Subscribe for free email updates . Click here to sign up, or log in . 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. Aggregated amyloid-beta proteins, also called amyloid fibrils, are found in the brains of Alzheimer's patients and cause tissue damage and eventually death.
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.