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Traumatic brain injury (TBI) is one of the main causes of human disability and death.
It can induce inflammatory reactions in the central nervous system and neurodegenerative diseases.
Traumatic brain injury (TBI) is the largest non-genetic, non-aging-related risk factor for Alzheimer's disease (AD).
At present, the treatment of TBI is mainly focused on stabilizing patients and reducing symptoms.
Currently, there is no drug specifically targeting the pathophysiological process that leads to neurodegeneration after brain injury.
Abnormal phosphorylation of tau protein is the basis of AD and other neurodegenerative diseases.
In recent years, it has been discovered that abnormal phosphorylation of au protein also exists in the process of TBI.
Speaking of the abnormality of the tau protein in TBI, I have to mention the famous Chinese scientist Professor Lu Kunping, who is a tenured professor of Harvard Medical School and the founder and director of the Translational Therapy Department of Beth Israel Deaconess Medical Center affiliated to Harvard Medical School.
Published in 2015 The article mentioned that within 12 hours after TBI, the brain will form an abnormal phosphorylated tau protein isoform, which subsequently destroys the axon microtubule network and mitochondrial transport, and leads to cell apoptosis.
Clinical studies have found that the acetylation of tau protein lysine (K) 280 in the brain of patients with chronic traumatic encephalopathy increases.
Due to the close relationship between TBI and AD, the increased acetylation level of tau protein may be the cause of neurological diseases.
On May 13, 2021, Andrew A.
Pieper's research team from the Department of Psychiatry at Case Western Reserve University published an article in the Cell magazine, revealing that TBI can induce AD-like tau acetylation, reducing this abnormal acetylation and exerting protection effect.After TBI, the levels of tau protein acetylation in the cortex and hippocampus of mice increased after TBI.
Researchers found that there were increased levels of tau protein acetylation in the hippocampus and cortical brain regions of brain injury model mice, but this increase was not observed in the hypothalamus (in In brain injury, the hypothalamus is like an umbrella to protect it from injury).
They examined the frontal cortex tissue of 9 AD patients and found that AD patients with a previous history of TBI had elevated tau protein acetylation levels.
In vitro cell experiments found that tau acetylation mimics can induce a large number of apoptosis in isolated brain injury model cells.
There is a certain degree of degeneration of the axon initiation segment in mutant mice that mimic tau acetylation.
This indicates that acetylation of tau protein is harmful to neurons.
Protein acetylation in AD disease is related to the nitrosylation of GAPDH.
The latter synergistically enhances the activity of histone acetyltransferase p300/CBP and inhibits the activity of histone deacetylase Sirtuin1 (Sirt1), thereby promoting acetylation.
They found that GAPDH and Sirt1 undergo S-nitrosylation after brain injury.
Continuous intraperitoneal injection of GAPDH S-nitrosylation blocker CGP3466B can reduce the levels of tau protein and p300/CBP acetylation, prevent degeneration of the initial segment of axons, and repair cognitive dysfunction after brain injury.
In addition, inhibiting p300/CBP acetylation can also play a similar role to inhibiting GAPDHS-nitrosylation.
The researchers found that after TBI, the acetylation level of tau protein in the serum of wild-type mice and Tau-knockout mice could be detected, and the level of tau protein acetylation in the serum was reduced after CGP3466B treatment.
In addition, the acetylation level of tau protein in the serum of TBI patients also increased.
Based on the above results, researchers believe that tau protein acetylation has the potential as a blood biomarker for neurodegeneration after TBI.
In general, this article reveals the molecular mechanism that causes tau acetylation in traumatic brain injury, which can play a protective role in inhibiting abnormal tau acetylation.
[References] 1.
Antibody against early driver of neurodegeneration cis P-tau blocks brain injury and tauopathy 2.
Shin et al.
, Reducing acetylated tau is neuroprotective in brain injury, Cell (2021), https://doi.
org/10.
1016 /j.
cell.
2021.
03.
032 The pictures in the article are all from the references.
Download the original method: Click on the Baidu web disk link: https://pan.
baidu.
com/s/1uBVahGq9ykpLXVYP22-v4w Extraction code: 1dpi
Traumatic brain injury (TBI) is one of the main causes of human disability and death.
It can induce inflammatory reactions in the central nervous system and neurodegenerative diseases.
Traumatic brain injury (TBI) is the largest non-genetic, non-aging-related risk factor for Alzheimer's disease (AD).
At present, the treatment of TBI is mainly focused on stabilizing patients and reducing symptoms.
Currently, there is no drug specifically targeting the pathophysiological process that leads to neurodegeneration after brain injury.
Abnormal phosphorylation of tau protein is the basis of AD and other neurodegenerative diseases.
In recent years, it has been discovered that abnormal phosphorylation of au protein also exists in the process of TBI.
Speaking of the abnormality of the tau protein in TBI, I have to mention the famous Chinese scientist Professor Lu Kunping, who is a tenured professor of Harvard Medical School and the founder and director of the Translational Therapy Department of Beth Israel Deaconess Medical Center affiliated to Harvard Medical School.
Published in 2015 The article mentioned that within 12 hours after TBI, the brain will form an abnormal phosphorylated tau protein isoform, which subsequently destroys the axon microtubule network and mitochondrial transport, and leads to cell apoptosis.
Clinical studies have found that the acetylation of tau protein lysine (K) 280 in the brain of patients with chronic traumatic encephalopathy increases.
Due to the close relationship between TBI and AD, the increased acetylation level of tau protein may be the cause of neurological diseases.
On May 13, 2021, Andrew A.
Pieper's research team from the Department of Psychiatry at Case Western Reserve University published an article in the Cell magazine, revealing that TBI can induce AD-like tau acetylation, reducing this abnormal acetylation and exerting protection effect.After TBI, the levels of tau protein acetylation in the cortex and hippocampus of mice increased after TBI.
Researchers found that there were increased levels of tau protein acetylation in the hippocampus and cortical brain regions of brain injury model mice, but this increase was not observed in the hypothalamus (in In brain injury, the hypothalamus is like an umbrella to protect it from injury).
They examined the frontal cortex tissue of 9 AD patients and found that AD patients with a previous history of TBI had elevated tau protein acetylation levels.
In vitro cell experiments found that tau acetylation mimics can induce a large number of apoptosis in isolated brain injury model cells.
There is a certain degree of degeneration of the axon initiation segment in mutant mice that mimic tau acetylation.
This indicates that acetylation of tau protein is harmful to neurons.
Protein acetylation in AD disease is related to the nitrosylation of GAPDH.
The latter synergistically enhances the activity of histone acetyltransferase p300/CBP and inhibits the activity of histone deacetylase Sirtuin1 (Sirt1), thereby promoting acetylation.
They found that GAPDH and Sirt1 undergo S-nitrosylation after brain injury.
Continuous intraperitoneal injection of GAPDH S-nitrosylation blocker CGP3466B can reduce the levels of tau protein and p300/CBP acetylation, prevent degeneration of the initial segment of axons, and repair cognitive dysfunction after brain injury.
In addition, inhibiting p300/CBP acetylation can also play a similar role to inhibiting GAPDHS-nitrosylation.
The researchers found that after TBI, the acetylation level of tau protein in the serum of wild-type mice and Tau-knockout mice could be detected, and the level of tau protein acetylation in the serum was reduced after CGP3466B treatment.
In addition, the acetylation level of tau protein in the serum of TBI patients also increased.
Based on the above results, researchers believe that tau protein acetylation has the potential as a blood biomarker for neurodegeneration after TBI.
In general, this article reveals the molecular mechanism that causes tau acetylation in traumatic brain injury, which can play a protective role in inhibiting abnormal tau acetylation.
[References] 1.
Antibody against early driver of neurodegeneration cis P-tau blocks brain injury and tauopathy 2.
Shin et al.
, Reducing acetylated tau is neuroprotective in brain injury, Cell (2021), https://doi.
org/10.
1016 /j.
cell.
2021.
03.
032 The pictures in the article are all from the references.
Download the original method: Click on the Baidu web disk link: https://pan.
baidu.
com/s/1uBVahGq9ykpLXVYP22-v4w Extraction code: 1dpi
