Molecular Chaperones and Cell Signalling [Paperback]

This text reviews understanding of the biological roles of extracellular molecular chaperones.Every living cell contains special proteins called molecular chaperones that help proteins fold and allow cells to survive stress. It has been shown that these same proteins also act as biological messengers with many and varied functions. This 2005 volume was the first to describe this new signalling activity.Every living cell contains special proteins called molecular chaperones that help proteins fold and allow cells to survive stress. It has been shown that these same proteins also act as biological messengers with many and varied functions. This 2005 volume was the first to describe this new signalling activity.This book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?Preface; Part I. Molecular Chaperones and the Cell Stress Response: 1. Chaperone function: the orthodox view R. J. Ellis; 2. Intracellular disposition of mitochondrial molecular chaperones: Hsp60, mHsp70, Cpn10 and TRAP-1 R. S. Gupta, T. Bowes, S. Sadacharan and B. Singh; Part II. Chlƒ-