A proven collection of readily reproducible techniques for studying amyloid proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.

Amyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. This volume is a comprehensive account of recent developments in the understanding of the process of amyloid fibrils. Contains up-to-date data on all of the clinical problems which, despite their pathological significance, are still largely unsolved.

This book summarizes the last ten years' research on Alzheimer's disease. Genetic mutations in the gene which codes for amyloid precursor protein (APP) have now been shown to cause Alzheimer's disease in some families. Other genetic loci are now being discovered which relate to Alzheimer's disease in some families. Understanding the normal structure and function of the APP gene product will eventually provide avenues for developing specific therapeutic strategies targeted at the amyloid deposition in the Alzheimer's disease brain. Drugs which can inhibit or dissolve the amyloid, affect the synthesis and proteolysis of APP, or which regulate the activity of the APP gene all hold the promise of eventually yielding an effective treatment for Alzheimer's disease.

This book is a gift from the international community of amyloid friends, presented to Professor Dr. Enno Mandema on the occasion of his retirement from the University of Groningen, the Netherlands. It is the "precipitation" of up to date knowledge of amyloidosis, as presented at the International Course on Amyloidosis in Groningen, on the 10th and 11th of October 1986. Twenty years ago, Professor Mandema invited a group of scientists, who were studying the various aspects of amyloidosis from different points of view, to discuss their mutual interest in the subject. This "First International Symposium" was held for five days in September 1967. It was a wonderful experience for the participants, as most of them had until then only read each others work in the literature. The proceedings of that symposium, which contained the "lively" dis cussions, became a text-book for the following years. Research continued, and while the book was still in preparation, the revolutionary method of "water-soluble amyloid" was published. In the following years, different amyloid proteins were discovered and the mo lecular basis of the different amyloid syndromes was elucidated. The increase in knowledge parallelled the availability of modern, ingenious and also rapid methods in the biomedical sciences.

This authoritative volume contains 179 chapters by international experts on recent developments in our understanding of amyloid proteins, protein folding disorders, and new and proposed clinical trials in amyloidosis. Topics include detection and characterization techniques; biological functions; genetics; disorders, diagnosis, and treatments, incl

In the search for an effective treatment for Alzheimer's disease, APP is a unique model protein that illustrates the wide array of basic and sophisticated characterization techniques available. Exploring a variety of biological techniques to clarify the structure and function of this transmembrane protein, this text presents each method with detail

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.