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

damage," Rogers said.

After 10 years of work, it appears Bush's and Roger's teams have connected the dots from the abnormal exchange of zinc to amyloid pathology and iron accumulation in Alzheimer's disease. "It's a sequence of dominoes falling onto each other," Bush said.

They show that APP is a bona fide iron oxidase, with properties much like the best-known iron oxidase (called ceruloplasmin), which is not expressed in neurons. Loss of APP in cells and primary neurons causes iron levels to build, while increasing APP promotes the export of iron out of cells.

Mice lacking APP become vulnerable to dietary iron, which causes the unsafe, oxidative form of iron to build in the animals' neurons, they show. Finally, they show that zinc in amyloid blocks APP's normal iron-balancing activities in the Alzheimer's brain.

Based on the new evidence, the researchers propose that elevated iron in the Alzheimer's brain summons further APP production. But that APP -- generated for the purpose of exporting iron -- gets disabled by high levels of zinc that dissociate from the amlyoid plaques.

The findings suggest that zinc may be an ideal target in the fight against Alzheimer's disease, the researchers say. In fact, studies in animals and early, short-term clinical trials of zinc-ionophore drugs including clioquinol and PBT2 in people with Alzheimer's disease have so far produced promising results. PBT2 is slated for further testing.

"Our findings authenticate zinc as a target," Bush said. "It really makes it look like an attractive place to hit."

Although Rogers said that he doesn't want to raise hopes for an Alzheimer's cure too high, "this is definitely an important step in getting to a therapy to retard the Alzheimer's disease process."


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Contact: Cathleen Genova
cgenova@cell.com
617-397-2802
Cell Press
Source:Eurekalert

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