ANN ARBOR---If you think you finally understand the human genome and why it's important, get ready for proteomics. Discovering how cells respond to genetic instructions by creating millions of protein variations and figuring out what all those proteins do will be the next frontier of biomedical research.
The ability to identify cellular proteins will be especially valuable in cancer research, because each type of cancer produces its own protein biomarkers, according to Samir M. Hanash, M.D., Ph.D., a professor of pediatrics and communicable diseases in the University of Michigan Medical School. Unfortunately, current technology is neither accurate nor sensitive enough to detect most of these proteins, which often exist only in trace amounts.
A new liquid-phase protein separation technology under development at the U-M could help scientists solve the proteomics puzzle. The system eliminates the difficult, time-consuming 2-D gel electrophoresis method scientists now use to separate cells into individual proteins---the critical first step in proteomics analysis.
In the U-M system, proteins remain in a liquid phase throughout the separation process. According to David Lubman, Ph.D., a U-M professor of chemistry, liquid phase has many advantages over gels. "The process takes hours instead of days. It can handle large quantities of protein and detect trace amounts of protein," Lubman says. "It is easily interfaced for mass spectrometry detection, data are automatically digitized online and the entire process has the potential to be fully automated."
Hanash presented data from studies of the U-M protein separation method compared to traditional 2-D PAGE techniques on April 18 at the "Experimental Biology 2000" meeting in San Diego, Calif. Results also were published in the March 15 issue of Analytical Chemistry in an article by Hanash, Lubman, and others on their research team.