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Small changes in protein chemistry play large role in Huntington's disease
Date:12/24/2009

r genetic engineering, Dr. Yang altered the same two critical amino acids at the end of the mutant huntingtin protein to either mimic phosphorylation (phosphomimetic) or resist it (phosphoresistant). Mice with the phosphoresistant version of the protein developed symptoms of Huntington's, but mice with the phosphomimetic version remained free of symptoms and huntingtin clumps up to one year.

Meanwhile, test tube experiments by Dr. Wetzel's group in Pittsburgh showed that phosphomimetic modification of a huntingtin fragment reduced its tendency to form clumps. Together, data from the mouse and test tube experiments provide strong support for the idea that phosphorylation acts as a molecular switch to alter clumping of the mutant protein, the researchers said.

The nearly complete lack of any signs of disease in the phosphomimetic Huntington mice may point toward new strategies to treat the disorder someday. Dr. Yang said, "Drugs that enhance or mimic the effects of phosphorylation may help to detoxify the mutant huntingtin protein."

If such drugs could be developed, Drs. Steffan and Thompson theorize, they would likely be most effective at early stages of the disease, but less so at later stages, when the clearance machinery appears to run down. Dr. Yang said he plans to examine older mice carrying the phosphomimetic version of mutant huntingtin to determine how long they are protected from the disease.


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Contact: Gregory Roa
greg.roa@nih.gov
301-496-5751
NIH/National Institute of Neurological Disorders and Stroke
Source:Eurekalert

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