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"2 NEW THERAPIES FOR ALZHEIMER'S"
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Patricio Reyes M.D.
Director, Traumatic Brain Injury, Alzheimer's Disease & Cognitive Disorders Clinics; Phoenix, AZ; Chief Medical Officer, Retired NFL Players Association

Barrow Neurological Institute

St. Joseph's Hospital and Medical Center
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Friday, November 18, 2016

 

Stopping brain protein from turning rogue prevents Alzheimer’s




























Alzheimer’s disease can be prevented by stopping a crucial brain protein from turning rogue, a study in mice suggests.

Tau protein has long been suspected to play a role in causing the condition. In healthy brains, tau is essential for normal cell functioning. But during Alzheimer’s disease, the protein goes haywire, clumping together to form twisted tangles and, it is thought, releasing toxic chemicals that harm the brain.

Now Lars Ittner at the University of New South Wales, Australia, and his colleagues have pinpointed a crucial enzyme that controls how tau proteins behave in the brain. The enzyme, called p38γ kinase, helps keep tau in a healthy, tangle-free state, preventing the onset of memory loss and other symptoms in mice that have been bred to develop Alzheimer’s disease.

Protective effect
The enzyme seems to block Alzheimer’s by interfering with the action of another problem protein, called beta-amyloid. Like tau, clumps of this protein accumulate in the brains of people with Alzheimer’s, making it another suspected cause of the disease.

When beta-amyloid forms these sticky plaques, it can also modify the structure of tau proteins, causing them to form tangles and release toxic chemicals. But Ittner’s team found that p38γ kinase makes a different kind of structural change to tau. If this change is made first, it prevents beta-amyloid from being able to turn tau bad, and mice do not develop the disease.

In people, the levels of this enzyme decline significantly as Alzheimer’s progresses, hinting that boosting this enzyme could help prevent or treat the disease.

New approach
Using an enzyme to stop tau from becoming toxic is novel because most existing research has focused on targeting beta-amyloid, says Ralph Martins at Edith Cowan University in Western Australia.

“We’ve got treatments now that decrease beta-amyloid levels, but they don’t have much efficacy,” he says. “Animal work is increasingly showing that beta-amyloid toxicity is mediated through tau, so it’s an attractive target.”

One reason why Alzheimer’s treatments that have shown promise in mice have frequently failed in clinical trials is because earlier mouse models were designed to only mimic beta-amyloid plaque formation in humans, he says.

Story Source: The above story is based on materials provided by NEWSCIENTIST
Note: Materials may be edited for content and length