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This book is a printed edition of the Special Issue "PrPSc prions: state of the art" that was published in Pathogens
C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands derived from self, non-self and altered self via its heterotrimeric globular (gC1q) domain and thus trigger the classical complement pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. C1q circulates in serum as part of the C1 complex, in association with a catalytic tetrameric assembly of two homologous yet distinct serine proteases, C1r and C1s. Binding of C1q to appropriate targets leads to sequential activation of C1r and C1s, the latter being able to cleave complement components C4 and C2 thereby triggering the complement cascade. Activation of the classical pathway plays an important role in innate immune protection against pathogens and damaged elements from self. However, its involvement has been shown in various pathologies including ischemia-reperfusion injury and hereditary angioedema. Unexpected roles for the classical pathway have also been discovered recently, linked to both physiological and pathological aspects of development, including brain and cancer cells. These new perspectives should arouse renewed interest in a search for specific inhibitors of the classical pathway. In addition, C1q has recently been shown to have a number of functions that are independent of the activation of the classical pathway. This research topic is aimed at providing a state-of-the-art overview of the classical pathway, including, but not restricted to emerging functions of C1q and of the C1 complex, as well as pathological consequences of C1 activation or of the presence of anti-C1q autoantibodies . Contributions are included in the areas such as structural basis of C1q ligand recognition, C1q family proteins, inhibitors of the classical pathway identified in pathogens and improved derived inhibitors, structural determinants of the substrate specificities of C1r and C1s, elucidation of the architecture of C1, structural and functional homology of C1 with the initiating complexes of the lectin complement pathway, and novel involvement of C1q in processes such as ageing, cancer, synaptic pruning, and pregnancy.
Prion-related diseases, known as transmissible spongiform encephalopathies (TSEs), are infectious, fatal neurodegenerative disorders for which there is no cure, treatment, nor even a means for early diagnosis. The horrific advent of Mad Cow Disease -- transmitted to humans through eating meat from steers sickened by bovine spongiform encephalopathy
The 'food scare' concept took on new meaning in 1996, which opened with variant CJD emerging as the human form of BSE, and closed with Britain's worst E.coli O157 outbreak in central Scotland. As people died, so did trust in government and science. This book tells the story of these events, what led up to them, and what has happened since. It breaks new ground by dissecting these tragedies alongside catastrophes like Aberfan, Piper Alpha, Chernobyl, and the worst ever railway accidents in Ireland and Britain (Armagh and Quintinshill), as well as classical outbreaks of botulism, typhoid, E.coli O157 and Salmonella food poisoning. Britain's ability to win Nobel prizes marches with a propensity to have disasters. The book explains why, demonstrating failures in policy making, failures in the application of science, and failing inspectorates. A unique feature of this book is its breadth since it covers history, politics and law as well as science. It also makes some fascinating connections, like those between 1930's nuclear physics, E.coli, and molecular biology, and the links between manslaughter in 19th century mental hospitals, syphilis, the Nobel Prize, and the prospects for successfully treating variant CJD. Royal murderers, vaccine research in Auschwitz and Buchenwald, and the race to develop the atom bomb appear as well. For the general reader its non-technical but authoritative account of the science behind these tragedies, its critical appraisal of how the government responded to them, its coverage of public inquiries and its analysis of risk will be informative and stimulating. Scientists will find its approach to the prion theory and the origins of BSE challenging and controversial. Policy makers will find not only diagnoses of what went wrong in the past, but remedies ror the future.
Prion diseases recently have attracted interest not only scientifically but also socially because of the bovine spongiform encephalopathy (BSE) epidemic and the outbreak of variant Creutzfeldt-Jakob disease (vCJD) in the United Kingdom. In 2004, the International Symposium of Prion Diseases for Food and Drug Safety was held October 31–November 2 in Sendai, Japan, where, 20 years earlier, arguments were first heard on whether the etiologic agent of transmissible spongiform encephalopathy was prions or scrapie-associated fibrils. This volume is a collection of current work on prion research that was presented at the 2004 symposium. Topics included range from basic research to clinical aspects of prion diseases, making the book a valuable resource for researchers and clinicians, and encouraging further developments by the next generation of researchers.
Sets forth the state of the science and technology in plasma protein production With contributions from an international team of eighty leading experts and pioneers in the field, Production of Plasma Proteins for Therapeutic Use presents a comprehensive overview of the current state of knowledge about the function, use, and production of blood plasma proteins. In addition to details of the operational requirements for the production of plasma derivatives, the book describes the biology, development, research, manufacture, and clinical indications of essentially all plasma proteins with established clinical use or therapeutic potential. Production of Plasma Proteins for Therapeutic Use covers the key aspects of the plasma fractionation industry in five sections: Section 1: Introduction to Plasma Fractionation initially describes the history of transfusion and then covers the emergence of plasma collection and fractionation from its earliest days to the present time, with the commercial and not-for-profit sectors developing into a multi-billion dollar industry. Section 2: Plasma Proteins for Therapeutic Use contains 24 chapters dedicated to specific plasma proteins, including coagulation factors, albumin, immunoglobulin, and a comprehensive range of other plasma-derived proteins with therapeutic indications. Each chapter discusses the physiology, biochemistry, mechanism of action, and manufacture of each plasma protein including viral safety issues and clinical uses. Section 3: Pathogen Safety of Plasma Products examines issues and procedures for enhancing viral safety and reducing the risk of transmissible spongiform encephalopathy transmission. Section 4: The Pharmaceutical Environment Applied to Plasma Fractionation details the requirements and activities associated with plasma collection, quality assurance, compliance with regulatory requirements, provision of medical affairs support, and the manufacture of plasma products. Section 5: The Market for Plasma Products and the Economics of Fractionation reviews the commercial environment and economics of the plasma fractionation industry including future trends, highlighting regions such as Asia, which have the potential to exert a major influence on the plasma fractionation industry in the twenty-first century.
A conformational transition of the cellular prion protein (PrPC) into an aberrantly folded isoform designated scrapie prion protein (PrPSc) is the hallmark of a variety of neurodegenerative disorders collectively called prion diseases. They include Creutzfeldt-Jakob disease and Gerstmann-Stäussler-Scheinker syndrome in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in free-ranging deer. In contrast to the deadly properties of misfolded PrP, PrPC seems to possess a neuroprotective activity. More-over, animal models indicated that the stress-protective activity of PrPC and the neurotoxic effects of PrPSc are somehow interconnected. In this timely book, leading scientists in the field have come together to highlight the apparently incongruous activities of different PrP conformers. The articles outline current research on celluar pathways implicated in the formation and signaling of neurotoxic and physiological PrP isoforms and delineate future research direction. Topics covered include the physiologcial activity of PrPC and its possible role as a neurotrophic factor, the finding that aberrant PrP conformers can cause neurodegeneration in the absence of infectious prion propagation, the requirement of the GPI anchor of PrPC for the neurotoxic effects of scrapie prions, the pathways implicated in the formation and neurotoxic properties of cytosolically localized PrP, the impact of metal ions on the processing of PrP, and the role of autophagy in the propagation and clearance of PrPSc. The book is fully illustrated and chapters include comprehensive reference sections. Essential reading for scientists involved in prion research.
Food proteomics is one of the most dynamic and fast-developing areas in food science. The goal of this book is to be a reference guide on the principles and the current and future potential applications of proteomics in food science and technology. More specifically, the book will discuss recent developments and the expected trends of the near future in food proteomics. The book will be divided into two parts. The first part (7 chapters) will focus on the basic principles for proteomics, e.g., sample preparation, such as extraction and separation techniques, analytical instrumentation currently in use, and available databases for peptide and protein identification. The second part of the book (26 chapters) will focus on applications in foods. It will deal with quality issues related to post-mortem processes in animal foods and quality traits for all foods in general, as well as the identification of bioactive peptides and proteins, which are very important from the nutritional point of view. Furthermore, consumers are now extremely susceptible to food safety issues, and proteomics can provide reassurance with different safety aspects, such as food authenticity, detection of animal species in the food, and identification of food allergens. All of these issues will be covered in this book. It is also worth noting that both editors are internationally recognized experts in the field of food science, and both have edited numerous food science books and handbooks.
This volume of the Subcellular Biochemistry series is the result of the long-standing research interest of the editor in the molecular mechanism underlying Alzheimer’s disease and other amyloid diseases, indicated also by the earlier book in the series (Volume 38), devoted to Alzheimer’s disease. The broad coverage within the present amyloidogenesis book represents an attempt to collate current knowledge relating to the proteins and peptides involved in most of the known amyloid diseases, together with some amyloid/fibril-forming proteins and peptides that are not involved in diseases. Thus, the range of topics included is comprehensive and furthermore it was thought appropriate to include both basic science and clinical presentation of the subjects under discussion.