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New Potential Drug Target For Alzheimer's Disease

Date:
June 5, 2000
Source:
University Of Kentucky Medical Center
Summary:
Researchers at the University of Kentucky College of Medicine and the Columbia University College of Physicians and Surgeons have determined that a cell receptor, called RAGE, may be a new potential target for compounds that may treat or prevent Alzheimer's disease.

Researchers at the University of Kentucky College of Medicine and the Columbia University College of Physicians and Surgeons have determined that a cell receptor, called RAGE, may be a new potential target for compounds that may treat or prevent Alzheimer's disease.

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The study leaders were Shi Du Yan, M.D., assistant professor of pathology, and David Stern, M.D., professor of physiology and cellular biophysics and of surgery, both at the Columbia University College of Physicians and Surgeons, and Mark Kindy, Ph.D., associate professor of biochemistry at the UK College of Medicine, UK Sanders-Brown Center on Aging, Stroke Program at the UK Chandler Medical Center, and Veterans Affairs Medical Center in Lexington. The results of the research are published in the June issue of Nature Medicine.

About 60,000 Kentuckians have Alzheimer's disease, and, nationally, 4 million people are estimated to have the disease. A protein called amyloid-beta is thought to be critical in the development of Alzheimer's disease, although the exact role of amyloid-beta is unknown. Aggregated amyloid-beta proteins, also called amyloid fibrils, are found in the brains of Alzheimer's patients and cause tissue damage and eventually death.

The UK researchers have shown that a receptor -- called the receptor for advanced glycation endproducts (or RAGE) and located on the surface of certain neurons -- interacts with amyloid fibrils. RAGE is a multiligand receptor, meaning that it interacts with many molecules. When RAGE interacts with the amyloid fibrils, it accelerates fibril formation and induces cellular dysfunction.

UK researchers disrupted the interaction of RAGE with amyloid fibrils two ways. They added additional amounts of soluble RAGE to neurons with amyloid fibrils. Because the RAGE molecules were not linked to cells, they could interact with the fibrils but not cause cellular dysfunction. They also added an antibody to RAGE that would bind to the receptor and prevent any interaction with amyloid fibrils.

Both methods suppressed amyloid formation in a systemic model of amyloid diseases, including Alzheimer's disease. In addition, by blocking RAGE with an antibody, the researchers found that the process of amyloid fibril deposition was reversed.

"The exciting thing about this research is that it suggests that RAGE may be a potential target for inhibiting amyloid fibril deposition, which would likely inhibit the progression of Alzheimer's disease," Kindy said.


Story Source:

The above story is based on materials provided by University Of Kentucky Medical Center. Note: Materials may be edited for content and length.


Cite This Page:

University Of Kentucky Medical Center. "New Potential Drug Target For Alzheimer's Disease." ScienceDaily. ScienceDaily, 5 June 2000. <www.sciencedaily.com/releases/2000/06/000602074932.htm>.
University Of Kentucky Medical Center. (2000, June 5). New Potential Drug Target For Alzheimer's Disease. ScienceDaily. Retrieved December 19, 2014 from www.sciencedaily.com/releases/2000/06/000602074932.htm
University Of Kentucky Medical Center. "New Potential Drug Target For Alzheimer's Disease." ScienceDaily. www.sciencedaily.com/releases/2000/06/000602074932.htm (accessed December 19, 2014).

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