Model Organism Section of HCA meeting March 2009

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Fraser Moss
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Model Organism Section of HCA meeting March 2009

January 9th 2009 Fairmont Hotel San Francisco California

http://www.the-infoshop.com/conference/high-content09/friday.shtml

HCA in Model Organisms

12:45-1:10 Automated Phenotyping of Zebrafish Embryos by High-Content Analysis
Andreas Vogt, Ph.D., Research Assistant Professor, Pharmacology, University of Pittsburgh
Currently there is no vertebrate animal model that is compatible with contemporary paradigms of drug discovery encompassing rapid screening of large compound collections. The zebrafish has the potential to become a viable model for high-throughput chemical screens, but tools required for automatic image analysis are lacking. We have developed an automated method to analyze transgene expression in specific subdomains of zebrafish larvae arrayed in multi-well plates. The application is independent of embryo orientation and imaging platform, applicable to a variety of phenotypes and deals effectively with morphological, toxicity, and imaging artifacts.

1:10-1:25 Sponsored Presentation
Fish Are Friends Not Food: High-Content Screening
of Zebra Fish

1:25-1:50 Whole Organism-Based Assays for the Identification of Chemical and Genetic Modifiers of Human Misfolded Protein Disorders Using C. elegans
Stephen C. Pak, Ph.D., Research Assistant Professor, Pediatrics, University of Pittsburgh School of Medicine
C. elegans has proven to be a useful model system for investigating numerous human diseases and physiological processes. Recently, there has been growing interest in using C. elegans as a tool for drug discovery. Their small body size and ability to grow in liquid culture makes them ideal for whole organism-based, high-content screening. We have developed a C. elegans model of misfolded protein accumulation similar to that seen in human alpha-1-antitrypsin deficiency. In addition, we have optimized an automated assay that allows rapid detection and quantification of the disease phenotypes. The described model and assay should have powerful implications for alpha-1-antitrypsin deficiency and also for other human diseases caused by misfolded protein accumulation.