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Gladstone scientists identify protein form linked to Huntington's disease
Date:10/30/2011

ypes were the most toxic. In laboratory experiments on mice, he and his colleagues screened numerous antibodies that each bind uniquely to one type of misfolded htt in order to identify and tag each type. These antibodies acted as molecular tracking devices that Dr. Finkbeiner monitored with an automated microscope and specialized software, both of which his lab created. Experiments revealed that one of the antibodies, 3B5H10, bound to a form of htt closely linked to neuron death and, therefore, disease progression.

"Now that our experiments have identifiedat a cellular levelwhen neurons will die, it will be easier to develop drugs that target the toxic form of htt that causes Huntington's symptoms," said Dr. Finkbeiner, who is also a professor of neurology and physiology at the University of California, San Francisco (UCSF), with which Gladstone is affiliated.

"Dr. Finkbeiner's powerful and precise approach could enable the development of pharmaceutical treatments for other diseases as well," added Lennart Mucke, MD, who directs neurological research at Gladstone. "These methods are applicable to many devastating neurodegenerative conditions, especially Parkinson's disease and Alzheimer's."


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Contact: Anne Holden
anne.holden@gladstone.ucsf.edu
415-734-2534
Gladstone Institutes
Source:Eurekalert  

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Gladstone scientists identify protein form linked to Huntington's disease
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