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One step further toward treatment for degenerative diseases

Montreal, May 17, 2004 - Scientists at McGill University's Faculty of Medicine have discovered a key step that will provide new targets for treatments of many degenerative diseases such as Alzheimer's, Cystic Fibrosis and Diabetes. Dr. David Thomas, Chair of Biochemistry, Dr. John Bergeron, Chair of Anatomy and Cell Biology and colleagues have identified a mechanism by which misfolded proteins are recognized in the cell. This is a critical process as proteins that are not correctly folded or shaped are extremely harmful to cells and are the basis for a number of human degenerative diseases. The findings were published in the prestigious journal Nature Structural and Molecular Biology.

"We have identified a central enzyme that is sensitive to very subtle changes in the folded state of a protein," explained Dr. David Thomas. "Proteins are the building blocks and machines of our bodies. In order for them to work correctly they have to fit together. Cells in our bodies have developed quality control mechanisms to assure proper folding. When something goes wrong, cells can accumulate misfolded proteins that don't work properly. The misfolding of proteins is the basis for a number of neurodegenerative diseases such as Alzheimer's and Parkinson's. Our findings are an important step toward the development of innovative prevention and treatment strategies for such diseases."

Dr. Thomas and Dr. Bergeron, together with graduate student Sean Taylor and post-doctoral fellow Andrew Ferguson, showed that the enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) can sense specific regions of disorder and activity of proteins key steps to recognizing misfolded proteins and removing them from the cells.

The paper and accompanying News and Views are currently available online.


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


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