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An Australian study joins a chorus of emerging research looking at the role of tau protein in the development of Alzheimer's.

Scientists unravel a key driver of Alzheimer’s disease

A new Flinders University study has shown how a protein called tau, a critical factor in the development of Alzheimer’s disease, turns from normal to a disease state.

Researchers say the discovery could help to prevent the tau transformation process from happening and lead to better and earlier diagnosis. 

“We have shown that this new concept has therapeutic potential,” says study lead author Kristie Stefanoska.

“Tau modification in Alzheimer’s disease is a complicated process. 

“Ours is the first study to link an initial change in tau with multi-site modification along the entire protein.”

In 2022, there are an estimated 487,500 Australians living with dementia, with Alzheimer's disease accounting for up to 70 per cent of diagnosed cases.

Alzheimer’s, the most common form of dementia, has no cure or effective therapy, in part due to gaps in our understanding of how the progressive neurodegenerative disorder arises in the brain.

While researchers have known for decades that tau accumulates in deposits inside brain cells and gets heavily modified, affecting memory function, it has remained unclear how this process occurs. 

The new findings, recently published in Science Advances, helps to explain the relationship between tau and protein kinases, which are enzymes that introduce changes in tau.

“Usually, protein kinases target specific spots, called phosphorylation sites, in tau and other proteins, and introduce changes only at these specific spots,” says Stefanoska.

“However, we suspected that some of these enzymes are able to target several spots in tau and would do so even more efficiently if tau were already modified at one spot to begin with.”

The study examined mice with both amyloid, a small peptide-protein that lumps around brain nerves in plaques, and tau.

Both proteins are found in the brains of people with Alzheimer's and have long divided researchers over which is a key cause of the disease. 

The Flinders research found that mice did not develop memory deficits when they had a version of tau that lacked one of the identified "master sites", compared with mice that had the usual version of tau.

Researchers will now see whether master sites could be targeted to reduce the toxic properties of tau in Alzheimer’s and be translated into a treatment.

This new mechanism could be used to treat a range of neurological disorders in which tau is involved, including Parkinson’s disease, concussion-induced chronic brain injury and stroke, according to senior study author Dr Arne Ittner.

“Slowing down the changes at master sites of tau in these diseases may put the brakes on tau toxicity and dementia,” says Ittner.

“This new mechanism helps us understand why there is extensive tau modification in Alzheimer’s disease in the first place.

"This will assist researchers and clinicians in designing means for better and earlier diagnosis.”

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