Summary: Studies show how the taut protein associated with Alzheimer’s changes from normal to sick.

Source: Flinder University

Alzheimer’s disease, the most common form of dementia, currently has no cure or effective treatment, partly due to gaps in our understanding of how neurodegenerative disorders develop in the brain.

Now, a study by Flinders University shows how a protein called tau, which is a key factor in the development of Alzheimer’s disease, changes from normal to disease and how this discovery can be used as a therapeutic target.

Published in the journal Advances in scienceThe team’s findings promise to prevent the change process, thus keeping the tumor healthy and eliminating toxic effects on brain cells.

“Along with the small amount of amyloid-beta, tau protein is a major cause of Alzheimer’s disease,” said Dr. Arne Etner, senior researcher at the Flinders Health and Medical Research Institute at Neuroscience. They are partners.

During the development of Alzheimer’s disease, toxins accumulate in the brain cells. In this process, the tau is greatly improved, and different deposits carry many small changes in the tau molecule.

While such changes have been known by neuropathologists for decades, it is unclear how Taw will come to this advanced stage. The new study uncovers this part of the secret and provides a new way to explain how to improve it.

The study set out to answer whether a change in one place in tau makes it easier to adjust to another place. The group focuses on the relationship between tau and protein kinases, which are enzymes that promote tau changes.

Dr. Christine Stefanosca, a lead researcher at Flindersz University, says:

However, we suspected that some of these enzymes could target multiple locations in tau and that it would be more effective if Tau was adjusted in one location.

The researchers conducted a large-scale experiment involving up to 20 different mutations in tau and 12 enzymes, focusing on the significant changes in the brains of Alzheimer’s patients.

Although the study found that one change made it easier to promote another, it identified “major sites” in tau as special areas that control subsequent improvements to most other websites.

“By streamlining these major websites, we have been able to drive improvements elsewhere in Tau, which is leading to a similar situation in Alzheimer’s patients,” said Dr. Itner.

The team’s next step was to see if master sites could be targeted to reduce Alzheimer’s toxicity at master sites.

The current study hired both amyloid and tau mice and developed Alzheimer’s-like symptoms, including memory loss. The researchers found that rats did not develop memory deficits when they had a missing version of tau, which was one of the main sites compared to rats with a standard version of tau.

The team is now examining how to translate the results into treatment.

“We have shown that this new concept has therapeutic potential, but future work is needed to understand the role of these major sites in health and disease,” said Dr. Stefanosca.

“Improvement in Alzheimer’s disease is a complex process. The first change in our tau is the first study to link whole protein to mass enhancement.

According to the authors, the new system and the main areas of the center are involved in a variety of neurological disorders, including Parkinson’s disease, chronic traumatic brain injury and stroke.

watch out

“Reducing changes in the major areas of the bowel in these diseases can lead to tau toxicity and dementia,” said Dr. Etner.

“This new method will help us understand why there is widespread improvement in Alzheimer’s disease in the first place. This will help researchers and clinics to design better and earlier diagnostic methods.

So Alzheimer’s disease research news

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Source: Flinder University
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Preliminary study Open access.
”The disappearance of Alzheimer’s disease single mast site eliminates hyperphosphorylation”By Kristie Stefanoska et al. Advances in science

Draft

The disappearance of Alzheimer’s disease single mast site eliminates hyperphosphorylation

Hyper phosphorylation of neuronal tumor proteins is a hallmark of neurodegenerative tumors such as Alzheimer’s disease. The central unanswered question is why Taw becomes hyperphosphorylate.

Here, we show that tau phosphorylation is governed by interdependence — the mechanical relationship between the first site-specific and the next multi-site phosphorylation. A systematic assessment of the location of various residues (threonine-50, threonine-69 and threonine-181) identified the major sites that determine phosphorus expansion in several epithelium.

CRISPR point mutation and human expression show that site support in Alzheimer’s mice regulates physiological and amyloid-related multi-site phosphorus and cognitive impairments.

Combined master sites and p38a targeting, central central tow kinase associated with interference, coordinated intermittent hyperphosphorylation. In summary, our work demonstrates how complex tau phosphorylation arises to inform the therapeutic and biomarkers design for tauopathies.