Welcome.- Elliott F. Osserman In Memoriam.- The 1990 Guidelines for Nomenclature and Classification of Amyloid and Amyloidosis.- I Protein Aa/Saa and Secondary Amyloidosis.- The Human Saa Genes and Their Regulation by Cytokines.- Genetic Isofocusing Variant of Human Serum Amyloid A.- Sequence Analysis of a Third Human Saa Gene.- Human Serum Amyloid-A Protein: Variability Demonstrated by Cdna Sequencing and Expression Studies.- Abyssinian Cat Model of Aa Amyloidosis: Saa Gene Analysis.- Mink Serum Amyloid a Protein - Expression and Primary Structure of Amyloidogenic and Non-Amyloidogenic Isotypes.- Primary Structure of Two Rabbit Serum Amyloid a Proteins (Saa) Based on Cdna Sequence.- Biosynthesis and Processing of Saa by Mouse L-Cells Transfected with the Human Saag9 Gene.- Regulation of Serum Amyloid a (Saa) Synthesis in Hep 3B Cells by Cytokines and Corticosteroids.- Regulation of Saa Synthesis by Cytokines in a Human Hepatoma Cell Line.- Saa Secretion from Cytokine-Stimulated Human Hepatoma Cells Requires Hdl.- Interferon a Induces Tnf Elevations in Vivo. Correlation with Other Acute Phase React Ants.- Acute Phase Protein, Serum Amyloid a, Inhibits Il-1- and Tnf-Induced Fever and Hypothalamic Pge2 In Mice.- Human Recombinant TNF-? and Poly I. Poly C Induce Saa and Enhance Amyloidosis in Hamster.- The Physiology of the Acute Phase Serum Amyloid a (Saa) Response in Mice.- Mouse Saa3: Detection in Mouse Tissues with Specific Antibody.- Generation and Use of Site-Specific Antibodies Against Saa.- The N-Terminus is the Lipid-Binding Site of Saa: Supporting Evidence by Moabs.- Epitope Mapping of Amyloid-a Protein Using Monoclonal Antibodies.- Reactive (Aa) Amyloidosis in a 14 Year Old with No Predisposing Disease.- Induction of Amyloidosis in Mice: Preparation of Active Azocasein (Azo) and Effect of Endotoxin (Lps).- Serum Amyloid a (SAA) Induction in the Serum High Density Lipoproteins of the Syrian Hamster.- The Complete Primary Structure of Bovine Serum Amyloid Protein a (SAA) and of Tissue Amyloid Fibril Protein a (AA) Subspecies.- Degradation of Saa in Amyloid Fibrils by Elastase.- Evolutionary Aspects of Protein Saa.- Strain Specific Variation in Expression of Novel Mouse Apo-Saa Isoforms.- Saa Isotypes in Patients with Secondary Amyloidosis.- Differential Regulation of Human Serum Amyloid a Isoforms.- The Effect of SAA-Derived Fragment - SAA2-82 - On Platelet Aggregation.- Serum Amyloid a, An Acute Phase Protein, Inhibits Platelet Activation.- Serum Amyloid a (SAA)-Related Peptide Isolated from Synovial Fluid Modulates Superoxide Production by Human Neutrophils.- Antiplatelet Aggregation Activity of Serum Amyloid a (SAA) Related Peptides.- Effect of Purified Serum Amyloid a on Growth and Differentiation of Transformed Cells.- II Al Protein and Light Chain Related Amyloidosis.- Primary Systemic Amyloidosis (AL) In 1990.- Comparison of the Amino Acid Sequences of Ten Kappa I Amyloid Proteins for Amyloidogenic Sequences.- Characterization of a X Al Protein and Two Amyloidgenic X Bjp in Three Cases of Immunoglobulin Amyloidosis.- Biclonality in Amyloidosis Patient Mal: One Clone Producing an Amyloidogenic, the Other a Non-Amyloidogenic Kappa L-Chain.- Complete Amino-Acid Sequence of a Kappa Light Chain Fragment Isolated from the Urine of Amyloidosis Patient Mal.- Comparative Studies of Two al Chains of Kappa-III Light Chain Origin with and Without Attached Carbohydrate (Al So124 and Al 700).- Structural Studies of two Carbohydrate-Containing Al Chains (?II) Al NoV and Al Mc.- Complete Amino-Acid Sequence of Al-Bence-Jones Protein Pol of the Lambda I Subclass.- Complete Amino-Acid Sequence of Al-Lambda 1.1 Bence-Jones Protein Ezi.- Complete Amino Acid Sequence of A A Amyloid Fibril Protein Isolated from the Liver of Amyloidosis Patient Dia.- Systemic Al Amyloidosis In A Cat.- Experimental Production of Human Amyloidosis Al.- Al Amyloid, L-Chain and L&H-Chain Deposition Diseases: Comparison of Ig Synthesis and Tissue Deposition

Both scientifically and socially the Vlth International Symposium on Amyloidosis, August 5 - 8, 1990 in Oslo was a great success. There were three and a half intensive days. It started with the Opening Ceremony, particularly highlighted with the Norway-Norway multi media show by David Cochron, and ended with a visit to the Edvard Munch museuro and the Farewell Salmon Dinner on the evening of August 8 (not to forget the "happy birthday" song for Dorothea Zucker-Franklin at the breakfast table the following morning). In between was the intellectual penetration into the science of amyloidosis and amyloid proteins, and a deepening of many friendships among young and old "amyloidologists", together with some of the cultural and historical features of Oslo and Norway. Among the numerous Ietters of thanks and gratitude that we have received, the senior organizer of the previous meeting, Takashi lsobe said it briefly and eloquently: "You have overwhelmed us, you have performed a drama with joy and cheer, you have hosted so nicely with lovely secretariat, you have arranged impressive hospitality in every respect, you certainly did for all of us" Now we are left with the proceedings book for the three coming years until the next symposium in Kingston, Canada, which will be organized by Drs. Robert Kisilevsky and Thomas Muckle from the Department of Pathology at Queens University in 1993. The scientific contributions herein cover all the sessions of the meeting.