Biology of Cell Stress Proteins

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. INDICE: 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 autoimmune diseases. This literature will be reviewed and the immune mechanisms explained.. .Chapter 8 Molecular chaperones and therapy of human disease. .It has emerged that molecular chaperones can be of therapeutic use or are targets for therapeutic agents. The potential therapeutic benefits of selectively modulating the cell stress response will be described.. .Chapter 9 Moonlighting and molecular chaperones. .The concept of protein moonlighting (one protein having more than one function) will be explained and applied to molecular chaperones which are emerging as very successful moonlighting proteins with the ability to exit from cells and act as intercellular signalling molecules or cell surface receptors.. .Chapter 10 Secreted molecular chaperones and human disease. .Evidence is rapidly emerging that secreted molecule chaperones act in the control of human pathology. The growing number of examples of such proteins will be reviewed.. .Chapter 11 Molecular chaperones: Friends or foes. .A summary, bringing out the salient arguments and gazing into the crystal ball for future developments in the field.. .Glossary. .Index

• ISBN: 978-1-4051-5848-0
• Editorial: Wiley–Blackwell
• Encuadernacion: Rústica
• Páginas: 300
• Fecha Publicación: 09/11/2015
• Nº Volúmenes: 1
• Idioma: Inglés