A study published last November in Science magazine has changed our understanding of the molecular cascade that triggers Alzheimer’s disease.

A team from the New South Wales University in Australia focussed on the role of tau protein phosphorylation in neurons.

Aberrant tau phosphorylation on multiple sites is known to be one of the first steps in promoting the formation of tangles in neurons, which ultimately lead to their death.

According to the research team, phosphorylation of at least one site, located at position 205, would play a protective role in the cell.

This protective mechanism is thought to delay beta-amyloid oligomers ability to trigger neuronal cell death until a certain point.

The research team made their discovery after studying the involvement of protein p38-gamma, which directly phosphorylates tau at position 205.

It showed, using genetic and molecular biology experiments, that removing p38-gamma could increase the speed at which Alzheimer-related symptoms developed in a mouse model.

It also noticed that the brains of Alzheimer disease patients were expressing fewer p38-gamma proteins compared to normal brains.

According to the authors of the paper, p38-gamma would therefore protect neurons from being damaged through its action on tau.

This observation suggests a new strategy for preventing the progression of Alzheimer’s disease.

Increasing the activity of this protein in the brain should theoretically improve neuronal survival and limit the speed at which the disease advances.

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