Chaperokine Activity of Heat Shock Proteins

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 principlesof 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.