From a process that from the days of Vir chow and Rokitansky, primarily stimulated the relatively narrow interest of pathologists, amyloidosis has risen full-blown as one of the most important of disease complexes. Its presence dominat:es the lesions of Alzheimer's disease, a disease affecting an estimated 2. 5 million people in the U. S. A. and thereby closely rivaling stroke as the third most common cause of death. If, as it has been de scribed, Alzheimer's disease is the "Disease of the Century," then amy loidosis is the Disease Complex of the Ages. It affects in one or more of its manifestations every organ of the body, and is at least as old as the afflicted Egyptian mummies of the pyramids. With an increasing percentage of older individuals amyloid of the senior population becomes increasingly more frequent. The subjects covered in this Symposium range through almost every clinical medical specialty. From an average of one paper in each of the past three Symposiums, the explosive interest in cerebral amyloidosis has led to the presentation of 12 papers on this subject in the present volume. The genetically predisposed familial amyloidotic processes, such as the polyneuropathies and familial Mediterranean fever have also stimulated ex tensive and intriguing investigations which have revealed the striking effect of a single amino acid substitution in transforming a normal protein into. a lethal "amyloidogenic" one.
'A. SAA, AA and AP Proteins.- Protein AA and Associated Proteins in Type-AA Amyloid Substance.- Heterogeneity of Human Amyloid Protein AA and SAA.- Vascular AA Amyloidosis is Characterized by Special Protein AA Subspecies.- The Physico-Chemical, Antigenic and Functional Heterogeneity of Human Serum Amyloid A.- Reaggregation of Bovine Amyloid A Fibril Components to ?-Pleated Sheet Fibrillar Structures.- Analysis of X-Ray Scattering by Human AA Fibrils using Secondary Structure Predictions of Human SAA1.- Characterization of Two Distinct Serum Amyloid A Gene Products Defined by Their Complementary DNAs.- Human Serum Amyloid Genes - Molecular Characterization.- Kinetics of Human Serum Amyloid A.- Ultrastructural Identification of AA-Type Amyloid Fibrils Using Polyclonal and Monoclonal Antibodies.- Human Serum Amyloid P-Component (SAP) as an Acute Phase Reactant in the Female.- B. Experimental Models.- Pathogenetic Mechanisms and Precursor Product Relationships in Murine Amyloidosis.- A Possible Effect of Oral Tolerance in Casein Induced Murine Amyloidosis?.- Isolation and Characterization of Amyloid Enhancing Factor (AEF).- Enhancement of Amyloid Degradation by Ascorbic Acid: In Vivo Evidence in a Murine Model.- Effect of Colchicine on the Acute Phase Serum Amyloid A Protein Response and Splenic Amyloid Deposition During Experimental Murine Inflammation.- Serum Amyloid A Protein (SAA) from Mink, Horse, and Man: A Comparative Study.- The Time Relationship Between Amyloid Deposition and Glycosaminoglycan Accumulation During Experimental Amyloidosis.- Kinetics of Selective Deposition of ApoSAA2 During Development of Amyloidosis in Mice.- InVivo Radioimmunodetection of Amyloid Deposits in Experimental Amyloidosis.- Prostacyclin and Thromboxane Production from Macrophages of Amyloid Resistant and Sensitive Mice.- C. In Vitro Synthesis.- Regulation of Serum Amyloid A Synthesis in Primary Mouse Hepatocyte Cultures.- Immunoelectron Microscopic Study of Liver in Experimental Murine Amyloidosis Using Anti-Mouse AA Antiserum.- Immunocytochemical Studies on the Site of Synthesis and Pathways of Amyloid Protein AA.- A Comparison of Serum Amyloid A (SAA) Synthesis With That of the Pentraxins: Serum Amyloid P (SAP) and C-Reactive Protein (CRP).- Further Studies on the Mechanism of Action of Surface Associated Proteolytic Enzymes on Lymphocytes and Monocytes Which Degrade SAA Precursor to AA-Like Products.- Down-Regulation of Kupffer Cell Ectoenzymes Precedes Deposition of Amyloid Protein A.- Specific Chemical Dissociation of Fibrillar and Non-Fibrillar Components of Amyloid Deposits.- D. Degrading Factors.- Degradation of AA-Amyloid, Clinical Experience: An Introduction.- In Vivo Degradation of Protein SAA to Protein AA and Incorporation in Amyloid Fibrils.- Isolation and Characterization of the Inhibitor of Amyloid Degrading Factor.- Amyloid-Agarose Plate Test: Ultrastructural Changes in the Fibril and Its Association with Human Neutrophil Elastase.- Decreased Esterase Activity in Serum of Patients with Reactive Systemic (AA) Amyloidosis.- Enhanced Degradation of Amyloid AA Proteins by Enzyme Activation: A Possible Model for a Therapeutic Approach.- Does Serum Degrade Amyloid Fibrils? Failure to Confirm Enzymatic Degradation of Amyloid A Fibrils as the Basis of the So-Called "Amyloid Degrading Activity" of Serum.- E. Hereditary and Familial (AF) Amyloidosis.- Statement Regarding Nomenclature for the Protein Known as Prealbumin, Which is Also (Recently) Called Transthyretin.- Family Studies of Transthyretin (Prealbumin) and Its Methionine 30 Variant in Portuguese Patients with Familial Amyloidotic Polyneuropathy.- Serum Concentrations of Prealbumin and Retinol Binding Protein in Familial Amyloid Patients From 15 Kinships.- Pre-Albumin and Retinol Binding Protein Serum Concentrations in the Brazilian Type (Portuguese) of Familial Polyneuropathy.- C
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