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Anorexia. Schitzophrenia. possession. psychic

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#31    crystal sage

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Posted 29 January 2008 - 08:58 PM



Conditions associated with undermethylation: Anorexia, Bulemia, shopping/gambling disorders, depression, schizo-affective disorder, delusions, oppositional-defiant disorder, OCD.

Conditions associated with overmethylation: Anxiety/Panic disorders, anxious depression, hyperactivity, learning disabilities, low motivation, "space cadet" syndrome, paranoid schizophrenia, hallucinations. (Oct 3, 2003)

One-carbon (methyl) groups are involved in numerous important biochemical reactions in the body, including genetic expression, neurotransmitter synthesis and metabolism, etc. Methylation (more properly, the methyl/folate ratio) is a major factor in the rate-limiting step (the tetrahydrobiopterin reaction) in the synthesis of serotonin, dopamine, and norepinephrine in the brain. Undermethylated persons tend to be depleted in these 3 neurotransmitters, and the opposite is true for overmethylation.

The SAM cycle in which dietary methionine is converted to SAMe (the primary CH3 donor in the body), and then to homocysteine, is a dominant cascade of reactions in methylation and also is very important in production of glutathione, cysteine, and other aspects of sulfur chemistry.

Most persons with depression, oppositional defiant disorder, OCD, bipolar disorder, or schizophrenia exhibit a genetic abnormality in methylation..... which appears to be central to their illness. Carl Pfeiffer, MD, PhD of Princeton, NJ was a pioneer in this field. (Oct 3, 2003)

About 25 years ago, Dr. Carl Pfeiffer (Princeton, NJ) identified the condition he called "histapenia" or histamine deficiency. After studying the metabolism of more than 20,000 schizophrenics he learned that this
"low histamine" syndrome was common in anxiety, panic disorders, and classical paranoid schizophrenia. His enormous biochemistry database revealed that most histapenics suffered from (1) copper overload and (2)
deficiency of folic acid and/or B-12. More importantly, he found that aggressive therapy using folic acid, B-12, and B-3 usually produced dramatic improvements in these persons. Pfeiffer thought the improvements were largely due to elevating histamine levels in the body & brain.

Subsequent research has indicated that the improvements are due to normalizing the methyl/folate ratio.

Also, a serious overload of homocysteine (homocysteinuria) can result in symptoms quite identical to paranoid schizophrenia. Folic Acid & B-12 serve to lower HCy levels.

One thing that is absolutely certain is that methionine and/or SAMe usually harm low-histamine (overmethylated persons)..... but are wonderful for high-histamine (undermethylated) persons. The reverse in true for histadelic (undermethylated) persons, who thrive on methionine, SAMe, Ca and Mg..... but get much worse if they take folates & B-12 which can increase methyl trapping.

Edited by crystal sage, 29 January 2008 - 09:02 PM.

#32    crystal sage

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Posted 29 January 2008 - 09:05 PM



Anorexia and bulimia

We have found that nearly all anorexic and/or bulemic patients are very undermethylated, low serotonin persons. Most of then respond very well, albeit slowly, to aggressive doses of methionine, Vitamin B-6, and calcium.A positive response can usually be achieved more rapidly with SAMe. In severe cases we often start with SAMe to get a quick improvement, and than gradually convery to methionine/B-6/calcium.

I certainly agree that a lousy food choices can aggravate an eating disorder, and might even trigger it in a person with a tendency for OCD and delusional thinking. An excellent dietary & nutritional program is an important component of success for these persons. (7 Jan, 2003)

In my experience, most anorexics are perfectionistic, obsessive-compulsive, high-histamine, low serotonin persons. Most have a history of high accomplishment in school and were never discipline problems. Most anorexics also have a history of being overweight, at least in their eyes. When they begin to diet, their OCD takes over and they go to great extremes. Also, when these emaciated skeletons of people look in the mirror, they tell me that all they see is FAT. It seems to involve a nasty combination of obsessive/compulsive disorder plus delusional thinking. I've never noticed a correlation with lousy diets. The anorexic I know best at present is a dedicated nutritionist/dietician..... who eats only the finest nutrient-dense whole foods. Her condition is still serious. (Jan, 2003)

I've observed that most anorexic and bulemic patients benefit greatly from a combination of biochemical therapy and counseling/psychotherapy. (30 Dec, 2002)

I've researched the biochemistry of hundreds of OCD patients, many of whom had comorbidity for schizo-affective disorder or delusional disorder. Typical characteristics for this patient population include undermethylation, weak functioning of the BH4 rate-limiting steps in synthesis of serotonin, and dopamine, low calcium levels, excessive folate levels, and high oxidative stress.  (Aug 4, 2003)

Other helpful nutrients for OCD are methionine, calcium and magnesium...... since virtually all OCD patients are undermethylated, low-serotonin persons. (Aug 8, 2003)

Inositol is especially helpful for undermethylated persons (for example most persons with OCD), but can cause negative side effects in those who are overmethylated. Since Inositol is one of the primary second messengers in neurotransmission, it's surprising is isn't more commonly used. It's especially useful in reducing anxiety and enhancing sleep.

To enhance sleep for a 160 lb person, we usually recommend 650 mg tablets, 1-3 as needed for sleep. Persons who have difficulty falling asleep should take it 30-60 minutes before sleep. Persons whose main problem is waking up in the middle of the night should take it at bedtime.

We've often given as much as 3-4 grams/day to undermethylated persons who respond beautifully to Inositol, and these persons take it morning, noon, and evening.

I once gave an invited presentation at a symposium at an APS annual meeting... in which data on megadoses (15-30 g) of Inositol were reported by another speaker. The volume of Inositol used seemed extreme to me, and would present daunting compliance problems. I believe such huge doses of Inositol are unnecessary, if methionine, calcium, B-6, and other nutrients to combat undermethylation are used. However, massive doses of Inositol might be needed if one tries to combat OCD with Inositol alone.

A word of caution --- Manganese supplements tend to aggravate Tourette's Syndrome, and can also worsen the symptoms of OCD.

Trichotillomania has been associated with OCD and undermethylation. If you can confirm the presence of undermethylation, the patient should benefit from (1) aggressive doses of l-methionine, calcium, magnesium, along with augmenting nutrients zinc, B-6, Inositol, Vitamin A & C and (2) strict avoidance of folic acid, choline, DMAE, and copper supplements

Edited by crystal sage, 29 January 2008 - 09:21 PM.

#33    crystal sage

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Posted 14 February 2008 - 03:27 AM



Basal Ganglia Contribute to Learning, but Also Certain Disorders
By Kayt Sukel
About Kayt Sukel
January 15, 2007

Move over, hippocampus. The basal ganglia, a group of interconnected brain areas located deep in the cerebral cortex, have proved to be at work in learning, the formation of good and bad habits, and some psychiatric and addictive disorders.

Scientists have found that the neurotransmitter dopamine, already linked to the basal ganglia in movement disorders, also is important in learning via reward and punishment, as well as in disorders including schizophrenia and attention-deficit/hyperactivity disorder. This new understanding of how the basal ganglia work has revealed possible avenues for treatment of these and other disorders.

Psychiatric Disorders and Addiction

The basal ganglia are involved not only with Parkinson’s disease but also an array of psychiatric and addiction disorders. Neuroimaging studies have shown abnormal activation of the striatum and other areas of the basal ganglia in patients with schizophrenia, attention-deficit/hyperactivity disorder (ADHD), Tourette’s syndrome, obsessive-compulsive disorder (OCD), and anorexia nervosa, as well as drug addiction.

O’Reilly and Frank have recently started looking at the basal ganglia in learning in patients with ADHD and OCD. Their research has shown that patients with ADHD, who generally show an overall decrease of dopamine in the basal ganglia, show not only impaired learning with positive feedback but also coordination deficits.





"There is a low blood flow in one specific part of the brain on one side. It only occurs in people with anorexia and does not occur in people without anorexia," Professor Lask said.

The part affected, called the insula, links other key parts of the brain involved in the disorder.

Anorexia is marked by intense feelings of anxiety, linked with the amygdala, restlessness and irritation (basal ganglia), obsessive thoughts (frontal lobe), visuo-spatial difficulties (parietal lobe) as well as body image (the somato-sensory cortex).

#34    crystal sage

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Posted 14 February 2008 - 03:42 AM

It has been found by exercising the Ganglia.. via balance balls.. stability balls help strengthen.. ..balance the  basal Ganglia..

Could it help these disorders???



Furthermore, training on a stability ball provides numerous benefits similar to those of Pilates, such as increased muscle tone and flexibility, improved posture, coordination and a greater sense of body awareness. The most significant difference is how the ball addresses core stabilization. Exercising on an unstable surface forces automatic recruitment of the body's core muscles to hold a position of balance. Since stabilization is a reflex action rather than a conscious effort, training on the ball is often more effective than performing similar movements on the floor.

On a neuromuscular level, the brain is focused less on which specific muscles are contracting and primarily on performing the activity without falling off the ball.

It is said to help with Autism... why not other mind/brain disorders

Edited by crystal sage, 14 February 2008 - 03:43 AM.

#35    crystal sage

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Posted 13 March 2008 - 01:46 AM



"Serum autoantibodies to brain in Landau-Kleffner variant, autism, and other neurologic disorders" (Journal of Pediatrics, vol. 134, no. 5, May 1999, pp. 607-613): "Etiologically unexplained disorders of language and social development have often been reported to improve in patients treated with immune-modulating regimens. Here we determined…children with L[andau] K[leffner] S[ydrome] V[ariant] and A[utistic] S[pectrum] D[isorder] have a greater frequency of serum antibodies to brain endothelial cells and to nuclei than children with non-neurologic illnesses or healthy children. The presence of these antibodies raises the possibility that autoimmunity plays a role in the pathogenesis of language and social developmental abnormalities in a subset of children with these disorders.

"Characteristics of antineuronal antibodies in systemic lupus erythematosus patients with and without central nervous system involvement: the role of mycobacterial cross-reacting antigens" (Israeli Journal of Medical Science, vol. 26, no. 7, July 1990, pp. 367-73): indirect immunofluorescence of human brain tissue sections revealed, in thirteen of sixteen patients, high antineuronal antibody titers. Competition assays showed that the binding of the antineuronal antibodies was blocked by mycobacterial glycolipids and bovine brain extracts.

"This finding suggests an additional link between mycobacterial infection and SLE."

"Increased prevalence of antibrain antibodies in the sera from schizophrenic patients" (Schizophrenia Research, vol. 14, no. 1, December 1994, pp. 15-22); "Antibodies to brain tissue in sera of schizophrenic patients-preliminary findings" (European Archives of Psychiatry and Clinical Neuroscience, vol. 242, no. 5, 1993, pp. 314-7): Antibrain antibodies have been found in the sera of schizophrenic patients, but not in normal controls. These seem to be directed against brain centers affected in schizophrenia.

<<behavior and movement disorders >>

"A controlled study of serum anti-locus ceruleus antibodies in REM sleep behavior disorder" (Sleep, vol. 20, no. 5, May 1997, pp. 349-51): "The newly identified association of human nonnarcoleptic rapid eye movement (REM) sleep behavior disorder (RBD) with human leukocyte antigen (HLA) DQwl class II genes raises the possibility that RBD may arise from autoimmune mechanisms."

[The following reports are not vaccine-specific; rather they serve to underline one of the possible conditions resulting from altered permeability of, or damage to the intestine, as occurs in association with measles and other viruses. Note: strep-type bacteria are among those which can translocate from the gut; these have been implicated in cases of Obsessive-Compulsive Disorder and Tourette Syndrome.] "Bacterial translocation from the gastrointestinal tract" (Trends in Microbiology, vol. 3, no. 4, April 1995, pp. 149-54): Viable indigenous bacteria from the gastrointestinal tract can migrate to other sites within the body, such as the mesenteric-lymph-node complex, liver, spleen, and bloodstream. Three mechanisms support bacterial translocation: intestinal bacterial overgrowth, deficiencies in host immune defenses and increased permeability or damage to the intestinal mucosal barrier.

#36    crystal sage

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Posted 16 March 2008 - 10:53 AM



. What it shows is that the same supplements that help one category, actually hurt another. So please be careful!



1. UNDERMETHYLATED, high histamines

GOOD: methionine, SAMe, Calcium, Magnesium, B-6, Inositol, TMG, zinc.

BAD: Folic Acid, B-12, Choline, DMAE, copper

2. OVERMETHYLATED, low histamines

GOOD: Folic Acid, B-12, DMAE, B-3

BAD: methionine, SAMe, Inositol

Notes compiled from all over his site:


UNDER METHYLATED = HIGH HISTAMINES, elevated basophils histamine ( > 70)

Conditions associated with undermethylation: Anorexia, Bulemia, shopping/gambling disorders, depression, schizo-affective disorder, delusions, oppositional-defiant disorder, OCD. most exhibit seasonal allergies, perfectionism, strong wills, slenderness, OCD tendencies, high libido, etc.

hives more undermethylated

methionine and/or SAM are wonderful for high-histamine (undermethylated) persons.

(undermethylated) persons thrive on methionine, SAMe, Ca and Mg, but get much worse if they take folates & B-12 which can increase methyl trapping. Generally, OCD patients respond nicely to methonine, SAMe, calcium, magnesium, B-6, Inositol, TMG, and zinc.

more than 40% of all clinically depressed men are undermethylated and benefit from therapies which enhance methylation.
High bloodhistamine indicates undermethylation, low serotonin levels

Most OCD patients (both obsessive thoughts AND compulsive actions) exhibit undermethylation and associated low levels of serotonin, dopamine, and norepinephrine. Choline is anti-dopaminergic and often makes OCD patients worse. Most OCD patients get worse if given supplements of DMAE, choline, copper, or folic acid.

Inositol is usually very helpful for UNDERMETHYLATED, HIGH HISTAMINE patients. This includes nearly every OCD patient we have seen. Inositol usually provides calming throughout the day and ability to settle down to sleep at night, for these patients.

Some practitioners like to tinker with the SAM cycle to promote conversion of homocysteine to methionine, but this can deplete the cystathione pathway and result in deficiencies of glutathione, cysteine, etc. Some persons have a genetic enzyme weakness which can disrupt the SAM cycle

Undermethylated adults typically require 2,000 - 3,000 mg/day of methionine for several months to see good results. Also, augmenting nutrients such as calcium, magnesium, B-6, and zinc are essential.

Personally, I believe the use of SAMe is the quickest way to help an undermethylated, high-histamine person.


Overmethylated persons generally exhibit anxiety, absence of seasonal allergies, presence of food/chemical sensitivities, dry eyes, low perspiration, artistic/music interests/abilities, intolerance to Prozac and other SSRI's, etc.

Conditions associated with overmethylation: Anxiety/Panic disorders, anxious depression, hyperactivity, learning disabilities, low motivation, "space cadet" syndrome, paranoid schizophrenia, hallucinations. (Oct 3, 2003)


?Over methylated do well on B-12 and folates?? ??

methionine and/or SAMe usually harm low-histamine (overmethylated persons)

Many anxious children are overmethylated and thrive on DMAE which passes the blood-brain barrier and enhances acetylcholine (which suppresses dopamine). Since DMAE tends to lower Dopamine, Norepinephrine, and Noradrenaline..... anxiety may be lessened and expressive language improved. Of course, DMAE is effective only for children who have a genetic tendency for elevated levels of these three neurotransmitters.

DMAE is usually indicated for children who are "space cadets" who have high anxiety, little motivation for learning, and poor organization. DMG is usually indicated for intense children who are strong willed, competitive, and exhibit obsessive/compulsive tendencies. (Oct 1, 2003)

On the other hand, OVERMETHYLATED patients usually derive little or no benefit from Inositol, and may experience very nasty side effects from it.

another 15% or so are overmethylated and need to head for the other goal line...... namely avoidance of methylating supplements and use of folate therapy.

histamine deficiency. After studying the metabolism of more than 20,000 schizophrenics he learned that this
"low histamine" syndrome was common in anxiety, panic disorders, and classical paranoid schizophrenia. His enormous biochemistry database revealed that most histapenics suffered from (1) copper overload and (2) deficiency of folic acid and/or B-12. More importantly, he found that aggressive therapy using folic acid, B-12, and B-3 (note: niacin) usually produced dramatic improvements in these persons.


Use caution if you have depression or bipolar disorder and are taking or considering taking inositol. There is a possibility that manic episodes may occur.



One of the components needed to synthesize SAMe in the body is methionine. Without adequate supplies of methionine, SAMe production falters. It is interesting to note that maintaining healthy levels of methionine depends on adequate levels of folic acid and vitamin B12. Depression has been associated with a deficiency in either of these vitamins.21,22 The implication of this is that deficiencies of vitamin B12 and folic acid lead to deficiencies of SAMe, and thus to deficiencies in crucial neurotransmitters such as dopamine, serotonin, and norepinephrine—all of which require the help of SAMe for synthesis.

#37    crystal sage

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Posted 16 March 2008 - 11:33 AM



Pellagra is a vitamin deficiency disease caused by dietary lack of niacin (B3) and protein, especially proteins containing the essential amino acid tryptophan.[1] Because tryptophan can be converted into niacin, foods with tryptophan but without niacin, such as milk, prevent pellagra. However, if dietary tryptophan is diverted into protein production, niacin deficiency may still result.

Pellagra is an endemic disease in Africa, Mexico, Indonesia and China. In modern societies, a majority of patients with clinical pellagra are poor, homeless, alcohol dependent, or psychiatic patients who refuse food.[2]

Tryptophan is an essential amino acid found in meat, poultry, fish, and eggs. If one's diet contains these foods, one's need for niacin from other sources will be reduced.[3]

The relationship between lysine and pellagra is unclear.[4]

The symptoms of pellagra include:

    * High sensitivity to sunlight
    * Aggression
    * Dermatitis, alopecia, oedema
    * Smooth, beefy red glossitis
    * Red skin lesions
    * Insomnia
    * Weakness
    * Mental confusion
    * Ataxia, paralysis of extremities, peripheral neuritis
    * Diarrhoea
    * Eventually dementia

Frostig and Spies (acc. to Cleary and Cleary) described psychological symptoms of pellagra[6]:

The elementary syndrome:

    * Psycho-sensory disturbances (impressions as being painful, annoying bright lights, odours intolerance causing nausea and vomiting, dizziness after sudden movements)

    * Psycho-motor disturbances (restlessness, tense and a desire to quarrel, increased preparedness for motor action)
    * Emotional Disturbanes
Impact on Skeletal Tissue

Gillman and Gillman related skeletal tissue and pellagra in their reseach in South African Blacks. They provide some of the best evidence for skeletal manifestations of pellagra and the reaction of bone in malnutrition. They claimed radiological studies of adult pellagrins demonstrated marked osteoporosis. A negative mineral balance in pellagrins was noted which indicated active mobilization and excretion of endogenous mineral substances, and undoubtedly impacted the turnover of bone. Extensive dental caries were present in over half of pellagra patients. In most cases caries were associated with severe gingival retraction, sepsis, exposure of cementum, and loosening of teeth. [7]
In the research conducted between 1900-1950 it was found that the cases of women with pellagra was consistently double the cases of men.[10] This is thought to be due to the inhibitory eddect of Estrogen on the conversion of the amino acid tryptophan to niacin.[11] It is also thought to be due to the differential and unequal access to quality foods within the household. Some researchers of the time gave a few explanations on the difference[12]As primary wage earners, men were given consideration and preference at the dinner table, they also had pocket money to buy food outside the household. Women gave protein quality foods to their children first. Women also would eat after everyone else had a chance to eat. Women also upheld the triad of maize, molasses and fat back pork which combine to contribute the cause of pellagra.

Abstract  Pellagra is a potentially fatal, nutritional disease with cutaneous, gastrointestinal, and neuropsychiatric manifestations. Because of the diversity of pellagra’s signs and symptoms, diagnosis is difficult without an appropriate index of suspicion. A case of pellagra in a 14-year-old girl with anorexia nervosa is presented. Signs and symptoms of pellagra were resolved after niacin therapy and dietary treatment.



My research program has focused on using animal models and chemically defined diets to study nutrition and disease problems that affect both animals and humans. In this review, I will describe and briefly discuss my own personal list of "15 vexatious questions" that have intrigued me over the course of my career as an academic scientist.

The first six questions deal with sulfur compounds and sulfur amino acids (SAA, i.e., methionine and cysteine). The role of these compounds in protein synthesis, transmethylation, synthesis of glutathione, taurine, CoA, and phosphoadenosine-5'-phosphosulfate as well as in ameliorating various inflammatory conditions have had longstanding emphasis in my laboratory. Clearly, the elegant research contributions of the late Vincent du Vigneaud (12), an Academy member and Nobel Laureate, provided great inspiration for the nutrition work on SAA done in my laboratory. Sulfur amino acid work is of great practical relevance to animal nutrition in that well over 90% of SAA production is used to fortify diets for animals, particularly poultry. Poultry diets around the world are based on corn and soybean meal, and these diets for poultry, without fortification, are deficient in SAA.


Question 1: Why Does the Addition of Methionine, Alone, to a Protein-Free Diet Increase Nitrogen Retention, Protein Accretion, and Growth? Several investigators have reported that methionine supplementation of a protein-free diet reduces body weight loss and improves nitrogen balance in rats (13), chickens (14), pigs (15), and dogs (16). Our own work (17) has confirmed the earlier suggestion (18) that the methionine response is not due to methionine per se but instead to methionine furnishing sulfur for cysteine biosynthesis via transsulfuration. Indeed, cysteine supplementation elicits a response equal to or greater than methionine. Protein turnover (degradation and synthesis) is an ongoing body process, even when no protein is being consumed. A portion of the amino acids released from body protein catabolism is oxidized and therefore not available for resynthesis of new protein. The cysteine response observed when a protein-free diet is fed implies that this amino acid is substantially depleted from body pools, making it the first limiting amino acids for endogenous protein synthesis.

Question 2: Why Is Excess Dietary L-Cysteine So Much More Toxic than an Isosulfurous Excess of L-Cystine, N-Acetyl-L-Cysteine or L-Methionine? At isosulfurous levels, L-cysteine, L-cystine, N-acetyl-L-cysteine, and L-methionine are equally efficacious for growth of animals fed a cysteine-deficient diet (19). Nonetheless, at pharmacologic dose levels these SAA elicit far different results (20–22). Addition of 3% or 4% L-cysteine to a typical corn–soybean meal diet for chicks or rats causes heavy mortality within 5 days. Similar levels of L-cystine, N-acetyl-L-cysteine, or methionine result in no mortality after 10 days of feeding. Cysteine is absorbed from the gut faster than cystine (22), and it has potent reducing-agent activity as well as mineral-chelation activity (21). It can also bind plasma proteins (22). N-acetylcysteine is less toxic than cysteine, perhaps because the deacetylation process occurs slowly. This is fortunate in that N-acetylcysteine is being used increasingly in the clinical setting (23, 24). It, along with cysteine itself, is also available over-the-counter in both health-food stores and pharmacies. They shouldn't be!

Question 3: Why Is Cystine the Least Digestible Amino Acid in Food and Feed Proteins? Most protein sources consumed by animals and humans have undergone some form of heat processing. This processing causes a significant portion of protein-bound cysteine to be oxidized to cystine, and protein-bound cystine is less digestible than protein-bound cysteine (25). The disulfide bridges created both within and between peptide chains when two cysteine residues condense to form cystine apparently restrict gut proteolytic enzyme attack. Whether the impaired digestibility results from presence of disulfide bonds within or between peptide chains is not known. Heat treatment together with alkaline food processing may also convert some of the dietary cystine to lanthionine (26), a crosslinked sulfur compound that has minimal SAA bioactivity (27). Thus, protein-bound cystine has a low bioavailability (28). This could be important clinically, because undigested cystine will pass to the colon where sulfate-reducing bacteria may degrade it to sulfides, and sulfides have been found noxious to colonic epithelial cells (29, 30). Still, the link between undigested SAA, particularly cystine, and colonic inflammation has not been firmly established.

Question 4: Are There Components of Foods and Feeds Other than Methionine, Choline, Betaine, Folacin, and Serine That Have Methyl Donating Capacity? Many foods and feedstuffs (e.g., soybean meal) contain significant and measurable quantities of S-methylmethionine (SMM), an analog of S-adenosylmethionine (SAM). As such, it may be capable of replacing (or sparing) SAM in biological methylation reactions such as choline biosynthesis from phosphatidylaminoethanol and creatine synthesis from guanidinoacetate. Our recent work using the chick as an animal model showed that SMM does indeed have choline-sparing activity (31). However, the methylation reaction in which homocysteine is converted to methionine prefers betaine as the methyl donor. Thus, methionine sparing by SMM was found to occur only when choline and betaine were deficient in the diet.

Dimethylsulfoniopropionate is another sulfur compound present in foods (32). Can consumption of this compound result in a choline-sparing effect similar to that observed with S-methylmethionine? Can ingestion of this compound reduce homocysteinemia via methylation of homocysteine to methionine? These two questions have not been answered.

Question 5: Why Are Sulfur Amino Acid Requirements for Adult Humans So Much Lower than Those for Adult Pigs? Amino acid requirements for maintenance have been determined based on attainment of zero nitrogen balance or on achievement of minimal oxidation of the test amino acid (direct oxidation method) or a target excess amino acid (indirect oxidation). With both humans and pigs, the maintenance SAA requirement (mg·kg–1·day–1) based on nitrogen balance has been found to be substantially higher than the maintenance lysine requirement (22). However, oxidation methodology has been used to set the official SAA and lysine requirements of humans (33), and this method has resulted in SAA requirement estimates that are less than one-half as great as the lysine requirement. Given that pigs and humans are similar physiologically and metabolically, how can the maintenance requirement ratio of SAA:lysine be so different between pigs and humans? Cysteine has an important precursor role (e.g., glutathione, taurine, CoA, and phosphoadenosine-5'-phosphosulfate biosynthesis) as well as an important role in synthesis of gut mucin and keratoid tissue that are ultimately sloughed from the body. Perhaps oxidation methodology underestimates the true requirement for an amino acid like cysteine. On the other hand, perhaps nitrogen balance methodology overestimates the requirement for an amino acid like cysteine. Clearly, these questions have not been resolved. Proper assessment of amino acid requirements is difficult and controversial (34–36).

Question 6: Why Do Some Dietary Copper Sources Provide Bioavailable Copper More Efficiently than Others, and How Does Cysteine Interact with Copper? Twenty years ago, cupric oxide (CuO) was the dominant source of Cu used in trace–mineral mixes for animals and in vitamin–mineral supplements for humans. However, research with pigs (37) and chickens (38, 39) has clearly shown that the Cu in CuO does not furnish any bioavailable Cu to the animal. However, copper oxide in the +1 state (i.e., Cu2O, cuprous oxide) is used as well as the sulfate and chloride salts of Cu. Many mineral supplements for humans continue to rely on CuO as a source of Cu, probably because this salt of Cu contributes to making a good (and smaller) pill (CuO is 80% Cu, whereas CuSO4·5H2O is only 25% Cu). Although definitive human data are not available on Cu utilization from CuO, the animal data make a convincing argument that CuO is probably poorly used by humans as well.

The liver and gall bladder are prominent storage sites for body Cu, but the bioavailability of Cu in pork liver (prominently used in pet foods) is near zero (40). The Cu in beef and chicken liver, on the other hand, is as bioavailable as that in CuSO4·5H2O (the accepted standard). What is the explanation for the poor Cu utilization in pork liver? A clear answer is problematic, although pork liver is known to be higher in cysteine than liver from other species, and cysteine is capable of binding Cu and therefore reducing its absorption from the gut (21).

Individuals with Wilson's disease (41) absorb too much and excrete too little Cu. Hepatologists treating these patients often use cysteine (or drug forms of cysteine such as D-penicillamine or dimercaptopropanol), N-acetylcysteine, or ascorbic acid as reducing agents and/or Cu-binding agents together with pharmacologic Zn supplementation to reduce dietary Cu absorption and enhance Cu excretion. Based on work with chicks fed high levels of Cu, cysteine compounds were found to be far more effective than either ascorbate or Zn in ameliorating the Cu-induced growth depression and reducing Cu deposition in the liver (42). Moreover, oral cysteine is over twice as effective as an isosulfurous level of either cystine or methionine (21). This finding, again, points to a marked difference between the pharmacologic effects of oral cysteine vs. cystine. The answer to this vexing difference between these two SAA probably lies in what is taking place in the gut, i.e., speed of absorption, amount taken up into mucosal protein, amount used for glutathione biosynthesis, and redox state and equilibrium.

Question 7: What Are the Priorities of Use When an Amino Acid with Multiple Functions Is Deficient in the Diet? Amino acids are used to synthesize a variety of different body proteins, e.g., myofibrillar, stromal, sarcoplasmic, keratoid, and acute-phase tissue proteins, hormones, enzymes, and specialized proteins such as metallothionein. Also, several amino acids have precursor roles. Concerning the synthesis priority of one type of protein over another when an amino acid is deficient, little is known about this intriguing question. Our work with chickens fed diets deficient in either histidine (43) or cysteine (44) suggested that protein synthesis is prioritized over either carnosine or glutathione synthesis. However, questions of priority remain for many amino acids that have important precursor roles: arginine for urea cycle function and synthesis of protein, creatine, polyamines, and nitric oxide; tyrosine for synthesis of protein, catecholamines, thyroxin, and melanin; tryptophan for synthesis of protein, serotonin, and niacin nucleotides; and glycine for synthesis of protein (contractile vs. collagen), heme, creatine, and uric acid. How gluconeognic amino acids are partitioned for gluconeogenesis vs. protein and precursor synthesis is another unresolved priority question. Other priority examples could be mentioned, but clearly, the priority for functional synthesis is an area of nutrition we do not fully comprehend.

Question 8: Why Does a Large Excess of Dietary Lysine Elicit a Growth Response in Niacin-Deficient Animals? Niacin activity comes not only from ingested niacin (or niacinamide) but also from ingested tryptophan. Most of the tryptophan flux during turnover goes to CO2 (via {alpha}-ketoadipic acid), with only a small portion going to serotonin and nucleotides of niacin. {alpha}-ketoadipic acid is also an intermediate in lysine catabolism to CO2. We demonstrated that addition of 1–1.5% excess lysine to a niacin-deficient diet elicits a growth response in chicks (45). The same lysine addition to a niacin-adequate diet caused a substantial growth depression. At the key branch point of tryptophan catabolism to either niacin nucleotides or CO2 (i.e., at 2-amino-3-carboxymuconic acid semialdehyde), {alpha}-ketoadipate is projected to accumulate due to lysine catabolism; we suggest that this forces more of the 2-amino-3-carboxymuconic acid semialdehyde flux in the direction of niacin nucleotide synthesis, with less being directed to CO2 via {alpha}-ketoadipic acid.

Golberger in 1922 (46) is generally given credit for discovering a cure for black tongue in dogs and pellagra in humans (47), but it was not until 1937 that Elvehjem et al. (48) isolated nicotinamide from liver extracts and showed that this compound would cure black tongue in dogs. Seventy years earlier, German chemists had actually synthesized nicotinic acid, but because this compound did not cure beri-beri in humans (now known to be caused by thiamin deficiency), it remained an unappreciated chemical entity for several decades (1). Today we know that diets poor in niacin and tryptophan cause pellagra, but we also know that iron deficiency anemia and poor protein quality (i.e., lysine deficiency) exacerbate the condition. Iron is required in two of the several enzymatic reactions leading to niacin biosynthesis from tryptophan (49). We also know that coffee consumption is a factor to be considered in pellagra, because coffee is rich in niacin (50). We suspect that diets very low in lysine result in minimal {alpha}-ketoadipic acid production from lysine, such that more of the tryptophan-derived 2-amino-3-carboxymuconate semialdehyde flux will be directed toward {alpha}-ketoadipic acid and, therefore, less will be directed toward niacin nucleotide biosynthesis.

Question 9: Why Is It That Growth on a Diet That Is Equally Deficient in an Amino Acid and Two Different B Vitamins Will Respond Markedly to Dietary Addition of Any One of the Three Deficient Nutrients? In underdeveloped countries, poor nutrition is characterized by multiple nutrient deficiencies. We developed a soy–protein isolate basal diet that could be made markedly deficient in several essential nutrients, e.g., methionine, choline, riboflavin, vitamin B6, and Zn (51). Surprisingly, when diets were made approximately equally limiting in any pairs or trios of these nutrients, marked growth responses were found to occur from any one of the deficient nutrients. Thus, the order of limiting amino acid concept in which responses will not occur to a 2nd or 3rd limiting amino acid unless the 1st (or 1st and 2nd) limiting amino acid is supplemented does not apply when multiple deficiencies of amino acids, vitamins, and trace minerals coexist in a diet. Logical explanations for this phenomenon are not obvious.

Question 10: Does a Single Deficiency of One Amino Acid Cause the Same Degree of Growth Depression as an Equal Deficiency of Another Amino Acid? All single amino acid deficiencies also involve a profile of excess amino acids over and above the single deficiency, and each single deficiency results in a unique and different profile of excess amino acids. The excess amino acids can have very different effects on voluntary food intake, depending on which specific amino acid is deficient. Using a chemically defined amino acid diet, Sugahara et al. (52) evaluated single deficiencies (60% of required level) and compared them to a deficiency of all essential amino acids (i.e., all at 60% of required level). Single deficiencies of phenylalanine plus tyrosine, tryptophan, or isoleucine resulted in poorer growth (due to lower food intake) than that which occurred from a deficiency of all amino acids together. The excess amino acids over and above each single deficiency, although having variable effects on voluntary food intake, did not have negative effects on food efficiency, i.e., relative to the deficiency of all amino acids. Why certain dietary excess amino acid profiles cause food intake reductions while other profiles do not remains a mystery.

Question 11: To What Extent Does Gut Synthesis of Indispensable Amino Acids Contribute to the Amino Acid Requirements of Pigs? Torrallardona et al. (53) used 15N and 14C labeling experiments to evaluate gut amino acid biosynthesis and subsequent ileal absorption in 20-kg pigs. Amino acid absorption of microbial origin was estimated at 1.1 g/day for lysine, 2.0 g/day for leucine, 1.8 g/day for valine, and 0.8 g/day for isoleucine. These quantities are not insignificant. In fact, they exceed the estimated maintenance dietary needs for these amino acids. Thus, the true maintenance requirements for amino acids must be the sum of true ileal digestible dietary needs plus the amount provided by gut microbial synthesis. For a 20-kg pig, this would make the total Lys maintenance requirement 1.4 g/day rather than the dietary Lys maintenance requirement of 304 mg/day (54). Because the gastrointestinal tract of pigs is similar to that of humans, microbial synthesis and subsequent absorption of amino acids probably also contribute importantly to the maintenance amino acid requirement of humans (55, 56).

Question 12: Why Are 10–50% of Absorbed Amino Acids Wasted (Catabolized) When Fed to Growing Animals Well Below Required Levels for Maximal Protein Accretion? Numerous studies have now verified what might be referred to as the inefficiencies of amino acids used for protein accretion (54, 57–62). Thus, at well below required levels, amino acids recovered in whole-body protein represent only 50–90% of the amino acids fed (i.e., absorbed, because the amino acids fed are crystalline amino acids or derived from highly digestible casein). The amino acid that stands out as being the most inefficiently used is tryptophan. Over 50% of absorbed tryptophan is apparently not used for protein synthesis (i.e., it cannot be recovered in whole-body protein). Work in this area also suggests that the efficiencies of utilization for each essential amino acid are constant at all levels of intake between maintenance and {approx}90% of the requirement for maximal protein accretion. The loss of (limiting) amino acids for functional protein synthesis may be related to the demands of amino acids for gluconeogenesis (63).

Question 13: Why Do Feline Species Often Die Within 24 h When Fed an Arginine-Free Diet? Felids evolved as true carnivores, and as such they have numerous nutritional idiosyncrasies (64, 65). In contrast to omnivorous mammals like dogs and pigs, cats either totally lack or have low levels of key enzymes for synthesis of vitamin A from {beta}-carotene, arachidonic acid from linoleic acid, taurine from cysteine, niacin from tryptophan, and ornithine from glutamic acid. Unique among nutrient deficiencies (in any species), ingestion by cats of a single meal of an arginine-free diet causes severe pernicious effects, including anorexia, hyperammonemia, emesis, ataxia, and even death (66, 67). Cats have a low capacity for gut mucosal ornithine biosynthesis from glutamic acid, because of low activities of pyrroline-5-carboxylate synthase and ornithine aminotransferase. Thus, with arginine deprivation, ornithine becomes critical for the liver to take up ammonia as carbamoyl phosphate, and intestinal mucosa is the primary site of de novo ornithine biosynthesis.


Arginine (abbreviated as Arg or R)[1] is an α-amino acid. The L-form is one of the 20 most common natural amino acids. Its codons are CGU, CGC, CGA, CGG, AGA, and AGG. In mammals, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. Infants are unable to effectively synthesize arginine, making it nutritionally essential for infants. Adults, however, are able to synthesize arginine in the urea cycle.

Arginine was first isolated from a lupin seedling extract in 1886 by the Swiss chemist Ernst Schulze.
Dietary Sources

Arginine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained directly through the diet. The biosynthetic pathway however does not produce sufficient arginine, and some must still be consumed through diet. Arginine is found in a wide variety of foods, including[2]:

    * Animal sources: dairy products (e.g. cottage cheese, ricotta, milk, yogurt, whey protein drinks), beef, pork (e.g. bacon, ham), poultry (e.g. chicken and turkey light meat), wild game (e.g. pheasant, quail), seafood (e.g. halibut, lobster, salmon, shrimp, snails, tuna in water)
    * Vegetarian sources: wheat germ and flour, buckwheat, granola, oatmeal, nuts (coconut, pecans, cashews, walnuts, almonds, Brazil nuts, hazel nuts, pine nuts, peanuts), seeds (pumpkin, sesame, sunflower), chick peas, cooked soybeans, chocolate
    * Other: some energy drinks

[edit] Biosynthesis

Arginine is synthesized from citrulline by the sequential action of the cytosolic enzymes argininosuccinate synthetase

Arginine plays an important role in cell division, the healing of wounds, removing ammonia from the body, immune function, and the release of hormones. Arginine, taken in combination with proanthocyanidins[4] or yohimbine[5], has also been used as a treatment for erectile dysfunction.

[edit] In proteins

The geometry, charge distribution and ability to form multiple H-bonds make arginine ideal for binding negatively charged groups. For this reason arginine prefers to be on the outside of the proteins where it can interact with the polar environment. Incorporated in proteins, arginine can also be converted to citrulline by PAD enzymes. In addition, arginine can be methylated by protein methyltransferases.

ncreased risk of death from heart disease

A clinical trial found that patients taking an L-arginine supplement following a heart attack didn't improve in their vascular tone or their hearts' ability to pump. In fact, more patients died who were taking L-arginine than placebo and the study was stopped early with the recommendation the supplement not be used by heart attack patients. The supplement still is widely marketed disgust.gif Yet Citrulline was important  and prevented this!!!??

Arginine biosynthetic capacity is very different among species. Avian species lack a mitochondrial source of carbamoyl phosphate synthase, and therefore synthesize no arginine. Other than felids, however, mammalian species synthesize enough arginine (in kidney) to meet about one-half of the requirement for maximal growth. For maintenance in adult mammalian species (other than cats), enough arginine is made from citrulline in the kidney to meet the entire requirement. Thus, adult pigs (68) and adult humans (69) do not have a dietary requirement for arginine. For growth, ornithine cannot replace arginine, but citrulline can. Oral ornithine is absorbed and taken up by the liver where arginine is indeed synthesized, but the activity of hepatic arginase is so high that virtually all of the liver arginine is catabolized to ornithine and urea. Even if ornithine of gut or liver origin could be transported to the kidney where arginase activity is low (70), kidney tissue cannot convert ornithine to citrulline due to lack of the enzyme ornithine transcarbamoylase. In contrast, oral citrulline is absorbed but not taken up by liver tissue, instead going to the kidney where net arginine synthesis takes place (70). Because enough citrulline is synthesized in gut mucosal tissue to meet the minimal maintenance need for arginine in pigs and humans, nitrogen balance is maintained, and neither hyperammonemia nor orotic aciduria occur when an arginine-free diet is fed (68–70). Whether extrahepatic tissues other than gut mucosa can produce citrulline is not known with certainty, although the small intestine likely accounts for the vast majority of circulating citrulline (71).
   (ohmy.gif  no.gif   Note there are huge drops of citrulline after bypass surgery!!!!

The effect of cardiopulmonary bypass on citrulline lev-. els was profound, with a precipitous drop seen immediately. after surgery (Fig 1).

CONCLUSIONS: In this first report of the use of intravenous citrulline in humans, we found citrulline to be both safe and well tolerated in infants and young children undergoing congenital cardiac surgery. Because of the rapid clearance, the optimal dosing regimen was identified as an initial bolus of 150 mg/kg given at the initiation of cardiopulmonary bypass, followed 4 hours later by a postoperative infusion of 9 mg/(kg.h) continued up to 48 hours. Using this regimen, plasma arginine, citrulline, and nitric oxide metabolite levels were well maintained. Intravenous citrulline needs to be studied further as a potential therapy for postoperative pulmonary hypertension.

What about arginine for adult pregnancy? Thirty years ago, we tested this hypothesis in gravid swine, completing studies (which would not be approved by today's animal care committees) in which an arginine-free purified diet was fed throughout the entire 114 days of pregnancy (72, 73). Pregnancy outcome was not affected in terms of litter size and birth weight, nitrogen retention was normal, and no hyperammonemia or orotic aciduria occurred. Lactation performance also was normal. Because the animals used were young first-litter females that were still experiencing some maternal growth, the conclusion was that swine pregnancy, regardless of parity, does not require a dietary source of arginine (74). Human pregnancy also may require no dietary arginine, but it is unlikely this experiment will ever be done!

Question 14: Are the Estimated Protein Requirements for Humans Optimal in All Circumstances? The Dietary Reference Intake (DRI) Committee of the Food and Nutrition Board (33) has suggested a minimal protein requirement for adults of 0.66 g·kg–1·day–1 and a recommended intake level of 0.80 g·kg–1·day–1, the latter amounting to 56 g/day for a 70-kg person. Obviously, any listing of a protein requirement depends on both protein digestibility and protein quality, i.e., the ability of a protein to supply indispensable amino acids. Because obesity is a serious problem in the U.S., some have suggested that a protein intake almost double the 0.8 g·kg–1·day–1 intake suggested by the DRI Committee may be beneficial to weight control (75, 76). Thus, diets with reduced carbohydrates and higher protein (1.5 g·kg–1·day–1) may stabilize blood glucose and increase the body lean/fat ratio. The mechanism proposed is that extra protein is needed to provide branched-chain amino acids, especially leucine, for regulation of muscle protein synthesis, insulin signaling, and glucose recycling via alanine. The estimated average requirement for branched-chain amino acids (i.e., leucine, isoleucine, and valine) by the DRI Committee is 68 mg·kg–1·day–1 for adults, but Riazi et al. (77, 78) suggest that more than double this intake may be required to achieve minimal oxidation of their indicator excess amino acid, phenylalanine. The branched-chain amino acid requirement for school-age children was also found to be considerably higher than the DRI Committee estimate (79).

The requirement for protein and individual amino acids has been estimated for pregnancy of both humans (33) and swine (74). Pregnancy includes amino acid needs for maternal maintenance (and maternal growth if dams are young), growth of the products of conception (placenta and fetal tissue), and growth of the mammary gland (80). With swine, amino acid requirements have actually been estimated for each of these components at various stages of gestation (80, 81). The lysine requirement (g/day) was found to be more than twice as great during the last one-third of gestation as during the first two thirds. The NRC Committee on Swine Nutrition (74) lists both protein and amino acid requirements as being the same at all stages of gestation; this can't be correct. With swine, it is easy to calculate that feeding a single gestation diet at 2 kg/day throughout gestation results in overfeeding protein and amino acids during the first 70 days of gestation, but underfeeding protein and amino acids during the last 44 days (80). Perhaps taking account of the greater need for protein and amino acids during the last one-third of gestation in both pigs and humans would result in better lactation performance. This has not been tested empirically, although the DRI Committee (33) has acknowledged this higher requirement for protein and amino acids in late gestation by recommending that the protein intake during the last trimester of human pregnancy be increased by 6 g/day.

Question 15: Can Maternal Diet Affect the Sex Ratio of Offspring? Rosenfeld et al. (82) and Rosenfeld and Roberts (83) fed (ad libitum) female mice a diet either high in saturated fat (lard) or a diet low in saturated fat but high in carbohydrates from 4 to 45 weeks of age. A total of 1,048 offspring were born from 108 pregnancies. Sex ratio of offspring was close to 1:1 for dams bred at 10 weeks of age, regardless of maternal diet. [b]However, sex ratio of offspring for dams bred at 20, 28, or 40 weeks of age was 0.67:0.33 (male/female) for dams fed the high-fat diet. Conversely, in mature dams fed the low fat-high carbohydrate diet, the sex ratio of offspring was skewed toward females (0.39:0.61 male/female)[b]. Explanations for these fascinating observations have been proposed but not empirically tested. However, Krüger et al. (84), in their 30-year evaluation of sex ratio in springbok (an African antelope), suggest that sex ratio determination most likely occurs at or near the time of embryo implantation. One wonders whether sex-ratio skewing due to diet could occur in dairy cows, and if so, how long the feeding period would need to be to effect the change. Clearly, any technique, nutritional or otherwise, that would yield more female calves from gravid dairy cows would be of great benefit to the dairy industry.


The years ahead will see continued advances in the nutritional sciences, particularly in areas involving how nutrient levels ranging from deficient to surfeit may affect overall health, longevity, mental capacity, and gene expression. Many of the big questions in nutrition have been largely answered, but there are many problems still remaining that deserve our attention.

Edited by crystal sage, 16 March 2008 - 06:02 PM.

#38    crystal sage

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Posted 16 March 2008 - 06:09 PM


These results indicate that most if not all patients with anorexia nervosa have abnormal levels of arginine vasopressin in their plasma and cerebrospinal fluid that are corrected very slowly with weight gain. The cause and consequences of these abnormalities remain to be determined.



Abnormal glucose tolerance is often found in patients with anorexia nervosa (AN). We attempted to evaluate pancreatic B-cell functioning after intravenous glucagon administration. Fourteen patients with the restricting type of AN (percentage of ideal body weight 71.5 ± 1.6%, mean ± SE) and 6 patients with the bulimic type of AN (77.0 ± 3.0%) were studied. After an overnight fast, glucagon (0.02 mg/kg) was injected i.v. into all subjects and 6 normal controls. Blood samples were obtained at 0, 5, 30, 60, 90 and 120 min to measure blood glucose (BS), serum insulin (IRI) and C-peptide (CPR). The same tests were repeated in 8 patients with restricting AN after therapy and restoration of body weight (85.9 ± 1.0% of ideal body weight). BS responses did not differ among the groups. Peak serum levels (5 min) of both IRI and CPR in restricting AN patients were significantly lower than those in bulimic AN patients and in normal controls. BS, IRI and CPR concentrations did not change significantly following restoration of body weight. Pancreatic B-cell dysfunction after glucagon administration was observed in restricting AN patients and the abnormality persisted after short-term weight restoration.

Edited by crystal sage, 16 March 2008 - 06:13 PM.

#39    crystal sage

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Posted 16 March 2008 - 10:44 PM

Benefits of inositol



The benefits of inositol include:

1. Fewer mood swings.

2. Relief from depression.

3. Relief from panic attacks.

4. Relief from OCD.

Many so called natural cures are just old wives tales or Internet snake oil. However inositol is one dietary supplement that even conservative medical experts agree can help bipolar people.

Let me explain . . .
Benefits of inositol

Research has shown a lack of inositol in bipolar patients. Research has also shown that supplementing with inositol reduces bipolar symptoms.

So why such positive benefits of inositol?

Phospholipids are fat-soluble, naturally-occurring molecules that help make up our cellular structure. Both inositol and the phospholipids play a major role in signal transmission for many neurotransmitters and hormones. There is growing evidence that lithium and fish oil may also exert their beneficial effects by regulating these same signal transmissions.

Inositol is important for regulating serotonin and insulin, and breaking down fats and reducing blood cholesterol.

Inositol and bipolar
There have been several clues alerting researchers to the connection between inositol in bipolar.

When postmortem brain tissue has been examined from deceased bipolar patients, low inositol levels have been found in the frontal cortex, as well as in lymphocytes. (Lymphocytes are a type of white blood cell responsible for immune responses.)

Another clue to a connection is that inositol plays a major role in the same brain and nerve systems that respond to mood stabilizers.

There have also been reports of reduced inositol in the cerebrospinal fluid (CSF) of some bipolar people.
Inositol treatment of obsessive-compulsive disorder

Inositol as a treatment for psychiatric disorders: a scientific evaluation of its clinical effectiveness


Research indicates that inositol is an effective and safe option in the treatment of panic disorder, obsessive-compulsive disorder (OCD), bulimia nervosa, binge eating and/or depression. (3-9) Inositol's efficacy, in the absence of side effects, makes this nutrient an attractive addition to treatment plans for specific mood disorders. Following is a scientific review of inositol for the treatment of mood disorders

Other uses

Low levels of inositol have been found in the nerves of diabetic patients and supplements may be useful in the treatment of diabetic nerve disorders. Inositol has also been used to treat multiple sclerosis. Recent research suggests that myo-inositol can prevent folate-resistant neural tube defects in mice.

Edited by crystal sage, 16 March 2008 - 10:58 PM.

#40    gomez


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Posted 07 January 2009 - 04:21 AM

Hi guys,thanks for the information about Eating Disorder.Because in my family no one has such a disorder.Anyway i am glad to know about it.That will help me to remind my friends.

Bulimia News and Discussion Forum

#41    daveivane


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Posted 17 March 2009 - 11:13 AM

This is a very informative and useful forum indeed. I learnt so much about eating disorders here. Thanks a ton. Cheers!

#42    SV-001


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  • You must learn to program your own mind. If you don't, others will learn to program it for you.

Posted 24 March 2009 - 11:00 PM

I do truely believe many mental illnesses are caused by psychic abilities that someone may not be in control/aware of
and therefore causes them to have some inblances that result from not being able to cope with certain
strong and negative thoughts or emotions.
I myself have at some points found it difficult to separate my own from others, causing me to stress.
And like many of you may know, stress can lead to certain mental and emotional disoders.

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