in proteins..
Chapter 5 Complex arrangements: The unfolded protein response.
Protein folding is intimately linked to the control of cellular homeostasis and the unfolded protein response (UPR) in the endoplasmic reticulum exerts significant control over cell behaviour. The control of the UPR and the signalling actions of molecular chaperones will be described..
Chapter 6 Unexpected immunogenicity of molecular chaperones.
The existence of proteins in bacteria and parasites with potent immunogenicity in infected individuals was recognised before the discovery of molecular chaperones. The paradoxical nature of the immunogenicity of these highly homologous proteins will be reviewed..
Chapter 7 Molecular chaperones are potent immunomodulators.
Molecular chaperones such as Hsp60 have been experimentally demonstrated to be powerful imunomodulators able to control a range of experimental

The AuthorsBrian 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.