Chaperokine Activity Of Heat Shock Proteins

This book makes a novel synthesis of the molecular aspects of the stress response and long term adaptation processes with the system biology approach of biological networks. Authored by an exciting mixture of top experts and young rising stars, it provides a comprehensive summary of the field and identifies future trends.

Based upon a workshop entitled “The Small HSP World” held in Québec 2-5 October 2014. Twenty-five scientists provided chapters for the book. The chapters are from the best scientists currently working in this field. These colleagues include Arrigo, Benesch, Benjamin, Buchner-Haslbeck-Weinkauf, Benndorf, Boelens, Carra, Chang, Currie, Ecroyd, Emanuelsson, Fu, Garrido, Golenhofen, Gusev, Hightower, Kampinga, Lavoie, MacRae, Quinlan, Tanguay, Vierling, Vigh, Weeks and Wu. Briefly, the book starts with the structure of small heat shock proteins, moving to their functions and finishing with their involvement in diseases. Although this is quite broad, the structural aspect will be the unifying theme of the book.

Heat shock proteins are emerging as important molecules in the development of cancer and as key targets in cancer therapy. These proteins enhance the growth of cancer cells and protect tumors from treatments such as drugs or surgery. However, new drugs have recently been developed particularly those targeting heat shock protein 90. As heat shock protein 90 functions to stabilize many of the oncogenes and growth promoting proteins in cancer cells, such drugs have broad specificity in many types of cancer cell and offer the possibility of evading the development of resistance through point mutation or use of compensatory pathways. Heat shock proteins have a further property that makes them tempting targets in cancer immunotherapy. These proteins have the ability to induce an inflammatory response when released in tumors and to carry tumor antigens to antigen presenting cells. They have thus become important components of anticancer vaccines. Overall, heat shock proteins are important new targets in molecular cancer therapy and can be approached in a number of contrasting approaches to therapy.

The second edition of this encyclopedia presents over 400 biologically important signaling molecules and the content is built on the core concepts of their functions along with early findings written by some of the world’s foremost experts. The molecules are described by recognized leaders in each molecule. The interactions of these single molecules in signal transduction networks will also be explored. This encyclopedia marks a new era in overview of current cellular signaling molecules for the specialist and the interested non-specialist alike. Currently, there are more than 30,000 genes in human genome. However, not all the proteins encoded by these genes work equally in order to maintain homeostasis. Understanding the important signaling molecules as completely as possible will significantly improve our research-based teaching and scientific capabilities.

The book Heat Shock Proteins and Stress provides the most comprehensive review on contemporary knowledge on the role of HSP in Stress. Using an integrative approach to understanding the regulation of HSP responses, the contributors provide a synopsis of novel mechanisms by which HSP responses are regulated under normal physiological and pathophysiological conditions. Key basic and clinical research laboratories from major universities and academic medical hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Translational Medicine, Clinical Psychologists, Human Physiology, Zoologists, Botanists, Biotechnology, Molecular Medicine, Infectious Diseases Experts and Pathologists.

Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.

Chaperokine, is a term that describes the unique function of extracellular heat shock protein (eHsp) as both chaperone and cytokine. The cellular consequence of binding and signaling of eHsp is the stimulation of a potent and long lasting immune response. eHsp induces a plethora of immune responses including the release of bioactive mediators like cytokines, chemokines, nitric oxide, apotogenic mediator, stimulation of the innate and adaptive immune response, migration and maturation of dendritic cells (DC) and the enhancement of natural killer cell-mediated cellular cytotoxicity. The book Chaperokine Activity of Heat Shock Proteins provides the most comprehensive review on contemporary knowledge on the chaperokine activity of heat shock proteins (HSP) in biology and medicine. Using an integrative approach to understanding the chaperokine activity of HSP, the contributors provide a synopsis of novel mechanisms, signal transduction pathways and how the principles of the chaperokine activity of HSP has been harnessed for therapeutic gain. To enhance the ease of reading and comprehension this book has been subdivided into various section, including; Section I, reviews current progress on our understanding of Immunological and Inflammatory Responses; Section II, evaluates the role of Physiological Responses and Section III, focuses the reader on the Therapeutic Approach. Key basic and clinical research laboratories from major universities, academic medical hospitals, biotechnology and pharmaceutical laboratories around the world have contributed chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Translational Medicine, Clinical Psychologists, Human Physiology, Zoologists, Botanists, Biotechnology, Molecular Medicine, Infectious Diseases Experts, Pathologists, Pharmaceutical Scientists and Researchers involved in Drug Discovery.

Heat-Shock Proteins: Advances in Research and Application: 2011 Edition is a ScholarlyPaper™ that delivers timely, authoritative, and intensively focused information about Heat-Shock Proteins in a compact format. The editors have built Heat-Shock Proteins: Advances in Research and Application: 2011 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Heat-Shock Proteins in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Heat-Shock Proteins: Advances in Research and Application: 2011 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.

An increase in ambient temperature pose a threat to any living cell, as heat shock destabilizes the native protein conformation that renders many proteins prone to aggregation. To counteract deleterious aggregation, cells express a certain set of genes that prevent aggregation in the cell, a phenomenon known as the heat shock response. The small heat shock proteins (sHsps) are molecular chaperones and constitute one component of the heat shock response. According to their cellular function as molecular chaperones, sHsps bind to partially unfolded polypeptides to form stable substrate complexes and maintain them in a refolding competent state under conditions detrimental for protein refolding. Here, the temperature-induced conformational changes mediating the temperature activation of Hsp26 were analyzed by fluorescence spectroscopy and FRET. In addition, its kinetic parameters and the energy barrier governing the structural rerangement were determined. It appears that the Hsp26 middle domain is a thermosensor and the intrinsic regulator of chaperone activity.