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Function found for Alzheimer's protein
Date:9/10/2010

In people with Alzheimer's, the brain becomes riddled with clumps of protein, forming what are known as amyloid plaques. Now, a report appearing in the September 17th print issue of Cell appears to have found a function for the amyloid precursor protein (APP for short) that yields the prime ingredient in those plaques.

It turns out that APP is an iron oxidase whose job it is to convert iron from an unsafe form to a safe one for transport or storage. When APP fails to function properly, as it does in Alzheimer's disease, iron levels inside neurons mount to toxic levels.

"This opens a big window on Alzheimer's disease and iron metabolism," said Ashley Bush of The Mental Health Research Institute, University of Melbourne.

"Although people have attributed several important physiological roles to APP," added Jack Rogers of Harvard Medical School, "this now gives us an idea of what this critical protein does to underpin its role in iron metabolism."

In fact, there were some clues. Some years ago, the researchers discovered that the RNA template for the APP protein includes an iron-responsive element. When iron levels rise, cells ramp up their APP production.

But amyloid in and of itself doesn't really explain what goes wrong in the Alzheimer's brain. "There has been a lot of attention on amyloid, but it seems it is not a simple matter of amyloid as the sole culprit," Bush said. For one thing, trials of drugs designed to target and clear amyloid plaques haven't worked as intended.

In fact, the disease is also complicated by high concentrations of metals, including iron that builds up inside neurons and zinc that accumulates within the amyloid plaques outside of those brain cells. And studies have also linked the loss of other iron oxidases to pathological iron accumulation and neurodegenerative diseases characterized by dementia. "If iron is left unbridled in its soluble form, it can cause nerve death and
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Contact: Cathleen Genova
cgenova@cell.com
617-397-2802
Cell Press
Source:Eurekalert

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