How do the potential "culprits" of various neurological diseases damage the brain?

Deep in the brains of patients with Alzheimer’s disease, most forms of dementia, or concussion-related syndromes (ie, chronic traumatic encephalopathy, CTE), you will find a common suspicious culprit: like a ball of thread Deposition of tau protein aggregates

Recently, a study published by researchers at the University of Colorado Boulder in the journal Neuron showed that tau protein aggregates not only gobble up ribonucleic acid (RNA) inside the cell, but also interfere An important mechanism called RNA splicing affects the cell's protein synthesis process

Dissecting tau protein aggregates

In this study, the researchers isolated tau protein aggregates from cultured cell lines and the brains of mice with Alzheimer's disease-like symptoms, and then used gene sequencing technology to determine the components contained inside

The research team confirmed for the first time that tau protein aggregates contain RNA, which is a key single-stranded molecule related to the normal synthesis of proteins by cells

The tau protein will force RNA and protein to "run in their pockets"

They also discovered that tau proteins interact with cellular structures called nuclear speckles, isolate and replace the proteins in them, and disrupt the RNA splicing process

Splicing is a key link in the process of mRNA maturation in cells.

The fibrous polymerized tau protein not only destroys the nuclear spots, but also grabs RNA and protein fragments from the nuclear spots, sends them into the tau protein aggregates, and enters the cytoplasm together

▲The green part in the picture represents the tangled tau protein aggregates

The first author of the paper, Mr.

Selectively "eliminate" tau protein

Several companies are already conducting clinical trials to test drugs that can completely eliminate tau in patients with neurodegenerative diseases

"A big problem in this field is that no one really knows what tau protein does in a healthy human body.

Note: The original text has been deleted

Reference materials:

[1] Lester, E.