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.
|Edition description:||Softcover reprint of the original 1st ed. 1986|
|Product dimensions:||6.10(w) x 9.25(h) x 0.03(d)|
Table of ContentsSection I.- I.1 General introduction and a brief history of amyloidosis.- Section II Chemical and Ultrastructural Aspects.- II.1 Amyloid proteins.- II.2 Carbohydrate-containing AL proteins.- II.3 Endocrine amyloid fibril proteins.- II.4 Amyloid P-component: structure and properties.- II.5 A brief review of the ultrastructure of amyloid.- Section III Clinical Aspects.- III.1 Clinical evaluation of AA and AL amyloid disease.- III.2 Cardiac involvement in amyloidosis.- III.3 Hemodialysis-associated amyloid of ?2-microglobulin nature.- III.4 Amyloid P-component: clinical implications.- Section IV Pathogenesis.- IV.1 Amyloid protein AA and its precursor, the acute phase proteins(s) ApoSAA: a perspective.- IV.2 Sites and regulation of biosynthesis of SAA.- IV.3 Serum amyloid A protein in plasma: characteristics of acute phase HDL.- IV.4 Correlation between sequence variability and structure prediction in AA proteins.- IV.5 Gene structure of a human serum amyloid A protein and comparison with amyloid A.- IV.6 Structure and expression of murine serum amyloid A protein genes: implications for amyloidogenesis.- IV.7 Amyloidogenic proteins in human central nervous system diseases.- IV.8 Structure of the Alzheimer paired helical filament.- IV.9 The significance of non-protein AA material in water-soluble bovine AA-amyloid fibrils.- IV.10 Fibril derived Amyloid Enhancing Factor (FAEF) in hamster: evidence for a close relationship between AEF and AA-amyloid fibrils.- Section V Familial Amyloidosis.- V.1 The hereditary amyloidoses.- V.2 Familial amyloidotic polyneuropathies.- V.3 Biochemical and genetic characterization of a variant transthyretin causing familial amyloidotic polyneuropathy.- Section VI Senile Amyloidosis.- VI.1 The nature and pathogenesis of the amyloid deposits in Alzheimer’s disease.- VI.2 Biochemistry of cerebral amyloid in Alzheimer’s disease, the unconventional slow virus diseases and Icelandic cerebrovascular amyloidosis.- VI.3 Amyloid of the islets of Langerhans and its connection with diabetes mellitus.- VI.4 Senile amyloid affecting the heart.- VI.5 Amyloid arthropathy.- VI.6 Peripheral angiopathy.- VI.7 Animal models.- Section VII Experimental Amyloidosis.- VII.1 Pathology of experimental amyloidosis.- VII.2 What factors are necessary for the induction of AA amyloidosis? (AA amyloid, glycosaminoglycans, amyloid enhancing factor, apo-SAA).- VII.3 Amyloidogenic proteins in mice.- VII.4 Sites of SAA/AA synthesis.- VII.5 The role of the macrophage phagocytic system (MPS) in the development of secondary amyloidosis.- VII.6 SAA kinetics in animals.- VII.7 Amyloid and female protein: sex-related occurrence in the Syrian hamster.- VII.8 Endocrine amyloid in animals.- VII.9 Dietary treatment during the induction and resorption phases of experimental amyloidosis.- Section VIII.- Section VIII.1 Future directions in amyloid research.- Contributors.