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Heat shock proteins (HSP) have received ample interest by immunologists over recent years. Initially they were found to be dominantly immunogenic microbial antigens. The connection with inflammation was established when it was uncovered that T cells specific for these antigens have a crucial role in the induction and regulation of experimental arthritis. Since then, the raised presence of immunity to HSPs in virtually all conditions of inflammation, including autoimmune diseases, transplant rejection and atherosclerosis, has emphasised the critical significance of immunity to HSPs in inflammatory diseases.
The Janeway's Immunobiology CD-ROM, Immunobiology Interactive, is included with each book, and can be purchased separately. It contains animations and videos with voiceover narration, as well as the figures from the text for presentation purposes.
Measles virus possesses a non segmented, single stranded, negative sense RNA genome that is encapsidated by the nucleoprotein to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein. This book focuses on the main structural information available on the nucleoprotein, showing that it consists of a structured core (NCORE) and of an intrinsically disordered C-terminal domain (NTAIL). The functional implications of the disordered nature of NTAIL are discussed in light of the ability of disordered regions to establish interactions with multiple partners, thus leading to multiple biological effects. Indeed, beyond the phosphoprotein, NTAIL also interacts with cellular partners, including the major heat shock protein, hsp72, the interferon regulator factor 3, IRF3, and a yet unidentified cellular receptor referred to as NR. This book consists of two chapters devoted to the general functions of the nucleoprotein in transcription and replication and to a detailed overview of its structural properties, and of three chapters focused on the functional relevance of the interaction between NTAIL and its various intracellular and extracellular partners.
This book surveys the current knowledge concerning the expression and function of stress proteins in different organisms, ranging from prokaryotes to humans. It provides an overview of the diversity and complex evolutionary history of cell stress proteins and describes their function and expression in different eukaryote models. The book will appeal to researchers and scientists in biochemistry, cell biology, microbiology, immunology, and genetics.
This book provides the most up-to-date review on new mechanisms and provides exciting insights into how heat shock proteins modulate the hosts’ immune response. Written by leaders in the field of heat shock protein immunobiology, the chapters systematically and in a step-wise fashion take the reader through the fascinating sequence of events by which heat shock proteins activate immune responses and provide answers as to its biological significance to the host.
Heat shock proteins (HSPs) were discovered as polypeptides induced by stress that can be found in all kingdoms of cellular organisms. Their functions were, a first enigmatic and these proteins were thus classified by molecular weight, as in—Hsp27, Hsp70, Hsp90, Hsp110. More recently, each of these size-classified molecules has attributed a role in protein folding, and they thus came to be known, as a class, as molecular chaperones. However, the they possess properties beyond chaperoning. Indeed, their discovery in the extracellular spaces suggested roles in regulation of the immune responses.
This volume includes contributions from the speakers of the Second IMD Congress (September 10-15, 2007; Moscow, Russia) who were eager to share some of the academic and clinical enthusiasm that defines the IMD meetings. The goal of the International Immune-Mediated Diseases: From Theory to Therapy (IMD) Congress is to bring the world’s best immunologists and clinicians to Moscow.
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.
Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease provides the most current review of the literature relating to the role and influence of heat shock (stress) proteins on the establishment, progression and resolution of infectious disease. Written by leaders in the field of heat shock proteins (HSP) and their biological and immunological properties, the contributors provide a fascinating insight into the complex relationship between, and the involvement of prokaryotic and eukaryotic HSP in disease states. It has been known for some considerable time that heat shock proteins from prokaryotic organisms are immunodominant molecules that are intimately involved in the induction of potential protective inflammatory responses, and this aspect of HSP biology is updated herein. In addition to regulating heat shock protein gene expression, the transcription factor HSF1 also appears to play an important role in regulating immune responses to infection. Heat shock proteins are now known to influence infectious disease processes in a number of diverse ways: they are involved in the propagation of prions, the replication and morphogenesis of viruses, and the resistance of parasites to chemotherapy. These proteins also appear to be important mediators of bacteria-host interactions and inflammation, the latter via interactions with cell surface molecules and structures such as Toll-like receptors and lipid rafts. Heat shock proteins can be expressed on the surface of infected cells, and this is likely to provide a target for the innate immune response. Elevated levels of circulating HSP are present in infectious diseases and these proteins might therefore regulate inflammatory responses to pathogenic challenge on a systemic basis. Heat shock proteins are also implicated in the impact of genital tract infections on the reproductive outcome, as well as in the local and systemic consequences of periodontal disease. Fever-range temperatures can induce the expression of heat shock proteins, and the final chapter in the book examines the influence of fever-range hyperthermia on a variety of cells and the organization of plasma membranes. This book is an essential read for graduates and postgraduates in Biology, pro- and eukaryotic Biochemistry, Immunology, Microbiology, Inflammatory and Infectious Disease, and Pathology.