Thursday, March 24, 2011

Physical Activity Decreases Salt's Effect on Blood Pressure, Study Finds

If you are looking for another reason to be active, how does this one sound to you. So, stop procrastinating and get moving now. At Jungle, Friday Classes are always FREE. So, we hope to see you around sometime.

ScienceDaily (Mar. 23, 2011) — The more physically active you are, the less your blood pressure rises in response to a high-salt diet, researchers reported at the American Heart Association's Nutrition, Physical Activity and Metabolism/Cardiovascular Disease Epidemiology and Prevention 2011 Scientific Sessions.

"Patients should be advised to increase their physical activity and eat less sodium," said Casey M. Rebholz, M.P.H., lead author of the study and a medical student at the Tulane School of Medicine and doctoral student at the Tulane University School of Public Health & Tropical Medicine in New Orleans. "Restricting sodium is particularly important in lowering blood pressure among more sedentary people."

Investigators compared study participants' blood pressure on two one-week diets, one low in sodium (3,000 mg/day) and the other high in sodium (18,000 mg/day).

The American Heart Association recommends consuming less than 1,500 mg/day of sodium.

If a person's average systolic blood pressure (the top number in the reading, measured when the heart is contracting) increased 5 percent or more from the low-sodium to the high-sodium regimen, the researchers labeled them as high salt-sensitive.

Based on physical activity questionnaires, researchers divided participants into four groups ranging from very active to quite sedentary.

The average increases in systolic blood pressure after switching from low to high sodium, adjusted for age and gender, were:

•5.27 mm Hg in the least active group

•5.07 mm Hg in the next-to-lowest activity group

•4.93 mm Hg in the next to highest activity group

•3.88 mm Hg in the most active group

Compared with the sedentary group, the odds of being salt-sensitive, adjusted for age and gender, fell:

•10 percent in the next-to-lowest activity group

•17 percent in the next-to-highest activity group

•38 percent in the most active group

"In all the analyses we found a dose-response relationship with the more activity, the better," Rebholz said.

The participants were 1,906 Han Chinese adults (average age 38) in the Genetic Epidemiology Network of Salt Sensitivity (GenSalt), a large project to identify genetic and environmental factors contributing to salt sensitivity. Siblings and their parents were invited to become involved in GenSalt if at least one sibling had pre-hypertension (blood pressure between 120/80 and 139/89 mm Hg) or stage-1 hypertension (between 140/90 and 159/99 mm Hg). No one was on blood pressure medication during the study.

The GenSalt project is located in rural China because the homogeneous population makes it more likely that genes influential to blood pressure control will be identified.

"The study needs to be repeated, but I suspect that the relationship between physical activity and salt-sensitivity will apply to other populations," Rebholz said.

Co-authors are: Dongfeng Gu, Ph.D.; Jing Chen, M.D., M.S.; Jian-feng Huang, M.D.; Jie Cao, M.D., M.S.; Ji-chun Chen, M.D., M.S.; Jianxin Li, M.D.; Fanghong Lu, M.D.; Jianjun Mu, M.D.; Jixiang Ma, M.D.; Dongsheng Hu, M.D., M.S.; Xu Ji, M.D.; Lydia A. Bazzano, M.D., Ph.D.; Depei Liu, M.D., Ph.D.; and Jiang He, M.D., Ph.D.

The above story is reprinted (with editorial adaptations by ScienceDaily staff) from materials provided by American Heart Association

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American Heart Association


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Monday, March 21, 2011

Amino Acids. Do you know what they are?

One of our Jungle animals had this quarry: "What are Amino Acids". We hear a lot about them but it is always good to refresh our information.  So, get comfortable, for this is a long reading but definitively worth it. This is Jungle Miami's post today.

Understanding Amino Acids

(Autumn 2000 Optimum Nutrition Magazine)

Amino acid requirements are tremendously increased by disease, prolonged periods of stress and inborn metabolic errors. Billie J Sahley Ph.D, Executive Director of the Pain & Stress Centre in San Antonio, USA, and co-author of Healing With Amino Acids highlights some of the latest research on amino acids in therapy

Proteins control almost every biochemical reaction in the body. Every protein is made from amino acids, which are commonly called the building blocks of life. All of the nearly 40,000 distinct proteins found in the human body are made up from only 20 amino acids called the proteogenic amino acids.

Amino acids can be divided into essential and nonessential. Essential amino acids cannot be synthesised in the body and must be obtained from the diet. Non-essential can be synthesised in the body, and are not mandatory in the diet. Although the body can manufacture non-essential amino acids, an abnormality in their production can be detrimental metabolically. There are some conditionally essential amino acids which are essential under certain circumstances, i.e., infancy, illness, stress, etc.

Most of the protein in the body is found in the skeletal muscles. Only 0.1% of all the protein is found as free amino acids. Plasma amino acids represent what is available to the body at the current time. A deficiency in one of the proteogenic amino acids can limit the body’s ability to make an optimal number of certain proteins. Deficiency effects result in both poor health and disease.



The branched chain amino acids include leucine, isoleucine, and valine. As essential amino acids, BCAAs must be obtained from foods. They are especially involved in stress reactions, energy and muscle metabolism. BCAAs are unique because the skeletal muscles use them directly as an energy source, and they promote protein synthesis.

The BCAAs are similar structurally, but have different metabolic routes. Leucine solely goes to fats; valine solely to carbohydrates; and isoleucine to both. A valine deficiency appears as neurological defects in the brain. Muscle tremors mark an isoleucine deficiency. Stress states such as infections, trauma, surgery, fever, cirrhosis and starvation require proportionally more leucine than valine or isoleucine. Diseases such as hepatitis, cirrhosis, hepatic coma or liver disease, lower the levels of BCAAs. BCAAs, as well as other amino acids, are commonly fed intravenously to chronically ill patients. The BCAAs, particularly leucine, stimulate protein synthesis, increase the re-utilisation of other amino acids in many organs, and decrease protein breakdown.

As stress rises, total caloric intake needs increase, primarily due to increased protein requirements. Stress causes proteins to break down rapidly, and increases amino acid utilisation three-to-four-fold. About 30% of the diet should be protein or amino acids, especially when the body undergoes severe stress. But when taken in supplement form, BCAAs decrease the rate of amino acid and protein breakdown. More BCAAs and vitamin B6, or pyridoxal 5’phosphate (P5’P), are needed as stress or disease accelerates.

Utilisation of BCAAs by athletes, especially weight lifters, in-creases available energy. They help replace steroids used by those who want to build muscle mass. The BCAAs, especially leucine, greatly produce energy under many kinds of stress from trauma, surgery, fever, infection, muscle training, and weight lifting. With prolonged exercise, about 5 to 10% of the energy used comes from amino acids, especially BCAAs. Normal dosage of BCAAs is 1,000 to 3,000mg per day, divided. They should be taken together as the ingestion of only one BCAA, particularly leucine, decreases the plasma tissue levels of valine and isoleucine.


Alanine is a non-essential amino acid, and functions as an inhibitory neurotransmitter in the brain. Highest concentrations of alanine are found in the muscles. During hypoglycaemia, alanine may provide an alternative source of glucose.

Elevated alanine levels in the blood can cause drug-resistant seizure disorders or severe depression. Low alanine levels are often seen with low glycine and taurine, and when the BCAAs are deficient. Normal alanine metabolism requires the presence of vitamin B6. Alanine is essential for the normal metabolism of tryptophan.

Best food sources of alanine include wheatgerm, turkey, duck and cottage cheese. Usual supplemental dose range is 200 to 600mg, daily.

"Recent research indicates stored body fat into carnitine plays an important role in converting energising the heart, reducing angina attacks, energy, controlling hypoglycaemia, and is beneficial in the treatment of diabetes, liver and kidney disease."


Aspartic acid is a non-essential amino acid and a major excitatory neurotransmitter. Formed in the body from glutamic acid with the presence of vitamin B6, aspartic acid plays a major role in the metabolism of ammonia via the urea cycle. Aspartic acid also metabolises carbohydrates via the Krebs cycle, and forms constituents of DNA called pyrimidine and orotates. Research indicates aspartic acid may be a stimulator of the thymus gland and the immune system.

Elevated aspartic acid levels may be seen in some patients with depression, epilepsy, stroke, high BCAAs, and low ornithine. Asparagine forms from ATP and aspartic acid, and can convert back into aspartic acid, if needed by the body.

Good food sources of aspartic acid include meats such as pork, turkey, chicken and wild game, wheatgerm, cottage and ricotta cheeses.


Carnitine was discovered in 1905 from extracts of meats, but no physiological role for it could be found until 50 years later. Early research indicated carnitine to be essential to the diet, but later it was discovered the body produced carnitine from lysine and methionine, provided sufficient amounts of niacin, vitamin B6, C, and iron were present. If a carnitine deficiency exists, deficiencies of lysine and methionine also exist. Concentrations of carnitine are 40 times greater in the muscles than in the plasma. Major sources of carnitine in the diet are meat, especially organ meats such as liver; and dairy products. Vegetables, grains and fruit contain little or no carnitine.

In 1973 research showed carnitine deficiencies exist in some people for various reasons. Between 1980 and 1983, almost 300 studies were published investigating carnitine's nutritional value and anomalies of carnitine metabolism causing clinical symptoms. Some carnitine deficiency symptoms include impaired lipid (fat) metabolism; lipid accumulation in the skeletal muscles, heart muscle, and liver; and progressive muscle weakness with a build-up of fats in the muscle cells. In children, carnitine deficiency may manifest as loss of muscle tone, failure to thrive, swelling in the brain, recurrent infections, hypoglycaemia and heart disturbances.

Carnitine is essential for the transportation of long-chain fatty acids into the cells where fats can be converted to energy. Recent research indicates carnitine plays an important role in converting stored body fat into energy, energising the heart, reducing angina attacks, controlling hypoglycaemia, and is beneficial in the treatment of diabetes, liver and kidney disease. Carnitine primarily regulates fat burning in the body. It transports large fat molecules into the part of the cells where fats can be converted into energy. If your level of vitamin C is low, you can have an apparent deficiency of carnitine. If carnitine is absent or deficient, many fats cannot be burned. Fats build up within the cell and bloodstream as triglycerides and cholesterol. Carnitine supplementation significantly reduces serum triglycerides and cholesterol levels, while increasing HDL (high density lipoprotein or “good” cholesterol). Dosages are 1,000 to 3,000mg per day, divided.


Cysteine is considered conditionally essential, and is one of the sulphur-containing amino acids. Cystine is the stable form of cysteine. Conversion of one to the other occurs in the body, as either is needed. If vitamin C is not present, cysteine converts to cystine. Cysteine spares methionine (another important amino acid) and can completely replace dietary methionine if the diet is supplemented by appropriate amounts of folic acid and vitamin B12.

Cysteine resides abundantly in proteins such as keratin in hair (12%) and trypsinogen (10%). It also acts as a detoxifier. Heavy metals such as mercury, lead, and cadmium are “tied up” by cysteine so they can be removed from the body.

Cysteine may protect heavy drinkers and smokers against acetaldehyde poisoning from chronic alcohol intake or smoking, according to Dr Herbert Sprince at the V.A. Hospital in Coatesville, Pennsylvania, and Thomas Jefferson University in Philadelphia. Biochemist, Durk Pearson reports cysteine is effective “not only in preventing hangovers, but also in preventing brain and liver damage from alcohol, and in preventing damage such as emphysema and cancer caused by smoking.” Cysteine has been found to offer a degree of protection against radiation.

Amino Acids for Brain and Body Functions

A specialised form of cysteine known as N-Acetyl Cysteine (NAC), was first produced by Mead Johnson for the treatment of excess mucus. The primary use for NAC is as a mucus-reducing agent. Mucus strands are broken up to decrease viscosity and congestion associated with excess mucus and sinus drainage. Oral supplementation of NAC is used with allergies, bronchitis, chronic sinusitis, asthma, pneumonia, cystic fibrosis, and even the common cold. Supplemental NAC dosage is usually 600mg, two to three times daily. Diabetics should not use cysteine because it can cause glucose levels to change.


GABA (Gamma Amino Butyric Acid), an inhibitory neurotransmitter, is found throughout the central nervous system (CNS). GABA assumes an ever-enlarging role as a significant influence on pain, stress, anxiety, and depression as well as stress-induced illnesses. By January 1998, there were over 3,000 documents and texts on GABA, describing how it affects anxiety/stress in the brain.

If you examine a step-by-step process of what happens in the brain when you feel stress and anxiety, you would see how GABA works to slow down messages. Panic, anxiety, or stress-related messages begin to release numerous signals, and concurrently a physiological response begins to take place - the fight-or-flight syndrome.

Research done at The Pain & Stress Center, San Antonio, USA, in stress, with patients suffering from all types of pain, muscle spasms or anxiety/panic attacks, demonstrated pure GABA, 750 mg, can mimic the tranquilizing effects of Valiumor Librium without the addiction or fear of being sedated The unceasing alert signals from the limbic system eventually overwhelm the cortex (the decision-making part of the brain), and the ability of the cortex and the rest of the stress network becomes exhausted. The balance between the limbic system and, in fact, the rest of the brain to communicate in an orderly manner depends critically on inhibition. GABA inhibits the cells from firing, diminishing anxiety-related messages from reaching the cortex.

GABA fills certain receptor sites in the brain and body. This slows down and blocks the excitatory levels of the brain cells that are about to receive the anxiety-related, incoming message. When the message is received by the cortex, it does not overwhelm you with anxiety, panic or pain. You are able to maintain control and remain calm. But, if you are under prolonged stress or anxiety, your brain exhausts all the available GABA and other inhibitory neurotransmitters, thus allowing anxiety, fear, panic and pain to attack you from every direction. Your ability to reason diminishes.

Research done at The Pain & Stress Centre, in San Antonio, with patients suffering from all types of stress, pain, muscle spasms or anxiety/panic attacks, demonstrated pure GABA (750mg) can mimic the tranquilizing effects of Valium or Librium without the possibility of addiction or fear of being sedated. GABA fills the receptor sites in the brain and nourishes the brain with what should be there. The calming effect usually occurs within l0 to 12 minutes.


Glutamic acid is a non-essential amino acid which can be synthesised by the body, or be converted into glutamine and GABA. Glutamic acid is thought to be an excitatory neurotransmitter. It acts as a brain ammonia detoxifier.

Since glutamic acid can be manufactured from aspartic acid, ornithine, arginine, proline, and alpha-ketoglutarate, deficiencies of this amino acid have not been seen. Elevation of glutamic acid may be present in some schizophrenics, epileptics, and patients with gout. In fact, epileptics generally have an elevation of glutamic and aspartic acids, and have low levels of GABA, taurine, and glycine. Rich food sources of glutamic acid include ham, bacon, turkey, chicken, duck, cottage cheese, yoghurt, wheatgerm and muesli.


Glutamine is the third most abundant amino acid in the blood and brain. Glutamine, an inhibitory neurotransmitter, acts as a precursor for GABA, the anti-anxiety amino acid. It helps the brain dispose of waste ammonia, a protein breakdown by-product. Glutamine assists the body in muscle development when illness causes muscle wasting, sometimes seen following a high fever, chronic stress, or a traumatic accident. It also provides a major alternative fuel source for the brain with low blood sugar levels.

Glutamine's most important function is strengthening the immune system. It supports the multiplication of selected white blood cells which strengthen the body's defense system. Glutamine aids other immune cells in killing bacteria, healing wounds, and maintaining and supporting glutathione, as an important antioxidant. Glutamine also supports pancreatic growth.

Scientists at the National Institute of Health, USA, in 1970 found glutamine to be the most important nutrient for the intestinal tract. During times of illness, the body uses glutamine to help tissue repair in the kidneys, intestines, and liver. Leaky gut syndrome is recognised more often today due to the increased use of anti-inflammatory medications. This makes the intestines more permeable and allows substances and foods which do not normally pass into the circulation to cross. Food allergies can result, causing discomfort and pain. But glutamine helps the gut to heal and makes the intestines less permeable. Japanese researchers found glutamine helps stomach ulcers heal. It helps clear the body of waste through the kidneys and liver. For those with impending surgery, glutamine supplements should be considered before, during, and after surgery.


Glycine is a non-essential amino acid, and has the simplest structure of all the amino acids, resembling glucose (blood sugar) and glycogen (excess sugar converted in the liver for storage). As the third major inhibitory neurotransmitter in the brain, glycine readily passes the blood-brain barrier. The body needs glycine for the formation of DNA, collagen, phospholipids, and for the release of energy.

According to Ronald Kotulak in his book, Inside the Brain, glycine “helps trigger brain cells to fire electric charges and speed learning.” Glycine helps spasticity and seizures, and is involved in behaviours related to convulsions and retinal function. If taken orally, glycine increases the urinary excretion of uric acid, and is possibly a useful adjunct to gout. It is an essential intermediate in the metabolism of protein, peptides, and bile salts. Liver detoxification compounds, such as glutathione, must have glycine present for their formation.

Glycine removes heavy metals such as lead from the body, and also decreases the craving for sugar. It has been shown to calm aggression in both children and adults. When combined with GABA and glutamine, glycine influences brain function by slowing down anxiety-related messages from the limbic system. Glycine is also effective in alcohol withdrawal.

Being a very non-toxic amino acid, glycine can be used in both children and adults. It is found in high concentrations in meats and wheatgerm. Usual dosage range is 500 to 3,000mg, per day, in divided doses.


Histidine, one of the essential amino acids, is required in large amounts in infants. It is necessary for the maintenance of the myelin sheath of nerves and has vasodilating and mild anti-inflammatory properties. The neurotransmitter histamine derives from histidine. Histidine promotes large increases in brain histamine content, especially in the hypothalamus.

People with abnormally high amounts of histamine often demonstrate a history of psychiatric problems ranging from mild to severe. People with chronic pain and fibromyalgia demonstrate high histamine levels represented by joint swelling. High histidine and histamine levels are often seen in patients with obsessive-compulsive disorders, depression, and phobias. Low blood-histamine levels are found with rheumatoid arthritis and Parkinson's disease.

Best food sources of histidine include pork, wheatgerm, chicken, turkey, duck, ricotta and cottage cheese.


Lysine is an essential amino acid, and must be obtained from the diet, as it cannot be produced by the human body. Lysine is a critical protein required for growth, tissue repair; and production of hormones, enzymes, and antibodies. Additionally, it helps reduce the incidence of herpes outbreaks. The proper balance of lysine to arginine helps suppress the virus.

Symptoms of lysine deficiency include fatigue, inability to concentrate, irritability, bloodshot eyes, retarded growth, anaemia, hair loss, and reproductive problems.

Good food sources of lysine include eggs, meat, fish, milk, cheese and yeast. Amounts required for optimum health varies widely from person to person from 500 to 1,600mg per day, depending on their particular biochemistry. If outbreaks of herpes occur increase the amount to 3,000mg, daily, until the symptoms subside.


Methionine, an essential amino acid, represents one of the sulphur-containing amino acids. It is a methyl donor, critical for the formation of many important substances such as nucleic acids, epinephrine, choline, lecithin, carnitine, melatonin, collagen, serine, creatine, and deanol. Additionally, methionine can be a detoxifying agent assisting the removal of heavy metals such as lead from the body. Methionine is necessary for selenium to be absorbed and utilised. As an antioxidant, it helps protect the body from the effects of radiation. Normal metabolism of homocysteine requires vitamin B6 and methionine.

People with abnormally high amounts of histamine often demonstrate a history of psychiatric problemsExcess homocysteine can cause plaque formation in the arteries, leading to cardiovascular disease. If supplementing with methionine, always add vitamin B6 and folic acid to prevent a build-up of homocysteine. Methionine can be synthesised into cysteine, cystine, and taurine, if sulphur is present. Excess methionine has been suggested in one type of schizophrenia, while low levels are seen with depression. Supplementing with methionine helps lower histamine levels in the body, and sufferers of allergies, asthma, and chronic pain may find methionine supplementation helpful. Heroin addicts often have low pain thresholds and high histamine levels. Methionine helps lower the excess histamine levels usually present during heroin, amphetamine, or barbiturate withdrawal. In some depressed patients, methionine lifts depression with supplementation of one gram of methionine, morning and evening. Compared to MAO-inhibitor antidepressants, methionine proves more effective.

Good food sources of methionine include pork, sausage, duck, wild game, lentils, pumpkin, sesame and sunflower seeds, avocado, cottage cheese, cheese and wheatgerm.


Phenylalanine, an essential amino acid, functions as the parent substance, or precursor of tyrosine. Phenylalanine converts to tyrosine in the liver. Phenoketonurics (PKU) cannot convert phenylalanine into tyrosine because they lack the enzyme, phenylalanine hydroxylase.

Although phenylalanine is not found in the brain, it resides in many brain peptides, proteins, and neurotransmitters. Phenylalanine is the raw substance that produces several compounds of the catecholamine family responsible for the transmission of nerve impulses, assuming an adequate supply of phenylalanine. Norepinephrine, a major neurotransmitter, derives from tyrosine or phenylalanine. The amount of norepinephrine available to the brain is predisposed by the amount of phenylalanine or tyrosine available. Phenylalanine is one of the few amino acids readily converted into brain compounds like norepinephrine that control a person's mood. Phenylalanine or tyrosine helps give a positive, uplifting effect on mood, alertness, and ambition. Often, this amino acid is deficient in depressed people. Phenylalanine can also stimulate the release of cholecystokinin (CCK) that, in effect turns off the appetite.

Other phenylalanine derivatives such as epinephrine are excreted at the nerve terminals in the hypothalamus, and norepinephrine is excreted at the sympathetic nerve endings, giving rise to the fight-or-flight response. Norepinephrine is stored in presynaptic vesicles in certain central synapses. During times of stress, the body's adrenal glands are under immense pressure to produce epinephrine and norepinephrine. Often, they become low or depleted. This depletion can lead to depression and stress which can cause pain, anxiety, uncertainty and fear. Supplementing with phenylalanine or tyrosine helps to increase the level of norepinephrine in the brain. Many antidepressants work by increasing or manipulating the norepinephrine level in the brain. Often the drugs work by blocking the norepinephrine from re-entering the vesicles or pouches found at the synapse. The natural way to normalise brain levels of norepinephrine is with supplementation of tyrosine or phenylalanine. Therapeutic dosage ranges from 500 to 1,500mg per day. Phenylalanine should be used with extreme caution in hypertensive patients and should always be taken with food. People taking MAO inhibitors or tricyclic antidepressants should not use phenylalanine or tyrosine.

The DL-form of phenylalanine, or DLPA, has been found to be effective in the treatment of pain, and for depression resulting from pain. DLPA increases the production of PEA (phenylethylamine), norepinephrine, and endorphins. PEA is a neurotransmitter-type substance with a structural resemblance to amphetamine, a stimulant drug. Endorphins are the morphine-like neurotransmitters that decrease pain and gives a sense of well-being. DLPA increases endorphins by preventing their breakdown in the brain, so they remain there longer. If you use DLPA, the suggested amount is 750mg, four times daily.

Food sources of phenylalanine include dairy products such as cheese and milk, meats such as chicken, turkey, and duck; and pecans, sesame seeds, lima beans and lentils. Therapeutic dosages of DLPA range from 500 to 3,000mg per day, divided.


As a non-essential amino acid, proline is required for the formation of collagen; but vitamin C must be present. The body can manufacture proline from ornithine or glutamic acid and, if needed, convert it back into ornithine.

Elevation of proline may be found in alcoholics with cirrhosis, and in some patients with depression or seizure disorders. Convulsions, elevated blood calcium levels, and osteoporosis may be caused by excess proline from a genetic error.

Good food sources of proline include cottage and ricotta cheeses, eggs, pork, luncheon meats, wheatgerm, turkey and duck. Supplemental doses range from 500 to 1,000mg, with vitamin C.


Serine, a non-essential amino acid, is synthesised from glycine in the presence of folic acid and vitamin B6. It is involved in DNA synthesis and in combination with carbohydrates, may form glycoproteins. Serine is required for the formation of choline, ethanolamine, phospholipids and sarcosine, is necessary for the formation of neurotransmitters, and to stabilise cell membranes. Phospholipids are made from phosphatidylserine, and require the presence of methionine and folic acid. Excess serine may cause psychosis and elevation of blood pressure.

Good food sources include cottage and ricotta cheeses, wheat, wheatgerm, pork, luncheon meat, turkey, peanuts, and soya.


Taurine is now classified as a conditionally essential amino acid in the adult, but in infants and children, taurine is essential. Taurine is one of the sulphfur-containing amino acids, and in the adult is synthesised from cysteine and methionine, provided vitamin B6 and some zinc are present. Taurine is found throughout the body, abundantly in the heart muscle, olfactory bulb, central nervous system, and brain -hippocampus and pineal gland. Taurine participates in a multitude of functions in the body involving the gallbladder, brain, heart, eyes, and vascular system. In the heart, taurine is the most concentrated amino acid. It is involved in the heart muscle contractility and rhythm. After a heart attack the levels of taurine often decrease dramatically. Taurine seems to assist in cardiac heart function by acting as a diuretic and a heart stimulator with doses of two grams per day.

In the heart, taurine is the most concentrated amino acid. It is involved in the heart muscle contractility and rhythm. After a heart attack the levels of taurine often decrease dramatically Taurine proves effective in the treatment of epilepsy, acting as an anticonvulsant. Usual dosage of taurine for epilepsy is 3,000 mg per day, with a non-protein meal. A deficiency of taurine has been demonstrated in some patients with depression. A deficiency can add to chemical sensitivity and decrease the body's ability to detoxify chemicals. Taurine is necessary for the formation of one of the bile acids and for proper functioning of the gallbladder. The bile may be a route of excretion of chemicals detoxified by the body. Taurine is sometimes called upon to help control inflammation or infection.

When tryptophan intake is deficient, especially during periods of stress, serotonin levels drop, causing depression, anxiety, insecurity, hyperactivity, insomnia, and pain

Best food sources of taurine include meats and fish. The need for taurine increases whenever you experience more stress than usual or have an illness. Supplementation is necessary as the taurine need becomes greater than can be obtained from the diet. Usual dosage of taurine is 500 to 3,000mg per day, preferably on an empty stomach.


Threonine is an essential amino acid, and is the precursor to brain glycine. It is required for proper digestion and intestinal tract function. Threonine breaks down into glucose, and into the amino acids glycine and serine.

A deficiency of threonine suppresses the immune system. It has also been found helpful in multiple sclerosis cases and in some patients with agitated depression and mania. Good food sources include pork, turkey, wheatgerm, and cottage and ricotta cheeses.


Tryptophan is an essential amino acid, and must be obtained from the diet. It ultimately breaks down into serotonin, the calming neurotransmitter in the brain. Serotonin helps us feel calm, relaxed and in control.

Tryptophan is essential to maintaining the body's protein balance. When food that is protein deficient or lacking tryptophan is fed to growing or mature individuals, such foods fail to replace worn-out materials lost by the body during the organic activities of its cells, tissues, and organs. The amino acid tryptophan is exhausted by the vital activities of the body and, in turn, must be replaced to prevent atrophy of the body's structures.

One of the few substances capable of passing the blood-brain barrier, tryptophan plays a variety of important roles in mental activity. When tryptophan intake is deficient, especially during periods of stress, serotonin levels drop, causing depression, anxiety, insecurity, hyperactivity, insomnia, and pain. The body requires ample supplies of vitamin B6 for the formation of tryptophan. About 1% of ingested tryptophan is metabolised to serotonin. About 90% of tryptophan is metabolised through Knudsen acid to nicotinic acid.

Tryptophan is obtained in the diet every day. Many rich natural forms of tryptophan include: bananas, green leafy vegetables, red meat, turkey, dairy products, pineapple, avocados, eggs, soya, sesame and pumpkin seeds, and lentils. Large doses of tryptophan, when combined with niacinamide and vitamin B6, can enhance the conversion of tryptophan to serotonin.

When tryptophan intake is deficient, periods of stress, especially during depression, serotonin levels drop, causing anxiety, insecurity, hyperactivity, insomnia, and painCurrently, tryptophan is available only by prescription. It was removed from sale in 1989 because of a contaminated batch that caused EMS (esoinophiliamyalgia syndrome). The

U.S Food and Drug Administration (FDA) determined the cause was tryptophan and not the contaminated batch. It reclassified tryptophan as an unapproved experimental drug, and ordered recall of all products except where tryptophan occurred naturally. To date, tryptophan is still banned for sale in the US and UK.

But within the last couple of years, 5-HTP, or 5-hydroxytryptophan, has become available. Derived from griffonia seeds, a member of the legume family, 5-HTP is about 10 times stronger than tryptophan and is one step closer to serotonin. Suggested dosage is 50 to 300mg daily.

One study compared 5-HTP to Luvox, an antidepressant. Subjects with depression were given 100mg of 5-HTP, three times daily, or 150mg, of Luvox, three times daily. Evaluations were done at two, four, and six weeks. After two weeks, both groups reported a significant reduction in depression. By week four, 15 of 36 5-HTP patients and 18 of 33 Luvox patients reported at least a 50% improvement in depression symptoms. Final assessment demonstrated the 5-HTP patients had the greatest improvement and the least amount of treatment failures. Another study involving endogenous depression (arising from within the individual, in all likelihood genetic) demonstrated marked improvement in 69% of patients receiving 5-HTP.


Tyrosine is the first breakdown product of phenylalanine, and is considered a non-essential amino acid because the body can make it from phenylalanine. Dr Gelenberg, at Harvard Medical School, USA, determined tyrosine more effective than anti-depressants for relief of depression. The suggested amount of tyrosine is one 850mg capsule three times daily. Do not take tyrosine with MAO inhibitors or tricyclic antidepressants.


The body constantly conducts many complicated series of chemical reactions in precisely controlled ways to keep us healthy. Over 5,000 reactions occur every second in a cell. By utilising the natural substances in optimal quantities to re-establish a normal balance, you can help correct the cause of some disease processes in a non-toxic way.

Amino acid metabolism disorders are becoming recognised as a major factor in many disease processes. Amino acid testing is an analytical technique on the leading edge of nutritional biochemical medicine. It gives a new approach towards illness, and can assist patients who have not responded to treatment as expected, or who present complex cases with diverse symptoms.

Amino acid analysis of urine or plasma goes a long way towards assessing vitamin and mineral status. It measures the levels of amino acids in the body that affect many important processes. Additionally, it provides insights into the patient's functional needs for a wide variety of vitamins and minerals. Many of the enzymes which catalyse the interconversion of amino acids require vitamin and mineral co-factors to function optimally. In many cases where incomplete conversion of one product to another is due to sluggish enzymes, this indicates a functional need for increasing levels of a co-factor.

Amino acid analysis has proven helpful in treating:

•Chronic Fatigue

•Candida Infections

•Food & Chemical Sensitivities

•Immune System Disorders



•Learning Disorders

•A.D.D./ Hyperactivity

•Behavioural Disorders

•Eating Disorders




•Cardiovascular Disease




•Chronic Pain


Pyridoxal 5'Phosphate (Active B6)

Pyridoxal 5' Phosphate, or P5'P, the biological (active) form of vitamin B6 is necessary for the utilisation of all amino acids, proteins, fats, and carbohydrates. If P5'P is not present, increased excretion of most amino acids occurs as well as increased formation of abnormal amino acid metabolites. Unlike vitamin B6 there is no fear of toxicity with P5'P.


Magnesium is an essential co-factor in over 300 enzyme reactions in the body. Many individuals are deficient in magnesium, and do not get enough from their diets. Magnesium and vitamins B6, or P5’P must be present or the body cannot assimilate and use amino acids properly.


For most of the amino acids covered in this article, the therapeutic dosage and food sources are provided. Where the dosage is not stated, this indicates that the amount is variable, according to individual circumstances and needs. Where food sources are not stated, this indicates that the quantity of a particular amino acid from food sources alone is not high enough to produce a therapeutic effect.

In order to avoid biochemical imbalances, amino acid supplementation should be taken under the supervision of a nutritionist or health professional.

This article has been adapted from Healing with Amino Acids by Dr Billie J Sahley and Dr Katherine M Birkner (Pain and Stress Publications, 1998).

Billie J Sahley is Executive Director of the Pain & Stress Centre in San Antonio. She is a Board-Certified Medical Psychotherapist-Behaviour Therapist, and an Orthomolecular Therapist.

Katherine Birkner is a Pain Therapist at the Pain & Stress Centre. She is a Registered Nurse and Orthomolecular Therapist.

For further information regarding the therapeutic use of amino acids contact the Pain and Stress Centre, 5282 Medical Drive, Suite 160, San Antonio, TX 78229-602, USA. 001-800-669-2256

The Institute for Optimum Nutrition is an independent educational charity, registered charity number 1013084.

Article's Webpage


For  IUPAC (International Union of Pure and Applied Chemistry) recommendations on AA (Amino Acids) and Peptide Nomenclature go to:


* From Jungle Miami: The information provided by this website is not intended as a substitute for medical advice.

Tuesday, March 15, 2011


In light of the ordeal japanese people are going through, we thought we should go to the prestigious Scientific American Magazine and bring you the most informed opinion on the subject.

Reuters Photo

Nuclear Experts Explain Worst-Case Scenario at Fukushima Power Plant

The type of accident occurring now in Japan derives from a loss of off-site AC power and then a subsequent failure of emergency power on-site. Engineers there are racing to restore AC power to prevent a core meltdown

By Steve Mirsky
Saturday, March 12, 2011

 First came the earthquake, centered just off Japan's east coast, near Honshu. The added horror of the tsunami quickly followed. Now the world waits as emergency crews attempt to stop a core meltdown from occurring at the Fukushima Daichi nuclear reactor, already the site of an explosion of the reactor's housing structure.

BOILING-WATER REACTOR SYSTEM: The system's inverted lightbulb primary containment vents below through
pipes to a pressure-suppression torus. Once that torus breaches due to overpressure, the secondary containment is all that separates the released radioactive steam from the outside environment.


At 1:30 P.M. Eastern Standard Time on March 12, American nuclear experts gathered for a call-in media briefing. Whereas various participants discussed the policy ramifications of the crisis, physicist Ken Bergeron provided most of the information regarding the actual damage to the reactor.

"Reactor analysts like to categorize potential reactor accidents into groups," said Bergeron, who did research on nuclear reactor accident simulation at Sandia National Laboratories in New Mexico. "And the type of accident that is occurring in Japan is known as a station blackout. It means loss of off-site AC power—power lines are down—and then a subsequent failure of emergency power on-site—the diesel generators. It is considered to be extremely unlikely, but the station blackout has been one of the great concerns for decades.

"The probability of this occurring is hard to calculate, primarily because of the possibility of what are called common-cause accidents, where the loss of off-site power and of on-site power are caused by the same thing. In this case it was the earthquake and tsunami. So we're in uncharted territory, we're in a land where probability says we shouldn't be. And we're hoping that all of the barriers to release of radioactivity will not fail."

Bergeron explained the basics of overheating at a nuclear fission plant. "The fuel rods are long uranium rods clad in a [zirconium alloy casing]. They're held in a cylindrical-shaped array. And the water covers all of that. If the water descends below the level of the fuel, then the temperature starts going up and the cladding bursts, releasing a lot of fission products. And eventually the core just starts slumping and melting. Quite a bit of this happened in TMI [Three Mile Island in Pennsylvania], but the pressure vessel did not fail."

Former U.S. Nuclear Regulatory Commission (NRC) member Peter Bradford added, "The other thing that happens is that the cladding, which is just the outside of the tube, at a high enough temperature interacts with the water. It's essentially a high-speed rusting, where the zirconium becomes zirconium oxide and the hydrogen is set free. And hydrogen at the right concentration in an atmosphere is either flammable or explosive."

"Hydrogen combustion would not occur necessarily in the containment building," Bergeron pointed out, "which is inert—it doesn't have any oxygen—but they have had to vent the containment, because this pressure is building up from all this steam. And so the hydrogen is being vented with the steam and it's entering some area, some building, where there is oxygen, and that's where the explosion took place."

Bergeron discussed the specific power plant in question, the General Electric design BWR Mark 1. "This is a boiling-water reactor. It's one of the first designs ever developed for commercial reactors in this country, and it's widely used in Japan as well. Compared to other reactors, if you look at NRC studies, according to calculations, it has a relatively low core-damage frequency. (That means the likelihood that portions of the fuel will melt.) And in part, that's because it has a larger variety of ways to get water into the core. So they have a lot of options, and they're using them now—using these steam-driven turbines, for example. There's no electricity required to run these steam-driven turbines. But they still need battery electricity to operate the valves and the controls.

"So there's some advantages to the BWR in terms of severe accidents. But one of the disadvantages is that the containment structure is a lightbulb-shaped steel shell that's only about 30 or 40 feet [nine to 12 meters] across—thick steel, but relatively small compared to large, dry containments like TMI. And it doesn't provide as much of an extra layer of defense from reactor accidents as containments like TMI [do]. So there is a great deal of concern that if the core does melt, the containment will not be able to survive. And if the containment doesn't survive, we have a worst-case situation."

And just what is that worst-case scenario? "They're venting in order to keep the containment vessel from failing. But if a core melts, it will slump to the bottom of the reactor vessel, probably melt through the reactor vessel onto the containment floor. It's likely to spread as a molten pool—like lava—to the edge of the steel shell and melt through. That would result in a containment failure in a matter of less than a day. It's good that it's got a better containment system than Chernobyl, but it's not as strong as most of the reactors in this country."

Finally, Bergeron summed up the events so far: "Based on what we understand, the reactor has been shut down, in the sense that all of the control rods have been inserted—which means there's no longer a nuclear reaction. But what you have to worry about is the decay heat that's still in the core—that will last for many days.

"And to keep that decay heat of the uranium from melting the core, you have to keep water on it. And the conventional sources of water, the electricity that provides the power for pumps, have failed. So they are using some very unusual methods of getting water into the core, they're using steam-driven turbines—they're operating off of the steam generated by the reactor itself.

"But even that system requires electricity in the form of batteries. And the batteries aren't designed to last this long, so they have failed by now. So we don't know exactly how they're getting water to the core or if they're getting enough water to the core. We believe, because of the release of cesium, that the core has been exposed above the water level, at least for a portion of time, and has overheated. What we really need to know is how long can they keep that water flowing. And it needs to be days to keep the core from melting.

"The containment, I believe, is still intact. But if the core does melt, that insult will probably not be sustained and the containment vessel will fail. All this, if it were to occur, would take a matter of days. What's crucial is restoring AC power. They've got to get AC power back to the plant to be able to control it. And I'm sure they're working on it."


Scientific American is a trademark of Scientific American, Inc.
© 2011 Scientific American, a Division of Nature America, Inc.


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You can look for and track down the most effective charities here.

Donate here

American Red Cross.

Monday, March 7, 2011

Do you suffer from back pain?

The stats are staggering. 85% of the US population suffers from back or neck pain at some point in their lives.  We  found this interesting article on  the subject. This is Jungle  Miami 's post today.

Is Your Ab Workout Hurting Your Back?


June 17, 2009

The genesis of much of the ab work we do these days probably lies in the work done in an Australian physiotherapy lab during the mid-1990s. Researchers there, hoping to elucidate the underlying cause of back pain, attached electrodes to people’s midsections and directed them to rapidly raise and lower their arms, like the alarmist robot in “Lost in Space.”

In those with healthy backs, the scientists found, a deep abdominal muscle tensed several milliseconds before the arms rose. The brain apparently alerted the muscle, the transversus abdominis, to brace the spine in advance of movement. In those with back pain, however, the transversus abdominis didn’t fire early. The spine wasn’t ready for the flailing. It wobbled and ached. Perhaps, the researchers theorized, increasing abdominal strength could ease back pain. The lab worked with patients in pain to isolate and strengthen that particular deep muscle, in part by sucking in their guts during exercises. The results, though mixed, showed some promise against sore backs.

From that highly technical foray into rehabilitative medicine, a booming industry of fitness classes was born. “The idea leaked” into gyms and Pilates classes that core health was “all about the transversus abdominis,” Thomas Nesser, an associate professor of physical education at Indiana State University who has studied core fitness, told me recently. Personal trainers began directing clients to pull in their belly buttons during crunches on Swiss balls or to press their backs against the floor during sit-ups, deeply hollowing their stomachs, then curl up one spinal segment at a time. “People are now spending hours trying to strengthen” their deep ab muscles, Nesser said.

But there’s growing dissent among sports scientists about whether all of this attention to the deep abdominal muscles actually gives you a more powerful core and a stronger back and whether it’s even safe. A provocative article published in the The British Journal of Sports Medicine last year asserted that some of the key findings from the first Australian study of back pain might be wrong. Moreover, even if they were true for some people in pain, the results might not apply to the generally healthy and fit, whose trunk muscles weren’t misfiring in the first place.

“There’s so much mythology out there about the core,” maintains Stuart McGill, a highly regarded professor of spine biomechanics at the University of Waterloo in Canada and a back-pain clinician who has been crusading against ab exercises that require hollowing your belly. “The idea has reached trainers and through them the public that the core means only the abs. There’s no science behind that idea.” (McGill’s website is

The “core” remains a somewhat nebulous concept; but most researchers consider it the corset of muscles and connective tissue that encircle and hold the spine in place. If your core is stable, your spine remains upright while your body swivels around it. But, McGill says, the muscles forming the core must be balanced to allow the spine to bear large loads. If you concentrate on strengthening only one set of muscles within the core, you can destabilize your spine by pulling it out of alignment. Think of the spine as a fishing rod supported by muscular guy wires. If all of the wires are tensed equally, the rod stays straight. “If you pull the wires closer to the spine,” McGill says, as you do when you pull in your stomach while trying to isolate the transversus abdominis, “what happens?” The rod buckles. So, too, he said, can your spine if you overly focus on the deep abdominal muscles. “In research at our lab,” he went on to say, “the amount of load that the spine can bear without injury was greatly reduced when subjects pulled in their belly buttons” during crunches and other exercises.

Instead, he suggests, a core exercise program should emphasize all of the major muscles that girdle the spine, including but not concentrating on the abs. Side plank (lie on your side and raise your upper body) and the “bird dog” (in which, from all fours, you raise an alternate arm and leg) exercise the important muscles embedded along the back and sides of the core. As for the abdominals, no sit-ups, McGill said; they place devastating loads on the disks. An approved crunch begins with you lying down, one knee bent, and hands positioned beneath your lower back for support. “Do not hollow your stomach or press your back against the floor,” McGill says. Gently lift your head and shoulders, hold briefly and relax back down. These three exercises, done regularly, McGill said, can provide well-rounded, thorough core stability. And they avoid the pitfalls of the all-abs core routine. “I see too many people,” McGill told me with a sigh, “who have six-pack abs and a ruined back.”

Copyright 2011 The New York Times CompanyPrivacy 620 Eighth Avenue New York, NY 10018
Well blog The New York Times.

Tuesday, March 1, 2011

A Metabolic Tune Up. Do you need one?

Today's Jungle Miami publishes an article written by Dr. Mark Hyman. It gives us the lowdown on our Metabolism/ Enjoy it.

ARE YOU TIRED and worn out? Do you have sore muscles, fatigue, and brain fog? If so, you might have metabolic burnout!

Imagine if you could find a way to tune up your metabolism, increase your energy levels, think clearly, and feel less achy.

Imagine if you could prevent diabetes, heart disease, Parkinson’s disease, and dementia.

Imagine if you could heal fibromyalgia and chronic fatigue syndrome.

Imagine if you could get to the roots of aging, slow the whole process, and eliminate most age-related diseases.

These aren’t just fantasies.

All these things are possible–if you give yourself a metabolic tune-up.

You might have heard of the rats fed high doses of resveratrol, the plant compound found in red wine. But did you know that those rats lived 30 percent longer than their peers — the equivalent of an additional 120 human years — even though they ate a bad diet?

In fact, they even became fitter and lost weight even while eating a poor quality, standard American diet.

How could they eat high amounts of bad food and not exercise, yet still become fitter AND live 30 percent longer than the average rat?

One word: MITOCHONDRIA — the source of your energy.

The resveratrol protected and improved the function of the mitochondria through its effects on special master aging genes.

So what are mitochondria and what do they have to do with having more energy, losing weight, and living to be 120 years old without any disease?

Today you will learn the answer to that question. And I will provide you with eight tips you can start using today to give yourself a metabolic tune-up and boost your energy metabolism.

The key to more energy lies in providing your mitochondria with the right environment to thrive. When you do, you can boost your energy metabolism. (This is actually step number six of the 7 Keys to UltraWellness, and it is absolutely essential if you want to obtain optimal health. Find out more here.)

So let’s look at what mitochondria are and what they do.

What Are Mitochondria?

Mitochondria are the little factories in our cells that take the foods we eat and the oxygen we breathe and convert them into energy. That energy is called adenosine triphosphate, or ATP, and it is used to support every function in our body.

When the mitochondria are damaged, you suffer all the symptoms of low energy–fatigue, memory loss, pain, rapid aging, and more.

Each cell holds hundreds or thousands of mitochondria; they are found in greater amounts in active organs and tissues such as the muscles, heart, and brain. In fact, we have more than 100,000 trillion mitochondria in our bodies, and each one contains 17,000 little assembly lines for making ATP.

Why are these are these little energy factories so important to your health?

The answer is simple: Mitochondria are the place where metabolism happens.

When your mitochondria aren’t working properly, your metabolism runs less efficiently or can practically shut down.

Problems occur because these powerful energy producers are VERY sensitive to damage.

And when they are damaged, you suffer all the symptoms of low energy–fatigue, memory loss, pain, rapid aging, and more.

Fatigue is the most common symptom of poorly functioning mitochondria, and it is the reason we tend to poop out as we age. We add constant insult and injury to our mitochondria, and this causes them to break down and stop producing energy.

The main way your mitochondria are damaged is by uncontrolled oxidative stress. That may sound complicated, but in reality we are all familiar with “oxidative stress” even if some of us don’t know what the term means.

Oxidation is the rust on our cars, the brown color that appears on an apple when cut and exposed to air, the rancid vegetable oil in our cupboards, even the wrinkles that form on our skin.

What most of us don’t realize is that our own tissues are rusting, our own fats are going rancid, and our brains are melting as we go about our daily life.

What starts this process is some insult — too many calories, smoking, a sunburn, exposure to toxins, anti-nutrients, sugar, and more — that tips the balance, starting a chain reaction of cellular and tissue damage that leads us down the long road to weight gain and chronic illness.

For a healthy metabolism eat less processed food, junk food, sugar, and empty calories. In fact, you should really avoid these things altogether.

The ultimate outcome of oxidative stress and the resultant loss of energy is death! But the good news is that we can counteract the damage by giving ourselves a metabolic tune-up.

Let me explain …

What Is a Metabolic Tune-up?

Dr. Bruce Ames, a renowned scientist from the University of California, Berkeley, has spent the last decade discovering how we can give ourselves a metabolic tune-up.

In one study, he gave two compounds to old rats who were tired, wouldn’t get on their treadmill or swim very far, and couldn’t find the cheese in the maze. These compounds make mitochondria run better, boosting metabolism.

They are alpha-lipoic acid and acetyl-L-carnitine.

Overnight, these old rats became young rats. They got onto the treadmill, swam long distances without fatigue, and could easily find the cheese in the maze, just like their young, healthy counterparts.

How could that happen?

Well, Dr. Ames simply gave the cells the raw materials they need for optimal function. That’s it!

You can do this too, and the process is very simple …

First, find the things that damage your metabolism and mitochondria, then eliminate them.

Second, give your body the things that help mitochondria function optimally.

Here’s how you do that.

Eight Tips for Giving Yourself a Metabolic Tune-up

The first step to giving yourself a metabolic tune-up is locating and eliminating the causes of damage to the mitochondria:

■Eat less processed food, junk food, sugar, and empty calories. In fact, you should really avoid these things altogether.

■Detoxify by getting rid of environmental and internal toxins.

■Cool off the inflammation in your body.

■Balance your hormones.

Once you’ve done that, you need to boost your mitochondrial function and provide the mitochondria with the correct environment to thrive:

■Try interval training, which increases the efficiency and function of your mitochondria, and strength training, which increases the amount of muscle and the number of mitochondria.

■Eat whole, real, colorful plant food. That’s eight to 12 servings of fresh vegetables, fruits, beans, nuts, seeds, and whole grains every day. These foods are full of antioxidants and phytonutrients.

■Take mitochondria-protective and energy-boosting nutrients such as acetyl-L-carnitine, alpha-lipoic acid, coenzyme Q10, N-acetyl-cysteine, NADH, D-ribose, resveratrol, and magnesium aspartate.

■Increase your intake of omega-3 fats to help build your mitochondrial membranes.

Taking care of your mitochondria and giving yourself a metabolic tune-up will allow you to increase your energy, lose weight, and age well. It is a cornerstone of creating lifelong vibrant health.

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