What is Glutathione? What are the Benefits of Glutathione?

 Your competent? doctor has this covered already, right? Oh NO, you DON'T have a functioning stroke doctor, do you?

• glutathione (7 posts to December 2013)

What is Glutathione? What are the Benefits of Glutathione?

What is Glutathione?

What are the Benefits of Glutathione? What Does It Do?

Which diseases is glutathione good for? 

How Should Glutathione Level Be? 

Which Foods Increase Glutathione Levels?

 How to Increase Glutathione Levels in the Body

How to take glutathione?

Pointing out that glutathione is a very important antioxidant that slows down the rate of aging, Harika Özkaya said, "The more glutathione you have in your body, the healthier your cells and your mitochondria, the energy source of your cells. She said.

What is Glutathione?

Glutathione is a tripeptide consisting of three amino acids (glutamate, cysteine and glycine) and is naturally produced in the liver. These amino acids that make up glutathione are non-essential amino acids that our body can produce on its own when needed. Glutathione, a powerful antioxidant, plays a critical role in reducing oxidative stress by fighting free radicals in the body.

What are the Benefits of Glutathione? What Does It Do?

Antioxidants fight molecules that damage cells in the body called free radicals. In particular, glutathione protects cells by neutralizing the effects of reactive hydroxyl free radicals and other oxygen-derived free radicals. However, glutathione also promotes cell health by counteracting the effects of oxidative stressors and other biomolecules that damage DNA. However, factors such as poor diet, infections and constant stress can lead to reduced levels of glutathione in the body. There is also a natural decrease in glutathione levels with age.

Research has also found that many chronic diseases are associated with a decrease in glutathione levels. These include;

• Alzheimer's
• Cancer
• Chronic liver disease
• Cystic fibrosis
• Diabetes
• Hypertension
• HIV, AIDS
• Lupus
• Infertility (female, male)
• Parkinson's 

As a result, glutathione is an important part of the body's natural defense mechanisms and maintaining these levels is essential for a healthy life.

Which diseases is glutathione good for? 

Diabetes is a health problem that develops as a result of the body not producing enough insulin or not being able to use the insulin it produces effectively. High levels of sugar in the blood (hyperglycemia) and insulin deficiency or resistance can lead to increased oxidative stress. This oxidative stress is a critical factor in the progression of diabetes. Furthermore, low levels of glutathione can exacerbate oxidative stress and insulin resistance.

Recent research has shown that dietary supplements can increase glutathione production, thereby reducing oxidative stress and improving insulin sensitivity. These findings suggest that glutathione supplements may be an important aid in diabetes management.
 

Anti-Aging Effects: Cell Regeneration and its Effect on the Aging Process

Glutathione has attracted attention in recent years as an effective solution against the aging process. The effects of aging are realized not only on the skin, but also in many areas of the body, from nails to hair. The accumulation of free radicals is one of the most important factors that accelerate this process. Glutathione helps slow down aging by fighting harmful free radicals. If free radicals accumulated in the body are not removed, problems such as wrinkles, broken nails and hair loss become inevitable. Glutathione not only repairs damaged cells but also contributes to the production of new and young cells through its mitochondrial action. Aging of cells can cause serious problems not only in terms of aesthetics but also in terms of physical health. Therefore, it is of great importance to take steps to protect the health of the body.

Studies have shown that people who live well into their 80s and beyond have higher levels of glutathione. Low glutathione levels send signals that trigger cell death (apoptosis). Given the critical role of glutathione in cellular and mitochondrial function, the health and longevity benefits are enormous.
In summary, the more glutathione you have in your body, the healthier your cells and mitochondria are. The lower the glutathione level, the greater the likelihood of cellular deterioration, disease risk and cellular death.
 

Liver Health: The Importance of Glutathione in the Detoxification Process

The liver is our most important detox organ. Glutathione is considered to be the most important assistant of detoxification processes in the liver.

How Should Glutathione Level Be? 

Glutathione levels may vary depending on a person's age, general health, lifestyle and other individual factors. Although there is currently no ideal glutathione level, it is accepted that this level should be optimal in order for the body to effectively cope with oxidative stress, for the immune system to function properly and for cellular functions to be protected.

Which Foods Increase Glutathione Levels?

Glutathione is very important for a healthy life. Although the body produces some of its own glutathione, poor diet, smoking, air pollution, stress, infections and radiation reduce the proportion of glutathione in the body.
 

Foods Containing Glutathione:

This is why the rate we get from daily food is very important. Foods that increase our glutathione levels are as follows:

• Broccoli
• Brussels sprouts
• Cabbage
• Cauliflower
• Avocado
• Peach
• Watermelon
• Cinnamon
• Cardamom
• Turmeric
• Tomato
• Peas
• Garlic
• Onion
• Red pepper

 How to Increase Glutathione Levels in the Body

• Include sulfur-rich foods in your diet (as they contain glutathione precursor compounds). Include garlic, onions, broccoli, cabbage, kale, collard greens, cauliflower, etc. in your diet.
• Drink the juice of cheeses that you are sure are homemade or made from antibiotic-free milk. This is a great source of cysteine and is important for glutathione synthesis.
• Exercise increases your glutathione level and thus strengthens the immune system.
• Alpha lipoic acid and N-acetyl cysteine play an important role in increasing glutathione levels.
• Broccoli, spinach, tomatoes, peas, cabbage, chard, red meat and organ meats are among the alpha lipoic rich foods. Eggs, milk, white and red meat, onions, garlic, cauliflower, cabbage support the production of N-acetyl cysteine.
• Take folate, vitamin B6 and B12 regularly.
• Selenium is known as a powerful anti-oxidant. Be careful to get it from food.
• Vitamin C and E help recycle glutathione and prevent disease.

How to take glutathione?

Glutathione supplements can be taken orally, by injection or intravenous (IV) infusion. IV treatment is usually the most effective because it provides glutathione directly and quickly to the body. 

Glutathione supplementation can be beneficial for generally healthy individuals, but is not necessary or appropriate for everyone. If you do not have health problems and are considering taking supplements to support your health, short-term use is generally safe. However, for long-term and high-dose use, it is important to seek medical advice based on individual needs.
 

Glutathione Prevents Cellular Clogs

 Ask your competent? doctor for the EXACT PROTOCOL that will deliver glutathione in the correct amounts to the right locations. S/he has known all about glutathione for over a decade, right?

• glutathione (6 posts to December 2013)

Glutathione Prevents Cellular Clogs

Summary: The endoplasmic reticulum (ER) is the cell’s busiest manufacturing hub, responsible for folding and exporting proteins. For decades, scientists knew the ER required a very specific chemical balance to function, but the “machinery” behind it was a mystery.

Now, researchers have identified a protein called SLC33A1 that acts as a glutathione regulator. The study reveals that this regulator ensures proteins are folded correctly, a process that, when broken, leads to the toxic “clogs” found in neurodegenerative diseases and cancer.

Key Findings

• Mitochondria vs. ER: While glutathione “keeps the lights on” in the mitochondria, its primary job in the ER is “quality control.”
• First Visual Evidence: Working with Memorial Sloan Kettering, the team was able to visualize exactly how the SLC33A1 protein binds and moves its cargo across the ER membrane.
• New Therapeutic Avenues: Identifying this transporter opens the door for synthesis inhibitors that could treat neurodevelopmental disorders or specific types of cancer by manually recalibrating the cell’s glutathione levels.

Source: Rockefeller University

In the past several years, Rockefeller University’s Kivanç Birsoy and his team in the Laboratory of Metabolic Regulation and Genetics have revealed remarkable details about the antioxidant glutathione, which plays many essential roles in the body, from clearing free radicals to repairing cellular damage.Among other things, they’ve discovered the transporter that shuttles glutathione to where it’s needed, how glutathione keeps iron levels in check, and the metabolite’s complicated relationship with mitochondria, the energy center of the cell, where it both keeps the lights on yet can drive the metastasis of breast cancer.

Defining how metabolites are transported across organelle membranes reveals fundamental principles of cell biology and disease. Credit: Neuroscience News

Now they’ve discovered glutathione’s key part in maintaining the smooth operations of a protein-producing hub in the cell called the endoplasmic reticulum (ER). They shared their results in a paper published in Nature Cell Biology.

“Rockefeller has an incredibly rich history of research on the endoplasmic reticulum, so we know that when things go wrong in this organelle, many diseases ranging from neurodegeneration to cancer can result,” says Birsoy. “We discovered a glutathione regulator in the ER that likely plays a key role in these conditions.”

That regulator, they learned, acts as a crucial proofreader, ensuring proteins in the ER are folded correctly.

Striking the right balance

Birsoy’s team discovered a few years ago that if glutathione levels aren’t precisely maintained in mitochondria, all systems fail. Among those team members were co-first authors Shanshan Liu, a postdoc in the lab who has long researched mitochondrial metabolism, and Mark Gad, a Ph.D student jointly supervised by Birsoy and Richard Hite, of Memorial Sloan Kettering Cancer Center.

On the heels of their initial findings, the group began to wonder about glutathione’s impact in the ER, which works with the mitochondria to keep the cell in a state of homeostasis.

Based on previous work, the team knew that glutathione contributes to maintaining the tightly regulated, Goldilocks-like environment of the ER, where secretory and membrane proteins manufactured by ribosomes are folded for export. These proteins are then exported into the cytosol (the jelly-like fluid that fills the cell) and then move further afield to complete their assigned tasks.

Unlike in the mitochondria—where the ratio between different forms of glutathione favors the unoxidized version—the ER prefers an oxidized environment. So, working with Hite’s lab, the team set out to discover not just why that is, but also what mechanisms calibrate the optimal ratio.

Quality control

After developing a new method to rapidly profile the chemical landscape within the ER, Liu began to directly observe functions within the organelle. She discovered that the ER maintains its oxidized equilibrium by importing from the cytosol an oxidized form of glutathione called GSSG and exporting a reduced form called GSH. The ER maintains its balance by keeping a high ratio of GSSG to GSH.A genetic screening revealed that a transporter called SLC33A1 oversees this process. Structural studies performed by Gad in collaboration with the Hite lab further confirmed that SLC33A1 protein indeed transports GSSG and revealed biochemical details of this process.

“Before this work, we knew the ER needed to stay oxidized to fold proteins correctly, but the machinery responsible for maintaining that balance was essentially a black box,” says Gad.

“We discovered that the correct glutathione ratio is essential to a proofreading step in protein folding. It may even be its primary job,” Liu says. “So if something goes wrong and the GSSG accumulates, it inhibits an enzyme that relies on the correct oxidation of the ER environment to operate a protein quality control system.”

Moreover, they discovered, when misfolded proteins don’t pass quality control, they won’t get exported, so they too pile up in the ER. Eventually this excess debris can lead to cell death.

“Identifying SLC33A1 as the key exporter—and being able to visualize exactly how it binds its cargo—gives us a handle on a process that, when it goes wrong, is linked to neurodegeneration and cancer,” says Gad.

Neurodevelopmental disorders and cancer

To that point, the researchers also identified glutathione-linked molecular mechanisms that may contribute to very different diseases. The first is Huppke-Brendel Syndrome, a severe neurodevelopmental disorder characterized by severe intellectual disability, motor deficits, and progressive neurodegeneration. Until now, researchers knew it was linked to mutations in the gene that produces the SLC33A1 transporter but little else.

“Our findings raise the possibility that the dysfunction of this gene alters the delicate glutathione balance in the ER and leads to protein misfolding during brain development,” Liu says. “We think this could lead to new interventions, such as reducing the glutathione overload through synthesis inhibitors or compounds that can dissipate it.”The findings also have implications for potential therapies for lung cancers related to mutations in the KEAP1 gene.

“These cancer cells rely on a high level of glutathione synthesis,” she adds. “So if we were to inhibit the SLC33A1 transporter, the GSSG would accumulate, and the cancer cells would die.”

“Our work demonstrates that defining how nutrients and metabolites are transported across cellular and organelle membranes reveals fundamental principles of cell biology while uncovering a major class of disease-relevant and therapeutically tractable proteins,” Birsoy says. “We will continue to illuminate this largely uncharted area in future work.”  

Key Questions Answered:

Q: Why does it matter if a protein is “misfolded”?

A: A protein’s shape determines its function. A misfolded protein is like a key with the wrong teeth, it won’t open the door, and it gets stuck in the lock. When thousands of these “stuck keys” pile up in the ER, the cell eventually dies.

Q: Could this lead to a treatment for Alzheimer’s?

A: While this study focused on Huppke-Brendel Syndrome, many neurodegenerative diseases (like Alzheimer’s and Parkinson’s) are characterized by misfolded proteins. Understanding how to fix the ER’s “proofreading” system could eventually help us clear those toxic protein clumps.

Q: How does this help fight cancer?

A: Cancer cells are “addicted” to glutathione to survive their own rapid growth. By blocking the SLC33A1 transporter, we can disrupt their internal chemistry, causing an “overload” of oxidized glutathione that triggers the cancer cell to self-destruct.

Editorial Notes:

• This article was edited by a Neuroscience News editor.
• Journal paper reviewed in full.
• Additional context added by our staff.About this genetics and neuroscience research news

Author: Katie Fenz
Source: Rockefeller University
Contact: Katie Fenz – Rockefeller University
Image: The image is credited to Neuroscience News

Original Research: Closed access.
“SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis” by Shanshan Liu  (刘珊珊), Mark Gad, Caifan Li  (李采蘩), Kevin Cho, Yuyang Liu  (刘雨洋), Khando Wangdu, Viktor Belay, Alon Millet, Hiroyuki Kojima, Henry Sanford, Michele Wölk, Linas Urnavicius, Maria Fedorova, Gary J. Patti, Ekaterina V. Vinogradova, Richard K. Hite & Kıvanç Birsoy. 
Nature Cell Biology
DOI:10.1038/s41556-026-01922-y

Glutathione in Brain: Overview of Its Conformations, Functions, Biochemical Characteristics, Quantitation and Potential Therapeutic Role in Brain Disorders

You just might want your doctor and hospital to contact researchers to follow this up with human testing for the improvement of cognitive decline possibility. Up to you, YOUR HOSPITAL WILL DO NOTHING WITHOUT YOUR PRODDING. 

Glutathione in Brain: Overview of Its Conformations, Functions, Biochemical Characteristics, Quantitation and Potential Therapeutic Role in Brain Disorders

Dwivedi D¹,

Megha K¹,

Mishra R¹,

Mandal PK¹

Author information

Neurochemical Research, 14 Apr 2020,
DOI: 10.1007/s11064-020-03030-1 PMID: 32297027 

Review

Abstract 

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Glutathione (GSH) is an important antioxidant found abundantly and synthesized intracellularly in the cytosol in a tightly regulated fashion. It has diverse physiological functions, including protection against reactive oxygen species and nitrogen species, antioxidant defense as well as maintenance of cellular thiol status. The human brain due to the high oxygen consumption is extremely susceptible to the generation of reactive oxygen species. GSH plays a paramount role in brain antioxidant defense, maintaining redox homeostasis. The depletion of brain GSH has also been observed from both autopsies as well as in vivo MRS studies with aging and varied neurological disorders (Alzheimer's disease, Parkinson's disease, etc.). Therefore, GSH enrichment using supplementation is a promising avenue in the therapeutic development for these neurological disorders. This review will enrich the information on the importance of GSH synthesis, metabolism, functions, compartmentation and inter-organ transport, structural conformations and its quantitation via different techniques. The transportation of GSH in the brain via different interventional routes and its potential role in the development of therapeutic strategies for various brain disorders is also addressed. Very recent study found significant improvement of behavioral deficits including cognitive decline, depressive-like behaviors, in APP (NL-G-F/NL-G-FG-) mice due to oral GSH administration. This animal model study put an emergent need to complete GSH supplementation trial in MCI and AD patients for cognitive improvement as proposed earlier.

Repression of adenosine triphosphate binding cassette transporter ABCG2 by estrogen increases intracellular glutathione in brain endothelial cells following ischemic reperfusion injury

Over my head but it talks about neuroprotection against ischemic injury, so go ask your doctor whom she is following up with to get this tested in humans.
https://www.sciencedirect.com/science/article/pii/S0197458018300642

• Jin A. Shin^{a, 1},
• Sae Im Jeong^{b, 1},
• Hye Won Kim^a,
• Gyeonghui Jang^a,
• Dong-Ryeol Ryu^c,
• Young-Ho Ahn^d,
• Ji Ha Choi^a,
• Youn-Hee Choi^e,
• Eun-Mi Park^{a, ,}

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https://doi.org/10.1016/j.neurobiolaging.2018.02.020

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Highlights

•

Estrogen decreased basal protein level of ABCG2 in the brain of OVX mice.

•

Estrogen prevented ischemia-induced brain ABCG2 level in OVX mice.

•

ABCG2 siRNA transfection reduced OGD-induced injury in bEnd.3 cells.

•

Estrogen enhanced survival in bEnd.3 cells transfected with ABCG2 siRNA against OGD.

•

ABCG2 inhibition increased intracellular glutathione in bEnd.3 cells exposed to OGD.

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Abstract

The adenosine triphosphate-binding cassette efflux transporter ABCG2 which is located in the blood-brain barrier limits the entry of endogenous compounds and xenobiotics into the brain, and its expression and activity are regulated by estrogen. This study was aimed to define the role of ABCG2 in estrogen-mediated neuroprotection against ischemic injury. ABCG2 protein levels before and after ischemic stroke were increased in the brain of female mice by ovariectomy, which were reversed by estrogen replacement. In brain endothelial cell line bEnd.3, estrogen reduced the basal ABCG2 protein level and efflux activity, and protected cells from ischemic injury without inducing ABCG2 expression. When bEnd.3 cells were transfected with ABCG2 small interfering RNA (siRNA), ischemia-induced cell death was reduced, and the intracellular concentration of glutathione, an antioxidant that is transported by ABCG2, was increased. In addition, after ischemic stroke in ovariectomized mice, estrogen prevented the reduction of intracellular glutathione level in brain microvessels. These data suggested that the suppression of ABCG2 by estrogen is involved in neuroprotection against ischemic injury by increasing intracellular glutathione, and that the modulation of ABCG2 activity offers a therapeutic target for brain diseases in estrogen-deficient aged women.

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Graphical abstract

Keywords

• ABCG2;
• brain endothelial cell;
• estrogen;
• glutathione;
• ischemic stroke;
• neuroprotection

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1. All authors disclose that there are no actual or potential conflicts of interest.

2. This study was supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIP) (2010-0011353 and 2014R1A2A1A11051461).

3. The data contained in the manuscript being submitted have not been previously published, have not been submitted elsewhere and will not be submitted elsewhere while under consideration at Neurobiology of Aging.

4. Animal experiments in the present paper comply with the NIH and Ewha Womans University guidelines for Laboratory Animals Care and Use, and the study was approved by the Institutional Animal Care and Use Committee of the Medical School of Ewha Womans University.

5. All authors have reviewed the contents of the manuscript being submitted, approve of its contents and validate the accuracy of the data.

Corresponding author: Eun-Mi Park, Department of Pharmacology, Tissue Injury Defense Research Center, College of Medicine, Ewha Womans University, 1071 Anyangcheon-ro, Yangcheon-gu, Seoul, 07985, Republic of Korea, Tel.: 82-2-2650-5743, Fax: 82-2-2653-8891.

Mushrooms are full of antioxidants that may have antiaging potential

Weasel words being used, so followup is needed. I'd prefer the magic mushrooms. You get two for one that way. Of course you'll never get magic mushrooms prescribed from your doctor.

How Magic Mushrooms Affect Your Brain: From Higher Levels Of Awareness To Hallucinations   March 2015

Mushrooms are full of antioxidants that may have antiaging potential

Pennsylvania State University Health and Medicine News

November 10, 2017

Mushrooms may contain unusually high amounts of two antioxidants that some scientists suggest could help fight aging and bolster health, according to a team of Penn State researchers.

In a study, researchers found that mushrooms have high amounts of the ergothioneine and glutathione, both important antioxidants, said Robert Beelman, professor emeritus of food science and director of the Penn State Center for Plant and Mushroom Products for Health. He added that the researchers also found that the amounts the two compounds varied greatly between mushroom species.

"What we found is that, without a doubt, mushrooms are highest dietary source of these two antioxidants taken together, and that some types are really packed with both of them," said Beelman.

Beelman said that when the body uses food to produce energy, it also causes oxidative stress because some free radicals are produced. Free radicals are oxygen atoms with unpaired electrons that cause damage to cells, proteins and even DNA as these highly reactive atoms travel through the body seeking to pair up with other electrons.

Replenishing antioxidants in the body, then, may help protect against this oxidative stress.

"There's a theory—the free radical theory of aging—that's been around for a long time that says when we oxidize our food to produce energy there's a number of free radicals that are produced that are side products of that action and many of these are quite toxic," said Beelman. "The body has mechanisms to control most of them, including ergothioneine and glutathione, but eventually enough accrue to cause damage, which has been associated with many of the diseases of aging, like cancer, coronary heart disease and Alzheimer's."

According to the researchers, who report their findings in a recent issue of the journal Food Chemistry, the amounts of ergothioneine and glutathione in mushrooms vary by species with the porcini species, a wild variety, containing the highest amount of the two compounds among the 13 species tested.

"We found that the porcini has the highest, by far, of any we tested," said Beelman. "This species is really popular in Italy where searching for it has become a national pastime."

The more common mushroom types, like the white button, had less of the antioxidants, but had higher amounts than most other foods, Beelman said.

The amount of ergothioneine and glutathione also appear to be correlated in mushrooms, the researchers said. Mushrooms that are high in glutathione are also high in ergothioneine, for example.

Cooking mushrooms does not seem to significantly affect the compounds, Beelman said.

"Ergothioneine are very heat stable," said Beelman.

Beelman said that future research may look at any role that ergothioneine and glutathione have in decreasing the likelihood of neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease.

"It's preliminary, but you can see that countries that have more ergothioneine in their diets, countries like France and Italy, also have lower incidences of neurodegenerative diseases, while people in countries like the United States, which has low amounts of ergothioneine in the diet, have a higher probability of diseases like Parkinson's Disease and Alzheimer's," said Beelman. "Now, whether that's just a correlation or causative, we don't know. But, it's something to look into, especially because the difference between the countries with low rates of neurodegenerative diseases is about 3 milligrams per day, which is about five button mushrooms each day."

Read the full article on Pennsylvania State University Health and Medicine News.

The Effect of 3′,4′-Dihydroxyflavonol on Lipid Peroxidation in Rats with Cerebral Ischemia Reperfusion Injury

Followup research needed in humans, but unlikely to occur for decades if ever.
http://link.springer.com/article/10.1007/s11064-016-1889-x

• Merve Caliskan
• , Rasim Mogulkoc 
• , Abdulkerim Kasim Baltaci
• , Esma Menevse

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Abstract

The aim of present study was to determine the effect of 3′,4′-dihydroxyflavonol (DiOHF) on lipid peroxidation in experimental brain ischemia–reperfusion in rats. Present study was performed on the 34 male Wistar-albino rats, weigth 350-400 g. Experiment groups were designed as 1-Sham; 2-Ischemia–reperfusion; animal were anesthesized and carotid arteried were clemped for 20 min and reperfusion (7 days). 3-DiOHF + Ischemia–reperfusion; DiOHF was given to animals as 10 mg/kg by intraperitoneal. 4- Ischemia + DiOHF + Reperfusion; 5- Ischemia–reperfusion + DiOHF. Blood samples and serebral cortex were analysed for malondyaldehyde (MDA), NO (nitric oxide), xanthine oxidase (XO), glutathione (GSH) and glutathione peroxidase (GPx). Blood MDA levels were significantly higher ischemia–reperfusion groups (P < 0.005). However, DiOHF inhibited MDA. Ischemia–reperfusion led to increased XO and NO but DiOHF supplementation reduced NO and XO. DiOHF increased GSH and GPx levels compared to ischemia–reperfusion group. All together, our present study showed that intraperitoneal DiOHF supplementation has protective effect on brain ischaemia–reperfusion injury in rat.

Milk, not just for your bones, for your brain - glutathione

An earlier post had reactive oxygen species(ROS) scavenger, glutathione as a good item to have.So you'll have to see if your doctor will add dairy to your post-stroke diet protocol.
A Lunatic Laboratories post here:

Milk, not just for your bones, for your brain

The research it is based upon here:

Dairy intake is associated with brain glutathione concentration in older adults

Transcranial amelioration of inflammation and cell death after brain injury

Would the same compound - ROS scavenger, glutathione - help in hyperacute stroke recovery? No one is going to look into this because we have crap for stroke associations. At least under current leadership.  Why don't the boards of directors do something about that?
http://www.nature.com/nature/journal/vaop/ncurrent/full/nature12808.html

• Theodore L. Roth,
• Debasis Nayak,
• Tatjana Atanasijevic,
• Alan P. Koretsky,
• Lawrence L. Latour
• & Dorian B. McGavern

• Affiliations
• Contributions
• Corresponding author

Nature

(2013)

doi:10.1038/nature12808

Received

27 April 2013

Accepted

21 October 2013

Published online

08 December 2013

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Traumatic brain injury (TBI) is increasingly appreciated to be highly prevalent and deleterious to neurological function^{1, 2}. At present, no effective treatment options are available, and little is known about the complex cellular response to TBI during its acute phase. To gain insights into TBI pathogenesis, we developed a novel murine closed-skull brain injury model that mirrors some pathological features associated with mild TBI in humans and used long-term intravital microscopy to study the dynamics of the injury response from its inception. Here we demonstrate that acute brain injury induces vascular damage, meningeal cell death, and the generation of reactive oxygen species (ROS) that ultimately breach the glial limitans and promote spread of the injury into the parenchyma. In response, the brain elicits a neuroprotective, purinergic-receptor-dependent inflammatory response characterized by meningeal neutrophil swarming and microglial reconstitution of the damaged glial limitans. We also show that the skull bone is permeable to small-molecular-weight compounds, and use this delivery route to modulate inflammation and therapeutically ameliorate brain injury through transcranial administration of the ROS scavenger, glutathione. Our results shed light on the acute cellular response to TBI and provide a means to locally deliver therapeutic compounds to the site of injury.