Is Alzheimer’s attributable to an enzyme mutation? – healing practice



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Alzheimer’s: tau protein deposition mechanism deciphered

We have now been able to identify a new mechanism by which accumulations of tau protein occur in the brain, leading to the development of Alzheimer’s disease. Understanding the mechanism could lead to new innovative therapeutic approaches.

Mutations in the MARK4 enzyme modify the tau protein in such a way that it forms deposits, which then contribute to the development of Alzheimer’s, according to a study conducted by researchers at Tokyo Metropolitan University. The results were published in the English-language “Journal of Biological Chemistry”.

Trigger of Alzheimer’s MARK4 mutation?

Tau proteins are normally responsible for the stability and supply of nutrients to the cells. However, a specific mutation in an enzyme called MARK4 changes the properties of tau, making it more likely to clump together and become more insoluble. This creates dangerous deposits that kill brain cells and cause Alzheimer’s disease, the researchers explain.

Effects of the accumulation of tau proteins

It has long been believed that Alzheimer’s is caused by the accumulation of tau proteins in brain cells. These sticky deposits lead to the death of nerve cells, which causes impaired memory and motor functions.

Why does tau accumulate?

Until now, it was unclear how and why tau accumulates in the brain cells of people with Alzheimer’s disease. Understanding the cause and mechanism behind this unwanted build-up could pave the way for new treatments and ways to prevent the disease, the researchers hope.

A team led by Kanae Ando of Tokyo Metropolitan University has now examined the mechanisms behind tau deposition and explored the role of the MARK4 (Microtubule Affinity Regulating Kinase 4) enzyme in Alzheimer’s disease.

The tau protein as an important part of the cells

If there are no problems and everything is working correctly, the tau protein is an important part of the structure of the cells or the cytoskeleton. However, if a mutation occurs in the gene that provides the blueprint for MARK4 production, the difficulties begin. Previous research had already linked this to an increased risk of Alzheimer’s, but it was not known why this was the case, experts said in a press release.

Mutations in fruit flies were examined

The team artificially introduced mutations in transgenic Drosophila fruit flies, which also produce human dew. The researchers then looked at how the proteins changed in vivo. They found that this mutated form of MARK4 changes the tau protein, creating a pathological form of tau.

The cause of the incorrect bending of the rope

This unhealthy form of dew had an excess of certain chemical groups that caused misfolding. Furthermore, this form of tau aggregated much more easily and was no longer soluble in so-called detergents, which makes it easier for tau to form clusters and clusters that lead to neuron degeneration, the research team reports.

MARK4: Association with other diseases

Additionally, according to the research team, MARK4 was found to also cause a variety of diseases in which other proteins clump and accumulate. The team’s findings on tau protein accumulation could lead to new treatments and preventative measures for a wider range of neurodegenerative diseases. (how)

Information on the author and source

This text conforms to the requirements of the specialist medical literature, medical guidelines and current studies and has been verified by medical professionals.

Sources:

  • Toshiya Oba, Taro Saito, Akiko Asada, Sawako Shimizu, Koichi M Iijima, Kanae Ando: Microtubule Affinity Regulating Kinase 4 with an Alzheimer-related mutation promotes tau accumulation and acerbates neurodegeneration, in Journal of Biological Chemistry (ver√∂ffentlicht 05.10.2020), Giornale of biological chemistry
  • Tokyo Metropolitan University: cause of Alzheimer’s disease due to common enzyme mutation, Tokyo Metropolitan University

Important note:
This article is a general guide only and should not be used for self-diagnosis or self-treatment. It cannot replace a visit to the doctor.

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