Amyloids and Other Abnormal Assembly Processes FASEB Summer Conference Copper Mountain, Colorado June 11-16, 2000

Abstract

The amyloid field has, over the past few years, experienced a rapid growth in a number of areas. The intent of this meeting was to examine the complete amyloid pathway from crystal structures to animal models and the creation of novel methods of treating these disorders. This involved bringing together different disciplines, ideas and approaches which examined amyloidogenic proteins from unique perspectives. The first keynote address was given by D. Cleveland (UC San Diego) who reviewed the aggregation pathway of superoxide dismutase (SOD) as it relates to amyotrophic lateral sclerosis (ALS) or Lou Gehrig's disease. This address provided insights into all aspects of the abnormal accumulation of SOD from the effects of mutations on protein folding to the recapitulation of these deposits in transgenic mice. The second keynote was delivered by J. Kelly (Scripps) who dealt with the complexities of amyloid assembly as seen from a protein folding viewpoint and addressed the question of whether or not it is possible to design specific inhibitory compounds. Using the transthyretin (TTR) model, it was demonstrated that aggregation could be monitored by techniques such as utracentrifugation and that molecules which maintained a stable native conformation were capable of reducing fibril formation. The combination of these two addresses encapsulated the overall goal of this meeting.