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Rebuilding the gut lining

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CausticSymmetry
scottyc33
Paradox
LittleFighter
hair grower
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Rebuilding the gut lining Empty Rebuilding the gut lining

Post  hair grower Tue Dec 01, 2009 10:29 am

Hey guys

I'm about to embark on a program to rebuild and strengthen the gut lining. My plan is to rotate some of the probiotic strains that LittleFighter has recommended, mainly the s. boulardii, plantarum 299v and the LGG. Another foundation could be the higher doses of L-Glutamine. I'm also thinking of these products:

Butyr-aid, http://www.iherb.com/Allergy-Research-Group-Nutricology-ButyrAid-100-Tablets/8510?at=0

PepZinGl, http://www.iherb.com/PepZinGl-120-Veggie-Caps/2467?at=0

Anyone have any experience with these two? And for the experienced posters here, do you know of any other products that would be of benefit to heal the gut lining?

I'm also going to fight candida and dysbiosis using Waiora NCD, garlic, different natural yeast killers (such as oregano oil, GSE etc.), maybe some mms when off the Waiora zeolites and, off course, anticandida diet.

Thanks!

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Post  LittleFighter Tue Dec 01, 2009 11:33 am

hair grower,

I have tested both. Pepzin GI is probably mostly helpful for ulcers in the stomach, I think the dose isn't enough to reverse leaky gut. I used butyraid, but caused me die-off and mild diarreah if I took it on an emtpy stomach. With my current progress I might be able to tolerate it... I still have a full bottle of it. BTW probiotics themselves, produce butyrate and other useful fatty acids when they ferment different carb's.

Things I currenlty use and help the most:

- A few grams of Glutamine 10-20 gms a day in divided doses, on an empty stomach (helps rebuild tissue and with SIgA); Glutamine can heal stomach ulcers by itself in a couple of weeks
- Whey protein (Jarrow's is good)
- LGG, L. P. 299v, boulardii
- Anti-fungals (seek a formula that provides oregano, garlic, berberine, etc.); oregano is the most powerful of all of them, try to take them away from probiotics
- Digestive enzymes (plant-based), betaine hcl + pepsin, with each meal; this way you can reduce fermentation, undigested matter, bad bacteria and more.

Other things to add is magnesium glycinate (take enough, 600 mg at least), l-optizinc (30 mg or more), omega-3's (EPA/DHA), Vitamin A (helps with SIgA and tissue regeneration). A natural source of nutrients like Brewer's Yeast will certainly help too.

I would also recommend you to drop wheat and casein, at least for a while.

Remember this, because it is crusial: Keep the healing process for a few months; it is very common to make the mistake of dropping the treatment because IT TAKES TIME TO HEAL COMPLETELY and sometimes to see progress. For the first time in my life, I'm sticking with the treatment and I'm seeing TRUE improvements!
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Post  Paradox Tue Dec 01, 2009 1:15 pm

Little Fighter,

Are you trying to avoid glutamate? I ask because there is a lot of glutamic acid in protein powders. I stopped taking my whey for this reason. I'm hyper-sensitive to glutamate right now as I'm tapering off medication. Do you take anything to balance glutamate/gaba. metagenics has a product called Trancor I was using with b6, mag, NAC, green tea cachethins (spelling?), and taurine. It was expensive so I just bought some NOW p-5-p with mag and b2 to try for a replacement.

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Post  Paradox Tue Dec 01, 2009 1:17 pm

BTW I'm not taking brewers yeast for the same reason. I wish I could take both for more energy and muscle mass from working out.

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Post  scottyc33 Tue Dec 01, 2009 2:09 pm

Littlefighter,

I bought some Saccharomyces Boulardii and LGG at your recommendation.

My question is should I take one before the other? Should I take both at the same time?
Does it matter?

Thanks.

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Post  Paradox Tue Dec 01, 2009 4:17 pm

Scottyc33,

I don't mean to speak for LF but I am doing the same protocol from this article that he posted here: http://www.nutricology.com/Oct-2009-In-Focus-Newsletter-Probiotics-Can-Shift-Mood-sp-97.html

To answer your question....In the article the protocol is to use the S.B. first for a couple months to raise SiGa levels enough to introduce other bacteria. After the S.B., is when the LGG is taken. It's a great article, but I believe LF said he is taking S.B. and LGG at the same time from what I can remember. I'll let him speak on that.

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Post  CausticSymmetry Tue Dec 01, 2009 4:33 pm

I'm not so sure that some varieties of brewer's yeast are a risk, such as Now Brand, as it doesn't appear to contain any free-form amino acids. Because the barley is fermented to me it would minimize the risk--of course I could be wrong but just saying.

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Post  Paradox Tue Dec 01, 2009 5:32 pm

That's interesting CS. So you are saying that it's not as simple as just reading the label for glutamic acid content? I'll have to take a look at the Lewis Labs BY I have. I was taking it for a while until I picked up on the glutamic acid being like 2 plus grams. My Doctor took me off glutamine because it can convert to glutamate so I figured if I was going to that extreme I might as well toss the brewer's yeast as well. She recommended N-A-G as an alternative to glutamine BTW, and I've been taking that for gut health. I didn't know N-A-G was a precursor to Hyaluronic acid, but it says so on the bottle. Talk about tangents...sorry

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Post  kijumn Tue Dec 01, 2009 6:34 pm

I don't mean to answer for CS but Brewers Yeast should be one of the very last food sources to be removed regarding "free" glutamic acid. The reason being the B vitamin such as B6, B12, niacin, etc is "very" helpful. If you're worried about oxalates in the beets from Lewis Labs taking a food that contains calcium you should be fine.
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Post  CausticSymmetry Tue Dec 01, 2009 8:12 pm

JHarsh80 - Interesting, I was just looking at Lewis Labs and see that they list all those amino acids. However, it is unlikely that they are in free-form, so as a complete protein it should be safe.

If you look at Now brand, there's no mentioned of the amino acids at all, but they are certainly there, just as complete protein, not fractionated.

In any case both use just brewer's yeast as the only ingredient.

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Post  Paradox Wed Dec 02, 2009 7:22 am

jdp710 wrote:I don't mean to answer for CS but Brewers Yeast should be one of the very last food sources to be removed regarding "free" glutamic acid. The reason being the B vitamin such as B6, B12, niacin, etc is "very" helpful. If you're worried about oxalates in the beets from Lewis Labs taking a food that contains calcium you should be fine.

I honestly am not familiar with oxalates, but I do take NOW's 'Adam' men's multivitamin so I am getting synthetic b's. Some are the methylated form like b12, and b6. I just ordered some more p-5-p (b6) to take later in the day. I am coming off psych meds and trying to limit anything that is going to create an excitatory response, i.e. glutamate. I have a feeling that some b's don't get along well with me in that regard while others do. It seems I almost feel more relaxed when I don't take the multi. That may not entirely be from the b's but other things in it like choline maybe?

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Post  Paradox Wed Dec 02, 2009 7:30 am

CS,

I noticed that as well. I admit that I'm not really sure why a complete protein with a certain level of glutamic acid would be less 'bad' than free form amino acids? If that is the case, would I be ok to take the 100% whey isolate again without risking any unwanted psychological effects as a result?

I read recently that the glutamic acid is a result from anything that has been hydrolyzed and that is why it is found in protein powders. It was on a web site for some special protein made from peas and rice I believe. I didn't bookmark it. I'd like to go back on the whey and the BY, but I don't want to risk a 'reaction' or increase my benzo withdrawal symptoms by doing so. I don't feel like my understanding of this subject is close to 100% so I'm hesitant to risk it.

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Post  CausticSymmetry Wed Dec 02, 2009 7:56 am

JHarsh80 - Check out Jarrow Brand, you'll see why:

http://www.iherb.com/Whey-Protein-Unflavored-2-lbs-908-g/343?at=0

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Post  kijumn Wed Dec 02, 2009 8:10 am

JHarsh80,

Here is a quote from Battling the "MSG Myth." I'd highly recommend this book if you are in fact MSG/free glutamic acid sensitive

"Whey - When cheese is produced, milk is treated with enzymes and heated to separate the curds from the whey, which is a liquid high in protein. Some glutamate may be freed up by the heat and enzyme activity, but when whey is further processed and then dried to a powder, it will contain more concentrations of free glutamate. It is then bagged and sold as a food product to be used in the manufacture of many products such as ice cream, crackers, boxed macaroni and cheese, and candy. The more whey is processed, such as in whey protein or whey protein isolate, the more glutamate it will likely contain. Sometimes hydrolyzed milk solids are added, making it even higher in glutamate. When a label says "whey", it may contain any of the whey products. Dry whey or dry milk solids are added to low fat milk to give it more creaminess. Since milk is naturally high in glutamate, many severely sensitive individuals avoid or go easy on all dairy products."

... when "milk" appears on the label, it means dry milk."
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Post  Paradox Wed Dec 02, 2009 11:42 am

CausticSymmetry wrote:JHarsh80 - Check out Jarrow Brand, you'll see why:

http://www.iherb.com/Whey-Protein-Unflavored-2-lbs-908-g/343?at=0

CS, I read the description and it states that hydrolyzation decreases glutamine content. This makes it more confusing to me because I still don't understand why that is significant considering that glutamine can be metabolized to glutamate and vice-versa. I'm still confused as to why glutamic acid in complete protein is different than in non-complete. This is from wikipedia on glutamate-glutamine cycle:

In biochemistry, the glutamate-glutamine cycle is a sequence of events by which an adequate supply of the neurotransmitter glutamate is maintained in the central nervous system.[1]

Initially, glial cells release glutamine, which is then taken up into presynaptic terminals and metabolized into glutamate by glutaminase (a mitochondrial enzyme). Glutamate can also be produced by transamination of 2-oxoglutarate, an intermediate in the Citric acid cycle.[1]

The glutamate that is synthesized in the presynaptic terminal is packaged into synaptic vesicles by the transporter VGLUT. Once the vesicle is released, glutamate is removed from the synaptic cleft by excitatory amino acid transporters (EAATs), of which there are five types. Glutamate taken up by glial cells is then converted into glutamine by glutamine synthetase, and transported out of the cells into the nerve terminal. This allows synaptic terminals and glial cells to work together in order to maintain a proper supply of glutamate.[1]

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Post  Paradox Wed Dec 02, 2009 11:52 am

Jdp710,

Thanks for that info, I appreciate it. It is hard for me to tell how glutamate sensitive I am because I am tapering off a benzodiazepine which acts on the gabanergic pathway. From what I have read, when you come off benzodiazepines glutamate can increase the withdrawal effects. It goes into detail about the NMDA receptors and the science get's beyond my level a bit. I have drank whey protein for years without any drastic problems, but in this hypersensitive state I am cautious and confused about if it is 'safe' for me to consume anything with glutamine, msg, or glutamic acid on the label? Am I missing something or is there no clear answer on that. The biggest thing for me is that I would like to get back in the gym and put some muscle back on. I know that whey protein is the best post workout form, but no matter what type of protein (powder) I consume....they all have about 2 grams of glutamic acid. This is frustrating because I want to shuttle the protein to the muscle as quickly as possible and consuming say eggs after a workout when you are in that highly catabolic state and insulin is high, is not going to do it because you have to wait for digestion.

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Post  Prague Wed Dec 02, 2009 8:58 pm

JHarsh

i've always had problems putting some muscle and this is what worked for me and what could solve your problem:
the window for the anabolic effect is 30 mins to 4 (or more hours) after the workout; workout on empty stomach (no carbs before training) for HGH production and to raise IGF2 levels in the muscles - your body switches during the workout to fat utilisation as energy source - this allows you to cosnsume some slowly digestible protein/fat combination after wo, since the fat can transport the protein as (well as carns can) at this state; 2 hours later you take care of the insulin based anabolic effect by consuming complex carbs with some protein too maybe

actually the carbs (insulin) related anabolic effect you can attain whenever ater the workout, even some 12h later if you previously supply some protein/fat

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Post  Paradox Wed Dec 02, 2009 9:36 pm

Prague,

That's interesting thanks. Everything I've read has suggested the opposite- immediate carbs followed by protein afterward. When you have that post wo insulin spike is when they say to hit your muscles with immediate glucose (grape juice for instance). Then to follow that with whey protein about 20min later. I'll experiment a bit with that. It is seeming like traditional body building ways aren't too healthy...i.e. consuming straight sugar. Although they argue that because your insulin is high you can utilize it. They say that morning (fasting) and post workout are the only two times that you can safely consume straight glucose because you;re in a catabolic state with high insulin. In fact they recommend sugar first thing in the morning to end that catabolic muscle wasting state asap and preserve muscle mass. The idea is stopping gluconeogenesis. (hope I'm using that word correctly. Physiology has been a while).

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Post  hair grower Fri Dec 04, 2009 6:26 pm

Now this is really interesting. For years I've had this unexplained pain in the area around my ribs and heart accompanied by a feeling of tightness in the chest. In the last few days I've stopped taking the gelatin caps and yesterday my heart was pain free - up until today when I ate ready made sushi and the pain slowly returned. I had great clarity of mind yesterday as well. I think this warrants going on the elimination diet that jdp suggests.

jdp: I remember seeing you recommend bromelain for gluten sensitivity. Was that just when actually eating gluten or could it be beneficial even on a gluten free diet?

LittleFighter: Thanks for your input. I'm going to do the probiotics you suggested, LGG, L. P. 299v, boulardii. Do you keep to the suggested doses or have you gone higher? Maybe it would make sense to double the dose of boulardii at least in the beginning in order to boost siga levels. Concerning magnesium, I'm using trandermal oil but can't always use it so a supplement makes when I don't use the oil. The glycinate seems pretty pricey, though, so I was thinking of going with some citrate instead. Additionally I'll do antifungals and Waiora's NCD.

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Post  hair grower Fri Dec 04, 2009 8:49 pm

hey jdp, I found this quote about msg from ted at earthclinic:
"The possible antidote for MSG toxicity is simple: take plenty of protein, especially L-glutamine, which would displace the free glutamate from the body."

Have you personally tried l-glutamine since you embarked on your msg free diet and if so, did you get a reaction?

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Post  LittleFighter Sat Dec 05, 2009 3:26 am

scottyc33 wrote:Littlefighter,

I bought some Saccharomyces Boulardii and LGG at your recommendation.

My question is should I take one before the other? Should I take both at the same time?
Does it matter?

Thanks.

I think it doesn't matter how you take them. Each one of them has a different key purpose.

Michael Ash (or anything I could find) doesn't mention anything about a bad interaction between the two of them (like when taking them together). Nevertheless, I take 1 S. Boulardii in the morning and another one in the night. I take LGG usually in the afternoon. I think this way I "maxmize" the action of each one of them, but this is just a personal belief.

I also take antifungals, usually very early in the morning to avoid the hindering the viability of S. Boulardii... So far so good!
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Post  kijumn Sat Dec 05, 2009 6:53 am

Hey hairgrower,

I looked everywhere for that ebook that I posted previously about bromelain helping with small quantities of gluten but I couldn't find it. In short, what the book mentioned what I believe was one case where the patient eliminated 100% gluten for one year and after one year was able to handle small amounts of gluten when taking bromelain. I personally believe it but I believe the important part is to make sure that gluten, etc. would need to be eliminated from the diet for a year. Probably the better enzyme to take instead of bromelain for gluten would be one that contains DPP IV such as this

http://www.iherb.com/Now-Foods-Gluten-Digest-60-Vcaps/12364?at=0

One problem with that is that a lot of supplements contain MSG. Notice maltodextrin in the above link. Small amounts are probably fine for most but MSG can add up. Also, keep in mind that while MSG is techinically not an allergy but when consuming MSG with a food you're sensitive it dramatically increases the reaction you'll get from that sensitive food. Also, MSG's effect on thyroid, glutathione, etc.... the list is very long.


As for taking enzymes in general, I very much believe in enzymes.

CausticSymmetry has previously posted a very good ebook that I tried looking for but couldn't find. It basically shows how the facial structure, teeth, etc. changes for the worse when eating modern food compared to other primitive societies that eat a primitive diet. A lot of this is probably due to the enzymes IMHO. Here is some good information that will have to do on cats instead that Gibson has posted before



"Enzyme-rich raw food diets and their positive effect on various diseased conditions in both humans and animals have been well documented throughout the world. The first major scientific paper on enzymes was published April 15, 1940, by Dr. Edward Howell, in "the Journal of the American Association for Medico-Physical Research." Dr. Howell is formally recognized as the discoverer of the vital role of enzymes in human nutrition. He pioneered more than 50 years of research and scientific experimentation with overwhelming evidence indicating that the primary cause of degenerative disease in humans is enzyme deficiencies exacerbated by enzyme deficient mothers passing on genetic deficiencies to their offspring. Numerous studies have documented that when captive or domesticated animals are fed diets similar to human diets common to industrialized nations, they develop diseases similar or identical to human beings. In the early 1930's, and over the following 25 years, Francis M. Pottinger, Jr., M.D. conducted studies on cats using two diets. One diet consisted of two-thirds raw meat, one-third raw milk and cod liver oil. The second diet consisted of two-thirds cooked meat, one-third raw milk and cod liver oil. Studies revealed the following:

Multiple generations of cats on the raw meat diet were healthy. They had adequate nasal cavities, excellent tissue tone, good fur with little shedding, and no facial deformities. The calcium and phosphorous content of their bones was consistent. Their internal organs developed and functioned normally. Throughout their lifespan they were resistant to infections, fleas and other parasites. They were free of allergies and miscarriages were rare. Litters averaged five kittens, with mothers experiencing no difficulty nursing.

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Multiple generations of cats on the cooked meat diet were not so healthy. They had many variations in facial bone and dental structure. Their long bones tended to be increased in length and smaller in diameter, showing less calcium. In the third generation, some of the bones were as soft as rubber. Other indications were heart problems, nearsightedness, farsightedness, underactivity or inflammation of the thyroid gland, infections of the kidney, liver, testes, ovaries and the bladder, arthritis and inflammation of the joints, inflammation of the nervous system with paralysis and meningitis. Infections of the bone appeared regularly, often appearing to be the cause of death. By the time the third generation was born, the cats were so physiologically bankrupt that none survived beyond the sixth month of life. Cats on the cooked meat diet were more irritable. There was evidence of role reversal, with female cats becoming the aggressors and male cats becoming docile and passive, either acting perverted or showing no interest in sex. Some females were dangerous to handle. Increasingly abnormal activities occurred between the same sexes. Vermin and intestinal parasites were rampant. Skin lesions and allergies were frequent and progressively worse from one generation to the next. Pneumonia and empyema (accumulation of pus) were principal causes of death in adults, with diarrhea, followed by pneumonia, the cause of death in kittens.

Females frequently had ovarian atrophy and uterine congestion. Males often failed to have active sperm development. Spontaneous abortion in pregnant females was about 25% in the first deficient generation, increasing to about 70% in the second generation. Deliveries were difficult, and many females died in labor. The mortality rate of kittens was high. Some mothers failed to lactate. Many failed to become pregnant, and those that did had difficulties. The average weight of kittens was 16% less than those born to mothers raised on a raw meat diet.

When cats of the cooked meat-fed first and second generation groups were returned to a raw meat diet, it took about four generations to recover a state of normal health.

Improvement in resistance to disease was noted in the second generation, with allergic manifestations persisting into the third generation. By the fourth generation, most of the severe deficiency symptoms disappeared, but seldom completely. Once a female cat was subjected to a deficient diet for a period of 12 to 18 months, her reproductive efficiency was so reduced that she was never able to give birth to normal kittens. Only when the kittens were put on an optimum diet did a gradual reversal and regeneration take place."
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Post  kijumn Sat Dec 05, 2009 6:55 am

Hair Grower,

As for your other question about glutamine, while I listen to Ted's posts a lot at earthclinic and I'm glad for the information he posts this is one post that he's wrong in. I've personally tried glutamine and actually it gives a major MSG reaction.

Here's some information

""I beleive that for the creators of that site, a little knowledge is a dangerous thing. Glutamic acid is not a conditionally needed amino acid. It is a non-essential amino acid. Everybody can make it. Easily. If they couldn't, the nervous system wouldn't function. Unfortunately ammonia crosses the blood brain barrier easily and when it does, the body - considering it toxic - turns ammonia into glutamic acid. The body then turns excess glutamic acid into glutamine, or GABA or something else. There are several ways the body gets rid of glutamic acid, but there seems to be trouble when the body can't get rid it. I believe this to some folks appears to be a "glutamine deficiency". They think supplementing with glutamine will solve the problem when the problem is that the body is having trouble getting rid of glutamic acid in the first place. Type I diabetics actually have immune systems that attack one enzyme that turns glutamic acid into GABA. I think supplementing with glutamic acid or glutamine may be trouble for what someone percieves as a "glutamine deficiency". Deficiency of any kind should ALWAYS be diagnosed by a physician. Chemical equations go both ways. If glutamate can form glutamine, glutamine can form glutamate. If there was no deficiency, supplementation may make the situation worse, not better."

http://www.msgmyth.com/discus/messages/10/928.html?1205432805

http://curezone.com/forums/am.asp?i=1244903&s=2

"By Russell L. Blaylock, M.D.
Advanced Nutritional Concepts, LLC.

Dr. Robert Crayhon posted comments on this site indicating that I was terribly mistaken in my caution concerning the use of glutamine and that he had consulted several "cell biologists" who were also concerned with my statements on glutamine safety. In fact it was stated that I apparently did not understand that glutamine was not an excitotoxin and was not converted into an excitotoxin.

Of course, I never stated glutamine was an excitotoxin, but I do state that it is converted into the excitotoxin glutamate within neurons. Numerous recent studies as well as Siegel’s Basic Neurochemistry textbook emphatically state that the major source of glutamate is from glutamine in the brain. Normally, when the brain finishes using glutamate for chemical communication between brain cells at the synapse the glutamate is taken up by surrounding glial cells and changed by the enzyme glutamine synthease into glutamine, where it is stored.

The Problem With Excitotoxins

The glutamine is then transported to the neuron and by the enzyme glutaminase, it is converted to glutamate--the potential excitotoxin. I say potential because unless it accumulates outside the brain cell it is harmless.

This is the major source of glutamate within the brain. Excitotoxins are usually amino acids, such as glutamate and aspartate. These special amino acids cause particular brain cells to become excessively excited, to the point they will quickly die. Excitotoxins can also cause a loss of brain synapses and connecting fibers. Food-borne excitotoxins include such additives as MSG, aspartame, hydrolyzed protein and soy protein extract.

In two recent studies it was found that the amount of glutamine in the brain could predict the brain damage seen both in pediatric brain injuries and brain damage secondary to seizures. Adding large amounts of glutamine to the diet increases significantly brain levels of glutamine and, hence, glutamate. Another study found that by adding glutamine to the diet of animals exposed to another powerful excitotoxin called quinolinic acid, brain cell damage was increased significantly. Quinolinic acid is known to accumulate in the brain in most cases of viral brain infection as seen with HIV dementia and viral encephalitis.

Glutamine and Liver Toxicity

Individuals with liver toxicity tend to accumulate ammonia in their blood and brain. Until recently, it was assumed that it was the ammonia that caused liver disease-associated brain injury and that glutamine was protective.

Newer studies indicate that actually it is the glutamine that is causing the brain’s injury. Increasing glutamine in the diet would significantly aggravate this damage.

Free Radicals in the Brain

Glutamine accumulation has also been found in Alzheimer’s disease, Huntington’s disease and high levels of brain glutamine have been associated with a worse prognosis in Lou Gehrig’s disease. Likewise, recent studies have shown that high brain glutamine levels increase brain levels of free radicals and impair the ability of brain mitochondria to produce energy. When the brain produces low energy, excitotoxins, such as glutamate, become even more toxic. It has been shown that the reason for glutamine toxicity under these conditions is because it is converted to the excitotoxin--glutamate.

Glutamine and Multiple Sclerosis

Of particular concern is the finding that people with multiple sclerosis have increased levels of the enzyme glutaminase (the enzyme that converts glutamine into glutamate) in areas of nerve fiber damage. High levels of glutamine in the diet would increase glutamate levels near these injured areas magnifying the damage. It has been shown that excitotoxicity plays a major role in multiple sclerosis by destroying the cells (oligodendrocytes) that produce myelin.

Glutamine and Pregnant Women

Another area of concern would be pregnant women. Glutamine passes through the placenta and may actually be concentrated in the baby’s blood, producing very high levels. Glutamate plays a major role in the development of the baby’s brain. Excess glutamate has been shown to cause significant impairment of brain development in babies and can lead to mental retardation.

When to Use Glutamine

The major use for high-dose glutamine would be to repair gastrointestinal injury. In such cases, I would recommend short-term use only. Those with a history of the following conditions should avoid glutamine, even for short-term use:

* Stroke
* Neurodegenerative disease
* Pregnancy
* Malignancy
* Recent vaccinations
* ADHD
* Hypoglycemia
* Autism
* Multiple sclerosis
* Other neurological disorders

Glutamine has recently been shown to produce extreme hypoglycemia, even more so than leucine, which is known to produce fatal hypoglycemia in infants.

The reason Chinese Restaurant Syndrome is not seen with glutamine challenge is that the glutamate receptors in the lungs and esophagus are stimulated by glutamate, not glutamine. The glutamine must be converted first and this occurs primarily in the brain.

The only safe situation for glutamine use is in the vigorous athlete. Glutamine is used as a muscle fuel, so that vigorous exercise will consume most of the glutamine before it can accumulate in the brain. I would still avoid long-term use in high doses. I would caution readers to avoid excess glutamine, especially in the above named conditions and situations"

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kijumn
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Post  Whip Sat Dec 05, 2009 8:11 am

Won't arginine get rid of the ammonia accumulation in the liver? What's the safest version of arginine (minimal side effects) to take Jdp? Is there anything to counter with the arginine while trying to get rid of the ammonia besides Lysine?

Thanks guys

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Post  kijumn Sat Dec 05, 2009 9:07 pm

edony posted a good study regarding anxiety levels decreasing when taking arginine and lysine previously

arginine and lysine will also increase growth hormone levels.

There was also one person who mentioned that arginine and lysine was his antidote for msg symptoms. I personally have my doubts though but I did buy some arginine and also citrulline and also already have lysine to test one day. Be careful with arginine as it may increase inflammation.
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