Dr. McPherson together with postdoctoral fellow, Dr. Franois Blondeau and other colleagues identified 209 proteins. "About half of the proteins we identified are already known to be associated with clathrin-coated vesicles, validating our approach," said Dr. Blondeau. "The rest are novel proteins or proteins with known function that were not previously known to be involved in this process. This identification allows us to hypothesize on how these proteins function in this essential activity of the cells."

"Dr. McPherson's work is a great example of the unique "Cell Map" approach that the Montreal Proteomics Network has taken to perform proteomics experimentation", said Dr. John Bergeron, Director of the Montreal Proteomics Network. "This work allows us to build a map of the location and function of the proteins in the cell, creating a picture of interacting complexes and networks. Ultimately this map will provide a guide to understanding a large number of human diseases."

In June 2000 researchers announced the first draft version of the human genome sequence. This was important because it spelled out all of the genes that define humans and gave the instructions for making the proteins. Proteins do the functional work in the cell and are much more complex than DNA. The roughly 30,000 human genes lead to more than three hundred thousand different proteins. The ability to rapidly and globally detect proteins represents the next step in biology. Revolutions in technology of mass spectrometry which were honoured by the 2002 Nobel Prize for chemistry, have paved the way for proteomics.

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Contact: Sandra McPherson
sandra.mcpherson@mcgill.ca
514-398-1902
McGill University
9-Mar-2004