Brain Enzyme is Like a Double Whammy for Alzheimer's Disease

by Krishna Bora on  August 22, 2012 at 10:17 PM Press Release
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The underlying cause of Alzheimer's disease are not fully understood, but still a good deal of evidence points to the accumulation of several proteins have come under light. â-amyloid, a protein that's toxic to nerve cells is formed by the activity of several enzymes, including one called BACE1.
 Brain Enzyme is Like a Double Whammy for Alzheimer's Disease
Brain Enzyme is Like a Double Whammy for Alzheimer's Disease

Most Alzheimer's disease patients have elevated levels of BACE1, which in turn leads to more brain-damaging â-amyloid protein. In a paper published August 15 in The Journal of Neuroscience, researchers at Sanford-Burnham Medical Research Institute (Sanford-Burnham) found that BACE1 does more than just help produce â-amyloid—it also regulates another cellular process that contributes to memory loss. This means that just inhibiting BACE1's enzymatic activity as a means to prevent or treat Alzheimer's disease isn't enough—researchers will have to prevent cells from making it at all.

"Memory loss is a big problem—not just in Alzheimer's disease, but also in the normal aging population," said Huaxi Xu, Ph.D., professor in Sanford-Burnham's Del E. Webb Neuroscience, Aging, and Stem Cell Research Center and senior author of the study. "In this study, we wanted to better understand how BACE1 plays a role in memory loss, apart from â-amyloid production."

To do this, Xu and his team used a mouse model that produces human BACE1. Mice produce a different type of â-amyloid, one that's far less toxic than the human version. So, in this system, they could look solely at how BACE1 functions independent from â-amyloid formation. If BACE1 only acted to produce â-amyloid, the researchers would expect to see no effect when mice produce human BACE1—since mouse â-amyloid isn't very toxic, extra BACE1 would be no big deal. Instead, they saw that the enzyme still impaired learning and memory, indicating a secondary function at work.

Source: Eurekalert

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