Description

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 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 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. Changing Paradigms of Protein Trafficking and Protein Function: 3. Novel pathways of protein secretion G. Chimini and A. Rubartelli; 4. Moonlighting proteins: proteins with more than one function C. J. Jeffery; 5. Molecular chaperones: the unorthodox view B. Henderson and A. Shamaei-Tousi; Part III. Molecular Chaperones as Cell Regulators: 6. Cell-cell signalling properties of chaperonins A. R. M. Coates; 7. Toll-like receptor-dependent activation of antigen presenting cells by Hsp60, Hsp70 and Gp96 R. M. Vabulas and H. Wagner; 8. Regulation of signal transduction by intracellular and extracellular Hsp70 A. Asea and S. Calderwood; 9. Hsp72 and cell signalling M. Y. Sherman; 10. Heat shock proteins, their cell surface receptors and effect on the immune system T. Lehner, Y. Wang, T. Whittall and L. A. Bergmei; 11. Molecular chaperone-Cytokine interactions at the transcriptional level A. Stephanou and D. S. Latchman; Part IV. Physiological and Pathophysiological Signals: 12. Heat shock protein release and naturally-occurring exogenous heat shock proteins J. Frostegård and A. G. Pockley; 13. Hsp27 as an anti-inflammatory Protein K. Laudanski, A. De and C. Miller-Graziano; 14. Bip, a negative immune regulator involved in rheumatoid arthritis V. M. Corrigal and G. S. Panayi; Part V. Molecular Chaperones as Therapeutics: 15. Neuroendocrine aspects of the molecular chaperones ADNF and ADNP I. Gozes, I. Vulih, I. Spivak-Pohis and S. Furman; 16. Heat shock proteins regulate by both molecular a