Alzheimers disease transmission may be similar to infectious prion diseases www.uthouston.edu/media/story.htm?id=3541058 HOUSTON (Oct. 4, 2011) The brain damage that characterizes Alzheimers disease may originate in a form similar to that of infectious prion diseases such as bovine spongiform encephalopathy (mad cow) and Creutzfeldt-Jakob, according to newly published research by The University of Texas Health Science Center at Houston (UTHealth). Alzheimers disease is a form of progressive dementia that affects memory, thinking and behavior. Of the estimated 5.4 million cases of Alzheimers in the United States, 90 percent are sporadic. The plaques caused by misshapen aggregates of beta amyloid protein, along with twisted fibers of the protein tau, are the two major hallmarks associated with the disease. Alzheimer's is the sixth leading cause of death in the United States, according to the Alzheimers Association. Researchers injected the brain tissue of a confirmed Alzheimers patient into mice and compared the results to those from injected tissue of a control without the disease. None of the mice injected with the control showed signs of Alzheimers, whereas all of those injected with Alzheimer's brain extracts developed plaques and other brain alterations typical of the disease. We took a normal mouse model that spontaneously does not develop any brain damage and injected a small amount of Alzheimers human brain tissue into the animals brain, said Soto, who is director of the Mitchell Center. The mouse developed Alzheimers over time and it spread to other portions of the brain. We are currently working on whether disease transmission can happen in real life under more natural routes of exposure.