Tau proteins are normally responsible for the stability and supply of nutrients to the cells. However, a specific mutation of an enzyme called MARK4 changes the properties of Tau, making it more likely to aggregate and become insoluble. This creates dangerous deposits that kill brain cells and can cause Alzheimer’s disease, explain the researchers.
Mutations of the MARK4 enzyme alter Tau protein to form deposits that contribute to the development of Alzheimer’s disease, according to a study involving researchers from Tokyo Metropolitan University. The results were published in the English-language “Journal of Biological Chemistry”.
A new mechanism has now been identified by which tau protein accumulates in the brain, which leads to the development of Alzheimer’s disease. Understanding this mechanism could lead to groundbreaking new treatment approaches.
Effects of Tau protein accumulation
Alzheimer: Mechanism of Tau protein deposits deciphered
It has long been assumed that Alzheimer’s is caused by the accumulation of deposits of the Tau protein in the brain cells. These sticky deposits lead to the death of nerve cells, resulting in impaired memory and motor functions.
Until now it was not clear how and why Tau accumulates in the brain cells of people with Alzheimer’s disease. Understanding the cause and the mechanism behind this unwanted accumulation could open the way for new treatments and ways to prevent the disease, the researchers hope.
MARK4 mutation trigger of Alzheimer’s disease?
A team led by Kanae Ando of Tokyo Metropolitan University has now investigated the underlying mechanisms of tau deposition and the role of the enzyme MARK4 (Microtubule Affinity Regulating Kinase 4) in Alzheimer’s disease.
If no problems occur and everything works properly, Tau protein is an important part of the structure of cells or the cytoskeleton. However, if a mutation occurs in the gene that provides the blueprint for the production of MARK4, the difficulties begin. Earlier research had already linked this to an increased risk of Alzheimer’s, but it was not known why this is the case, the experts report in a press release.
The team artificially introduced mutations into transgenic Drosophila fruit flies, which also produce human dew. The researchers then investigated how the proteins changed in vivo. They discovered that this mutated form of MARK4 makes changes to the tau protein, resulting in a pathological form of tau.
In addition, according to the research group, MARK4 was also found to cause a variety of diseases in which other proteins aggregate and accumulate. Thus, the team’s findings on tau protein accumulation could lead to new treatments and preventive measures for a broader range of neurodegenerative diseases. (as)
This unhealthy form of dew had an excess of certain chemical groups that caused it to misfold. In addition, this form of dew aggregated much more easily and was no longer soluble in so-called detergents, making it easier for the dew to form accumulations and clumps that lead to neuron degeneration, the research team reported.
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