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Researchers find new clue to degenerative disease
McGill team shows how mutated proteins that 'misfold' in cells are recognized
Irwin Block
The Gazette Wednesday, May 19, 2004
Researchers at McGill University have discovered a key step that they believe will help provide targets
for treating degenerative diseases like Alzheimer's,Parkinson's and cystic fibrosis.
The research team from the faculty of medicine identified a
mechanism that recognizes misfolded proteins in cells.
This is considered crucial, as misfolded proteins are extremely harmful to cells and contribute to degenerative diseases, David Thomas, McGill's chairperson of biochemistry, said yesterday.
Once misfolded proteins are identified, they can be removed from the cells.
The finding comes after 10 years of research by Thomas and John Bergeron, chairperson of anatomy and cell biology at McGill. The laboratory experiments, described in an article in the February edition of Nature Structural and Molecular Biology, were carried out by doctoral student Sean Taylor and post-doctoral fellow Andrew Ferguson.
"Misfolded proteins are the basis of everything from mad cow disease to cystic fibrosis, emphysema and Tay-Sachs," Thomas said.
Proteins that contain mutations will invariably misfold.
The researchers showed that a central enzyme known as UDP-glucose: glycoprotein glucosyltransferase can detect areas of disorder and activity of proteins in cells. "Our findings are an important step toward the development of innovative prevention and treatment for such diseases," Thomas said.
The scientists received grants from the Canadian Institutes of Health Research and the Canada Foundation for Innovation.
iblock [at] thegazette [dot] canwest [dot] com
Originally reported on Canada.com
Reference: "The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation." Nat Struct Mol Biol. 2004 Feb;11(2):128-34. Epub 2004 Jan 04.