Amino Acids and Kidney Disease

Amino acids and kidney disease are inextricably linked. There is no circumstance in which the judicious use of dietary essential amino acids can provide more unique benefit than kidney disease.

Amino acids and kidney disease are inextricably linked. The kidneys are responsible for excreting metabolic waste products, including urea and ammonia, which are the end products of amino acid metabolism. Kidney disease is characterized by the failure to effectively clear these and other compounds from the blood.

Many individuals have a degree of kidney disease. Approximately 60% of people over the age of 65 have some impairment in renal function. This gradual decline in kidney function is called chronic kidney disease (CKD) or chronic renal failure and affects over 30 million Americans. The biggest risk factors for developing renal disease are high blood pressure, cardiovascular disease, insulin resistance, and diabetes, all of which put excess stress on the narrow blood vessels in the kidneys.

Monitoring Kidney Health

Kidney health is typically measured by looking at the GFR (glomerular filtration rate), which is a measure of how well the kidneys are filtering toxins from the blood. As part of a blood test a doctor will measure the kidneys’ ability to handle the waste product creatinine in what is called the creatinine clearance rate, and from this, the doctor can measure the rate at which blood is being filtered through the kidneys. The National Kidney Foundation recommends that GFR tests be performed regularly as part of an annual physical exam since early detection can help stop the progression of the disease.

Kidney Failure and Muscle Loss

In addition to causing massive oxidative stress that can result in a cardiovascular event such as a heart attack, kidney failure induces the stress response, and by association, loss of muscle mass and strength. The onset of the stress response is brought about in part by inflammation, as well as hormonal responses, including elevations in cortisol and epinephrine. In addition, the accumulation of urea and ammonia acidifies the blood, which has a direct inhibitory effect on muscle protein synthesis and can cause metabolic acidosis. The result is a profound loss of muscle mass and strength that has many unfavorable consequences.

Kidney Failure and Protein Intake

When kidney function is adequate, excreting the urea and ammonia produced from the metabolism of dietary protein intake is not an issue. In fact, it is well established that high-protein intake does not cause kidney failure when kidney function is normal. Unfortunately, with kidney failure, dietary protein has to be limited because of the impaired secretion of urea and ammonia.

Anabolic resistance—the compromised ability of the body to build muscle protein—is difficult to overcome in any circumstance but is particularly problematic when it comes to kidney disease. It would seem logical that the most effective dietary approach to anabolic resistance would be to consume a high-protein diet because protein metabolism fuels muscle protein synthesis. However, consumption of large amounts of dietary protein increases urea and ammonia production due to the metabolism of the absorbed amino acids that are not incorporated into protein. This is a high metabolic price to pay since anabolic resistance minimizes the effectiveness of protein intake.

Consequently, a low-protein diet is usually recommended for chronic kidney disease patients. While a protein-restriction diet minimizes the amount of urea and ammonia in the blood, in the setting of anabolic resistance a low-protein diet accelerates the rate of muscle loss. Because the importance of maintaining muscle mass is becoming much more widely appreciated, many experts in kidney disease are torn between the traditional recommendation for CKD patients to eat a low-protein diet and the adverse effects a low-protein diet has on muscle mass and function.

Essential Amino Acids and the Kidney

There is no circumstance in which the judicious use of dietary essential amino acids can provide more unique benefit than kidney disease. A brief overview of the relationship between amino acids and the kidney should make clear the role of dietary essential amino acids in lessening the devastating loss of muscle mass and function that normally occurs with kidney disease.

Muscle protein is in a constant state of turnover—protein is being broken down and releasing the component amino acids into the cell (protein breakdown), while at the same time cellular amino acids are being incorporated into new protein (protein synthesis). Part of the process of muscle protein turnover also involves the release of amino acids into the blood. While some of those amino acids released by muscle are taken up by other tissues and organs and incorporated into protein, others travel to the liver for metabolism, resulting in the production of urea and ammonia. The balance between protein synthesis and breakdown is determined by the rate of these various processes that are all occurring simultaneously.

The free amino acids in muscle cells are derived from blood, protein breakdown, or, in the case of the nonessential amino acids, production from other amino acids. In turn, cellular amino acids may be incorporated into protein or released into the blood in their original form. Additionally, they may be partially metabolized, and the nitrogen transferred to form the nonessential amino acids glutamine and alanine.

Glutamine and alanine are the major vehicles that transport nitrogen from muscle to the liver, where the nitrogen is then converted to urea and ammonia and released into the blood. The blood is filtered by the kidneys to selectively clear both urea and ammonia so they can be excreted in urine.

Dietary essential amino acids stimulate the synthesis of new muscle protein. Since nonessential amino acids make up approximately half of muscle protein, and consumption of an essential amino acid dietary supplement does not include the nonessential amino acids, the production of complete muscle protein requires that nonessential amino acids be derived in part from protein breakdown. As a result, nonessential amino acid concentrations, including alanine and glutamine, are reduced when you take an essential amino acid supplement. This imparts a positive effect on individuals with chronic renal insufficiency because a release of alanine and glutamine into the blood from muscle is correspondingly reduced. As a result of reduced flux of alanine and glutamine to the liver, the production of both urea and ammonia are lowered, which greatly helps uremic patients.

Thus, essential amino acid consumption stimulates muscle protein synthesis while lessening the burden on the kidney to excrete urea and ammonia. The devastating effect of the combination of anabolic resistance and reduced protein intake can be overcome with essential amino acids.

The relationships between muscle protein and amino acid metabolism, urea production in the liver, and urea excretion by the kidney are shown in the figures below. (Ammonia is not shown because it contributes much less than urea to the flux of nitrogen in the body.)

Amino acids and kidney disease are inextricably linked. The kidneys are responsible for excreting metabolic waste products, including urea and ammonia, which are the end products of amino acid metabolism. Kidney disease is characterized by the failure to effectively clear these and other compounds from the blood.

Since kidney disease necessitates a reduction in protein intake to minimize the burden of ammonia and urea on the kidneys, supplemental essential amino acids are even more important in kidney disease than in other catabolic states. The dosage should, therefore, be greater than in other circumstances to maintain a healthy nutritional status, and the supplement must contain all the essential amino acids and not just the branched-chain amino acids. Two 15-gram doses per day of essential amino acids are reasonable.

A Case Study

A noteworthy Johns Hopkins study published in the journal Kidney International confirmed the unique influence amino acids have on kidney disease, specifically on serum albumin levels. Your liver makes the protein albumin to help keep fluid in your bloodstream from leaking into other tissues.

Of the 47 patients studied, 29 were on hemodialysis and 18 were on peritoneal dialysis. On hemodialysis, the waste is filtered directly from the blood, and on peritoneal dialysis, toxins are removed through a soft tube in the abdominal wall that is replaced several times a day.

Patients were randomly prescribed either 5 amino acid capsules or 5 placebo capsules with meals 3 times a day for 3 months. Serum albumin levels were taken at the end of each month.

The hemodialysis patients who took the amino acid supplements had a 0.22 g/dl increase in serum albumin levels, but the peritoneal dialysis patients only had an average increase of 0.01 g/dL.

“We hope that this increase in serum albumin will result in better health and increased survival for patients treated with hemodialysis,” says Joseph A. Eustace, M.D., lead author of the study and an instructor of medicine at Hopkins.

By making sure the protein needs of CKD patients are met with amino acid supplements, secondary conditions such as metabolic acidosis, bone disease, and insulin resistance can be better prevented.

Amino Acids and Protein Nutrition for Cancer Cachexia

Virtually all forms of cancer induce a condition called cachexia, a weakening and wasting away of the body during serious illness. The effects of cancer cachexia have become recognized as a major factor in determining the effectiveness of cancer therapy and ultimately mortality. Amino acids are an important nutritional therapy for combating cancer cachexia.

There are many forms of cancer, each with specific and unique characteristics. However, virtually all forms of cancer induce a condition called cachexia, a weakening and wasting away of the body during serious illness. The effects of cachexia have become recognized as a major factor in determining the effectiveness of cancer therapy and ultimately mortality.

What Is Cachexia?

A consensus of experts defined cachexia as follows: “Cachexia is a complex metabolic syndrome associated with underlying illness and characterized by loss of muscle with or without loss of fat mass.”

Cachexia has two components:

  1. A loss of appetite that reduces food intake.
  2. Metabolic changes in the body that render normal nutrition ineffective.

The result is malnutrition and loss of lean tissue, which is mostly muscle. Malnutrition and loss of lean muscle tissue in cancer patients has a number of detrimental effects:

Virtually all forms of cancer induce a condition called cachexia, a weakening and wasting away of the body during serious illness. The effects of cancer cachexia have become recognized as a major factor in determining the effectiveness of cancer therapy and ultimately mortality. Amino acids are an important nutritional therapy for combating cancer cachexia.

Every single one of these consequences can impair a patient’s ability to recover from cancer. A study published in 2013 in the Journal of Clinical Oncology sought to determine the degree to which muscle loss contributes to cancer mortality. Results showed that regardless of weight, patients who were cachexic (with involuntary weight loss, muscle depletion, and low muscle attenuation) had a “poor prognosis.” Patients who maintained more lean muscle mass survived lived nearly two years longer.

A 2017 study determined that low muscle mass and muscle attenuation contribute to a poor outcome for metastatic breast cancer patients. Is it possible to do anything about the devastating effects of cancer cachexia on muscle?

To determine the treatment, we must first understand what causes the onset of cachexia. Unfortunately, at a molecular level, scientists don’t know fully understand the precise mechanisms. However, we do understand that at the physiological level, nutritional therapy is the key to tackling cancer cachexia.

The Stress Response in Cancer

Cancer places the body under physiological stress. As a result, appetite is reduced and food intake falls. During the stress response there is a greater need than ever for amino acid nutrition. Amino acids are needed to produce new proteins that can help battle cancer, such as proteins involved with immune function, as well as proteins in tissues and organs such as the liver and brain whose uninterrupted function is necessary for survival.

Nonessential amino acids can be produced in the body, but the nine essential amino acids cannot be produced in the body. Since there is no reservoir of amino acids in the body, muscle protein starts to break down at an accelerated rate to maintain a steady supply of both nonessential and essential amino acids for the other tissues and organs.

Muscle is the primary tissue that can afford to lose some of its protein mass without affecting normal physiology. However, the stress response is adaptive for only a few days—continued loss of muscle protein for longer than that will begin to adversely affect many normal physiological responses. Thus, the continued loss of muscle protein at an accelerated rate is the physiological basis for the development of cancer cachexia.

What Is the Conventional Treatment for Cancer Cachexia?

Cancer scientists have been searching for a treatment for cancer cachexia for many years but have yet to produce a successful solution. The most current recommendations for treatment of cancer cachexia come from the European Society of Parenteral and Enteral Nutrition (ESPEN). These recommendations focus on the early diagnosis of nutritional risk. They also recommend the use of a variety of nutritional interventions, decreasing inflammation, and increasing physical activity.

Unfortunately, there may be significant problems to implementing the ESPEN recommendations. Increased activity is the most effective way to reverse muscle protein breakdown, but the cancer patient usually does not feel like doing a lot of activity. Reducing inflammation with nutrients such as omega-3 fatty acids is useful for mild cases, but the level of systemic inflammation in cancer cachexia is so great that dietary approaches often have little impact. Further, suppression of appetite in cancer cachexia limits how much adequate nutrition can actually be consumed. It is often necessary to provide nutritional support via tube feeding or even providing nutrition intravenously. In addition, the normal effectiveness of dietary protein in reversing the breakdown of muscle protein is limited in cancer cachexia.

Anabolic Resistance and Cancer Cachexia

Anabolic refers to building up muscle. Normally dietary protein is anabolic, because it stimulates the production of new muscle protein. In cancer cachexia the muscle is resistant to the normal anabolic effect of dietary protein (a condition called anabolic resistance). For example, a study published in Clinical Nutrition showed that feeding a normal nutritional supplement containing protein, carbohydrate, and fat designed specifically for cancer cachexia was completely ineffective in stimulating the production of new muscle protein.

The problem in anabolic resistance is that the molecular machinery in the muscle that must be activated to initiate the process of protein synthesis is in an inactive state and cannot be activated by normal nutrition. A high dose of the amino acid leucine, on the other hand, can activate these intracellular factors. When a high dose of the essential amino acid leucine was added to the nutritional supplement in the study described above, the nutritional supplement became an active stimulator of muscle protein synthesis.

Essential Amino Acids and Muscle Protein Synthesis

The effectiveness of a nutritional supplement for cancer cachexia spiked with leucine can be further enhanced by using a balanced mixture of essential amino acids to stimulate muscle protein synthesis. A balanced mixture of essential amino acids with a relatively high proportion of leucine not only activates the initiation of muscle protein synthesis, but also provides all the amino acids necessary for synthesis of muscle protein, since there are ample nonessential amino acids available already. Essential amino acids have the great advantage in this circumstance of being effective in a very small amount. A dose of essential amino acids as small as 3 grams can effectively stimulate muscle protein synthesis, thereby reversing the loss of muscle protein.

Do Essential Amino Acids Stimulate Tumor Growth?

The notion that providing nutrition to cancer patients feeds the tumor and accelerates growth has been kicked around for more than 40 years. Studies done on mice support this perspective, as feeding mice specific amino acids can stimulate tumor growth. However, one must be extremely cautious extrapolating results from mice to humans. Experimental cancer in mice usually involves the implantation of tumors that become much larger, relative to body weight, than any tumor in humans. Further, mice have very little muscle. Thus, a big tumor without much muscle means that the tumor is not getting all the amino acids it needs from muscle protein breakdown for optimal growth.

Therefore, dietary amino acids can stimulate tumor growth in mice. Mice don’t accurately reflect the response in humans. In humans, muscle mass is large relative to tumor load, so muscle protein breakdown provides the tumor with all the amino acids necessary for rapid growth. Consequently, dietary protein will not stimulate tumor growth (the tumor is already getting all the amino acids it needs), but rather the absorbed amino acids will start to replete the muscle protein that has been lost due to the cachexia response.

Essential Amino Acid Supplementation for Cancer Patients

The rapid loss of muscle mass in cancer cachexia contributes directly to mortality and should be treated nutritionally. Because of anabolic resistance and decreased appetite, normal dietary intake is generally insufficient to combat the rapid loss of muscle. Consuming dietary supplements containing essential amino acids, including a relatively high dose of leucine, is a reasonable approach to slowing the rate of muscle protein loss.

Grow Older Gracefully with Anti-Aging Amino Acids

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

When it comes to aging, there’s one thing we know for sure—it happens. As for the exact mechanisms behind it, there are many theories. One theory is that our genes determine our longevity and how the aging process plays out in our lives. Other aging experts believe aging is the result of accumulated DNA and cellular damage over time—all those UV rays, free radicals, and destructive oxygen compounds taking their toll on skin, heart, brain, and overall health. Chances are, there are myriad contributors to aging. And there are also many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to ensure you remain vital and vibrant as you grow older.

How Anti-Aging Amino Acids Rejuvenate Your Skin, Connective Tissues, and More

Often, the skin is the first place where unwanted signs of aging appear. Aging shows up on the skin first as fine lines, then as wrinkles. As we approach our 30s, our skin becomes drier. In our 40s, the aging process can begin to accelerate. Not only can your skin become markedly thinner while losing firmness and elasticity, but you may also begin to experience hair loss, thinning and weakening of the nails, and degradation of the connective tissue that allows your joints to function.

Anti-aging amino acids can help maintain smoothness and elasticity of the skin, strengthen connective tissue, and keep nails strong and hair lush.

If you’re seeking amino acid anti-aging supplements, you should pay particular attention to these six important amino acids: creatine, arginine, lysine, glutamine, alanine, and cysteine.

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

The Relationship Between Collagen and Amino Acids

Before delving into the specifics of how each of these amino acids can help you grow older gracefully, let’s explore the  relationship between collagen and amino acids, which is central to their anti-aging properties.

Amino acids form the protein collagen. Collagen makes up our bones, tendons, cartilage, connective tissues, and skin. It’s what keeps wrinkles away and, alongside elastin, supports skin elasticity.

When collagen production tapers off, as it does with age, our skin sags and succumbs to wrinkles, our joints and ligaments become less pliable and more stiff and sore, and our hair starts to thin. Certain amino acids can help increase collagen production, which in turn can suppress unwanted symptoms of aging.

While several amino acids are involved in boosting collagen production, glycine and proline are the two amino acids that make up collagen (along with the amino acid derivative hydroxyproline made from proline and lysine). Together, glycine and proline account for two-thirds of collagen protein. However, proline and glycine are nonessential amino acids that are rarely limiting for collagen synthesis. The limiting amino acid is the amino acid that is in shortest supply in relation to need. The rate of protein synthesis—how much collagen can be produced—is limited to the availability of the least abundant amino acid. Typically, the essential amino acids are rate limiting, even when they comprise a relatively small amount of the total amino acids in the protein.

Our Paleothic ancestors got plenty of glycine and proline because they ate pretty much all the components of meat, but these days, we tend to leave out the bones and tendons. Bone broth is a great way to increase your intake of these two amino acids. Bone broth is also a great source of arginine. While it is a good idea to ensure that your diet includes proline and glycine, keep in mind that healthy skin requires an abundance of all the essential amino acids to trigger the synthetic response in skin collagen.

The Top 6 Anti-Aging Amino Acids

1. Creatine

Creatine is made from three amino acids: arginine, methionine, and glycine. It is an important energy source for cells and can help stimulate the repair of cells and connective tissue. Creatine also plays a key role in skin metabolism.

As we age, collagen production and skin cell division decline at a steady rate. After age 20, collagen production decreases by 1.5% every year, and from 30 onwards our bodies’ ability to produce collagen and elastin, the proteins that give structure, strength, and elasticity to skin, is greatly limited. Whereas skin cells used to renew every 28 days, by the time we reach our 40s, skin cell turnover happens every 30 to 40 days.

Creatine helps skin cells repair damaged DNA and stimulates cells to produce more collagen and elastin. It also wraps cells in a film of water, thereby helping to shield cells from harmful substances as well as supplying much-needed moisture.

2. Arginine

The conditionally essential amino acid arginine occurs naturally in the human body, but production diminishes over time. This means that if you wish to continue to reap the benefits of this powerful amino acid, it can be quite helpful to incorporate arginine-rich supplements into your wellness  routine.

Arginine aids in the synthesis of protein and improves collagen production. At a cellular level, it helps cells to divide properly and ensures they don’t suffer premature apoptosis (cell  death). Arginine also offers a natural way to help revitalize human growth hormone.

Human growth hormone (hGH) is best known for helping the body build lean muscle mass and burn fat. Studies show it can also help elevate bone density, improve cardiovascular health, and boost collagen production in those with deficient levels. Increased levels of human growth hormone can be a boon for those who wish to preserve the youthful appearance of their skin, as research indicates it can increase skin elasticity and reduce the appearance of fine lines and age spots.

Human growth hormone injections are a mainstream medicine approach to increasing hGH levels, but they are expensive, inconvenient, and many experts recommend against the use of this synthetic approach as an anti-aging treatment.

Arginine acts as an hGH secretagogue, which is a substance that triggers the pituitary gland to release more human growth hormone. According to a 2010 scientific review published in the Journal of Advanced Research: “The demonstrated anti-aging benefits of L-Arginine show greater potential than any pharmaceutical or nutraceutical agent ever previously discovered.”

3. Lysine

Lysine, an essential amino acid that we must get from our diet, functions as a foundational building block for many of the proteins that make up the muscles and other internal structures. Because it’s not naturally produced by the human body, lysine must be obtained from a balanced diet or from supplements.

Lysine is arguably one of the most essential components in any nutrient-based approach to growing older healthily as it works to combat both internal and external damage associated with the aging process.

By ensuring adequate lysine intake, we increase the body’s production of carnitine, a specialized amino acid that plays a vital role in energy production by converting fatty acids to usable energy forms. In doing so, it helps lower cholesterol levels and stimulate collagen production. Lysine also contributes to the production of elastin, which alongside collagen, keeps skin looking firm and fresh.

High levels of arginine, however, may lower lysine levels in the body because the two aminos share common pathways, which is why taking arginine supplements can lead to unwanted side effects. When taking anti-aging amino acid supplements, it’s crucial to supplement with a complete essential amino acid formula that maintains the balance of amino acids in the blood. Working together in an appropriate balance, arginine and lysine have been shown to boost human growth hormone levels.

4. Glutamine

Glutamine, a nonessential amino acid, is the most abundant amino acid in the human body. A multitude of health benefits can be attributed to glutamine, including forming the cells that line the small intestine as well as those that form the immune system, contributing to the production of other amino acids, and functioning as metabolic fuel to power cells throughout the human body. As with arginine, however, glutamine production naturally declines with age, making supplementation beneficial. Increasing your glutamine intake can also help you weather periods of stress, during which the body craves more glutamine.

Glutamine gives skin its strength, elasticity, and firmness, and when levels start to diminish, skin starts to sag and wrinkle. By eating a glutamine-rich diet—plenty of kale, plain yogurt, walnuts, fish, turkey, spinach, lima beans, and whey protein—you can promote flexible, strong muscle tissue and skin. If you’re not getting enough glutamine, your body will take it from muscle and skin tissues.

If the load of your diet is meat or you drink a lot of coffee or smoke, you may be suffering from an acid imbalance, which can harm cells and tissues. Glutamine can help regulate the acid-base balance of your body by flushing out poisonous ammonia that is a byproduct of the kidneys’ filtering process. Glutamine lends a proton to an ammonia molecule. An acid is neutralized and an alkalizing bicarbonate is preserved.

5. Alanine

Though alanine, a nonessential amino acid, can be readily synthesized by the human body, adding supplemental alanine can increase the anti-aging benefits you experience.

Alanine helps to clear toxins released by muscle protein breakdown from the bloodstream, regulates glucose and cholesterol levels, and serves as an important energy source for the muscles and central nervous system. It’s second only to glutamine when it comes to concentrations in the blood.

The primary anti-aging benefits of alanine have to do with its ability to interfere with the glycation process. This process damages collagen, so by disrupting it, alanine protects the body’s natural stores of collagen.

Alanine also supports the process by which muscle tissue rebuilds itself, reduces fatigue, and improves sugar metabolism.

6. Cysteine

Cysteine is a nonessential amino abundant in beta-keratin, a major protein that makes up your hair, skin, and nails. Beta-keratin, in turn, is a rich source of sulfur. Connective tissue and cartilage depend on sulfur bonds for structure and stability. We’ve already explained how age decreases flexibility and firmness in skin and joints, and a lack of sulfur is a common culprit in these age-related symptoms.

One of the most important roles of cysteine is as a component of the antioxidant glutathione, which is used throughout the body to neutralize free radicals, diminish oxidative stress, and protect the immune system.

Cysteine and glutathione help to defend against age-related health conditions that have been linked to an accumulation of toxins, such as dementia and multiple sclerosis.

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

Amino Acids vs. Protein Powder: Who’s the Victor?

Amino acid powder supplements offer potential advantages compared to protein powder supplements. While amino acids are the victor in the amino acids vs. protein powder debate, it’s not really an either/or situation. Whey protein and amino acids can work synergistically to produce superior results.

Amino acid powder supplements offer potential advantages compared to protein powder supplements in several respects.

  1. Amino acid mixtures can be formulated exactly as desired. Precise mixtures of amino acids can be produced that target specific metabolic issues. Dietary proteins are made up of a range of amino acids including both essential amino acids and nonessential amino acids. Consequently, intact protein supplements, such as whey protein powder, cannot target a specific amino-acid related metabolic response.
  2. Free-form amino acids can be completely absorbed more rapidly than any intact protein, including whey protein. When you ingest a mixture of free-form essential amino acids, the corresponding peak concentrations are higher and are achieved more rapidly.

What’s the Best Boost for Muscle Protein Synthesis?

Whey protein is a “fast” protein, which means it is digested and absorbed very rapidly compared to other dietary proteins. But free-form amino acids surpass the absorption characteristics of even the fastest protein. The result is that the metabolic response to free amino acid supplements often surpasses the maximal effect that can be achieved with intact protein such as whey, and often with a smaller dose.

The figure below illustrates the advantages of supplementing with free-form essential amino acid mixtures when it comes to spiking muscle protein synthesis. Participants supplemented with three different doses of a balanced mixture of all the free-form essential amino acids (3.6 grams, 6.7 grams, and 15 grams). Researchers then compared the results to those produced by15 grams of whey protein and to a partial essential amino acid mixture of only branched-chained amino acids (BCAAs). An amino acid powder supplement formulated with all essential amino acids is the clear muscle protein synthesis booster.

Amino acid powder supplements offer potential advantages compared to protein powder supplements. While amino acids are the victor in the amino acids vs. protein powder debate, it’s not really an either/or situation. Whey protein and amino acids can work synergistically to produce superior results.

We can see how the increase in muscle protein synthesis is more responsive to essential amino acids. The ratios of essential amino acids in amino acid powders can also be optimized. A properly formulated essential amino acid supplement can be three times as effective as a whey protein powder supplement.

While essential amino acids are more potent than whey protein, there are advantages to combining aminos with whey as part of a muscle-building amino acid powder supplement. Whey protein is digested over a longer time frame than free-form essential amino acids, and (as far as intact proteins go), has a good balance of essential amino acids (about 45% of the total). When you consume whey protein with essential amino acids you prolong the beneficial effects of the aminos. So, while amino acids are the victor in the amino acids vs. protein powder debate, it’s not really an either/or situation. Whey protein and amino acids can work synergistically to produce superior results.

A Word of Caution on the Labeling of Protein Supplement Products

The discerning customer knows what he or she wants, but the information provided about a product is often limited to the label on the package. Unfortunately, labels can range from uninformative to downright deceptive. For example, it is not unusual for “pure whey protein” to contain as little as 60% of calories as whey protein, with the balance of calories being comprised of carbohydrate and fat. The lesson is this: Buyer beware! Don’t just buy on the basis of product name. Dig deep into what the product actually provides.

Another labeling issue of considerable concern is how to figure out the relative proportions of different proteins in a protein mixture. Most supplements include some whey protein, as it is widely accepted as one of the highest quality proteins. However, because of cost and certain characteristics, other proteins are often included, such as soy and collagen. Labeling rarely includes the proportion of each protein. Consequently, the true protein quality of some supplements is uncertain. Ingredients are listed in order of descending quantity, so the first ingredient listed is ideally a high-quality protein such as whey.

Finally, it is the right of consumers to get what the product promises. Often, this is not the case. Spot-checking of nutritional supplements has revealed that the actual contents do not always match the labelling. There can be ingredients lurking in protein supplement products that aren’t even listed on the label. For this reason, it is advisable to only buy supplements whose contents have been certified by an independent source, such as US Pharmacopeia, or to at least check the website of the producer to determine if they have the appropriate certifications. This issue is of particular concern for athletes who could be unwittingly consuming banned substances. Numerous cases of positive tests for banned substances have occurred because an ingredient was included in a supplement but not mentioned in the packaging. Although the industry has been making progress in cleaning up this problem, it still persists. Protein supplements are not regulated by the Food and Drug Administration, so the responsibility falls on the consumer to deal only with reputable suppliers.

Amino Acids for Insomnia: What Causes Those Restless Nights and Tips for Sweet Sleep

If you’re like many other adults, you’ve spent more than one night tossing and turning with sleeplessness. Insomnia impacts energy level, mood, and health. Amino acids can be helpful in treating insomnia.

If you’re like many other adults, you’ve spent more than one night tossing and turning with sleeplessness. According to the American Sleep Association, 30% of American adults have occasional insomnia, while 10% have chronic insomnia. Although many of us think that insomnia is just a side effect of modern life, poor sleep can lead to a number of health conditions, including heart disease, colon cancer, obesity, diabetes, stroke, and dementia. Thankfully, however, amino acids may be all you need to get the restful sleep you’ve been craving. So if you’re curious to learn how amino acids for insomnia can help you get a good night’s sleep, you’ve come to the right place.

What Causes Insomnia?

Insomnia is the most common sleep disorder in the United States. While many people experience occasional episodes of acute insomnia, which may last days or weeks, some deal with chronic insomnia, which may last for a month or more.

Whether acute or chronic, insomnia can be caused by a number of different factors, from an imbalance in brain chemicals to other sleep disorders, such as sleep apnea. In addition, conditions like anxiety and depression as well as lifestyle factors, such as watching television before bed, using stimulants like nicotine or caffeine, or sleeping in a room that’s too hot or cold, can all cause insomnia.

Additional factors that can increase your risk of insomnia include:

  • Stress: When you’re under stress, it can be difficult to fall asleep and stay asleep. Moreover, the release of stress hormones can make it difficult to reach restorative deep sleep, which can leave you feeling even more stressed when you wake up.
  • Poor sleep habits: Napping, getting into bed at a different time each day, and using your bed for working, eating, or computer or cell phone activity can all lead to insomnia.
  • Eating before bed: Eating a large meal before bed can make you feel too uncomfortable to fall asleep or cause acid reflux, which can lead to insomnia. Likewise, eating high-carbohydrate foods can cause a quick surge of energy when you need to be winding down. So if you eat anything before bed, it should be a light, protein-rich snack that stabilizes your blood sugar and doesn’t fill you up.
  • Sleep pattern disruptions: Disturbances to your circadian rhythm, or sleep-wake cycle, caused by odd work schedules or travel that takes you across time zones can lead to insomnia.
  • Medical conditions: Health problems like chronic pain, cancer, diabetes, heart disease, and asthma can all lead to symptoms of insomnia.
  • Medications: Certain medications, such as antidepressants, medications for asthma and high blood pressure, and over-the-counter cold and allergy medications that contain stimulants, may lead to insomnia.

Many people with insomnia rely on sleeping pills to fall asleep. However, these types of medications can have negative side effects, including daytime grogginess and an increased risk of falling. And getting into the habit of using conventional sleep aids to get to sleep every night brings with it a very real risk of addiction, which can make insomnia even worse.

However, supplying the body with the nutrients it requires can support a healthy sleep-wake cycle and help you get the better sleep you need.

Amino Acids for Insomnia

Amino acids are known as the building blocks of life because we must have them to create the proteins our bodies use for almost every biological process. And some amino acids have been found to be especially effective at creating the conditions necessary for healthy sleep. These are:

  • Gamma-aminobutyric acid (GABA)
  • L-theanine
  • L-tryptophan
  • Glycine


GABA is an amino acid that also acts as the primary inhibitory neurotransmitter of the central nervous system. This inhibitory action means that GABA is helpful in aiding relaxation and shortening the time it takes to fall asleep. In fact, a 2008 study found that levels of GABA are approximately 30% lower in people with insomnia.

In addition, a study from 2010 demonstrated that a combination of GABA and 5-hydroxytryptophan (5-HTP)—an amino acid that acts as a precursor of serotonin, a neurotransmitter that plays a role in both mood and sleep—can reduce the time it takes to fall asleep and increase both sleep quality and the amount of sleep achieved.

And if you’re interested in raising levels of GABA on your own, try exercising. A 2013 study found that vigorous exercise leads to increased levels of GABA, which helps explain why exercise is known to improve sleep.


L-theanine is an amino acid that was first discovered in green tea in 1949. Like all amino acids, L-theanine works in concert with other amino acids, and it’s known to increase levels of GABA—as well as the neurotransmitters serotonin and dopamine. A 2019 study found that a combination of GABA and L-theanine works better than either alone to reduce sleep latency and improve duration of sleep. In addition, GABA and L-theanine were found to significantly increase both rapid eye movement (REM) and non-REM sleep.


Like 5-HTP, the amino acid L-tryptophan also functions as a precursor of serotonin. Moreover, L-tryptophan is converted in the body into 5-HTP, which is then converted into serotonin. Interestingly, studies have shown that 5-HTP crosses the blood-brain barrier at a higher rate than L-tryptophan and may be even more effective as a dietary supplement.

Part of serotonin’s role in sleep has to do with the fact that it acts as a precursor of melatonin—the hormone that helps regulate your sleep-wake cycle. When levels of both serotonin and melatonin are low, sleep suffers. By increasing levels of serotonin in the brain, amino acids like 5-HTP and tryptophan help increase feelings of well-being and regulate sleep.

Studies have also shown that L-tryptophan can induce a state of subjective sleepiness and decrease the time it takes to fall asleep. And a study from 2018 found that L-tryptophan is not only helpful for sleep but can also aid conditions as diverse as autism, heart disease, chronic kidney disease, depression, inflammatory bowel disease, and multiple sclerosis.


Like GABA, glycine acts as an inhibitory neurotransmitter and plays a role in promoting sleep. However, glycine has the added benefit of lowering body temperature, which makes falling and staying asleep easier.

In addition, a 2012 study found that glycine can significantly reduce fatigue and sleepiness in people experiencing sleep deprivation. Moreover, similar to 5-HTP and L-tryptophan, glycine helps increase serotonin levels and correct circadian rhythm disorders.

If you’re suffering from insomnia and interested in avoiding the potential side effects and risks inherent in pharmaceutical approaches and would like to begin a program of amino acid supplementation instead, it’s important to be aware that amino acids work best when used as part of a balanced formula that contains all essential amino acids.

So be sure to look for a supplement that provides a balanced supply of all essential amino acids while also emphasizing amino acids for insomnia. In this way, you’ll be providing your brain with the fuel it needs to create the perfect conditions for optimal sleep.

It’s also a good idea to remember that insomnia may be a sign of a more serious medical condition, so if your symptoms get worse or don’t improve, speak with your health care provider about additional treatment options.

Amino Acids for Insomnia: What Causes Those Restless Nights and Tips for Sweet Sleep

How Many Grams of Amino Acids Do You Need a Day?

When it comes to how many grams of amino acids you need in a day the dose is generally referred to in gram amounts. How the body responds to essential amino acids depends on how many grams it gets. A dose of as little as 3 grams can stimulate muscle protein synthesis significantly.

When determining how much of a nutrient you need a day, it is customary to consider macronutrients in the diet (protein, carbohydrates, and fats) as a percent of total caloric intake. But when it comes to how many grams of amino acids you need in a day the dose is generally referred to in gram amounts. The number of calories in a pure essential amino acid (EAA) supplement, for instance, is insignificant in the context of total caloric intake, and for this reason supplements are generally sold in gram (g) units.

The Standard 3-Gram Dose

How the body responds to EAAs depends on how many grams it gets. A dose of as little as 3 grams can stimulate muscle protein synthesis significantly. Consuming a 3-gram EAA supplement can generate almost 6 grams of muscle protein—the perfect balance of EAAs enables the muscle to incorporate every single one of the EAAs into protein.  The body also reuses readily available nonessential amino acids to contribute to the total amount of protein produced.

While a 3-gram dose can be effective over time, the amount of muscle protein made from that small dose is limited to the amount of EAAs consumed relative to the size of the muscle mass. While the production of 6 grams of muscle protein from 3 grams of EAAs is impressive, it is not a large amount of new muscle protein when compared with total muscle mass. Muscle mass can range from 25-80 pounds depending on your gender, size, and body type. Certain EAA benefits, such as the anti-inflammatory effects, are immediately activated with a dosage of 3 grams, but it will take some patience before you see the benefits in terms of muscle size and strength—at least a month of regular consumption, preferably twice per day, to achieve noticeable gains in muscle mass and function.

The Maximum 15-Gram Dose

The amount of muscle protein produced in response to EAA intake increases linearly up to a dose of 15 grams. Quite simply, a bigger dose will give you a bigger response, but more than 15 grams is unnecessary. Also, as long as you wait at least one hour after one dose before taking another dose, you will get the same response to each of the multiple doses in one day.

So, there is a big range of possible doses of EAAs. The appropriate dose depends on your desired results, and how fast you want to achieve them. If you are on the smaller side and are seeking to support muscle health, a basic dose of 3 grams is reasonable. For example, a petite woman of around 100 pounds with about 30 pounds of muscle will get a robust response and over time see positive effects with a 3-gram dose of EAAs. A young healthy man who weighs 200 lbs and has a muscle mass of about 80 pounds would be better off with a 6-gram dose of EAAs. (A 3-gram dose would be just 0.008% of the muscle mass, so 6 grams would be more appropriate in order to account for the larger muscle mass.) Two doses per day, between meals, is optimal, but you will still get beneficial effects if you only take one dose per day.

The important point to keep in mind is that EAAs are required nutrients with many roles in the body beyond acting as components of muscle protein. A small dose of 3 grams can have beneficial effects in a number of respects in addition to building muscle, so even a large muscular man will benefit from a small dose. The activities in which one participates, and the desired results from the EAA supplement, are probably more important than a person’s size or physical makeup.

How to Take EAAs

EAAs can be consumed either as powder dissolved in water, as capsules, as a beverage, or a combination of all three. EAA supplements usually contain amino acids and some flavoring. It is common that about 20-25% of the weight of a supplement is flavoring. When determining the right EAA dose for you, be sure you are using the weight of the active component of the mixture (i.e, the EAAs), and you are not including the weight of the flavoring. If you are using a supplement that has a mixture of free EAAs and protein, add the EAA component of the protein to the amount of free EAAs to determine the dose you are consuming. For example, if you are using a supplement containing 3 grams of free EAAs and 1.5 grams of whey protein you’re consuming approximately 4.5 grams of EAAs, since whey protein is roughly 50% EAAs.

If you are taking EAA supplements because your regular diet falls short in meeting the recommended intake of high-quality protein, then, in addition to the between-meal doses, I recommend taking supplements with your meals to enhance the physiological effectiveness of the consumption of the incomplete protein food sources in your diet. The dosage with meals to make up for dietary deficiencies depends on how far short your diet falls of the goal intake of high-quality protein. In the case of a vegan diet, this could be up to 15 grams of EAAs with each meal to obtain optimal results.

Optimal nutritional supplementation with EAAs will help maintain an adequate supply of amino acids in the blood throughout the day to support various physiological functions without the interruptions that normally occur when food is not being absorbed. Best results are therefore obtained by taking an EAA supplement twice per day, between meals or before going to bed.

If you are still unsure how many grams of amino acids you personally need in a day, don’t worry about it. The beauty of essential amino acids is that there are no known adverse responses to a balanced formulation of EAAs, so you don’t have to be concerned that you are taking too much. A very small dose has proven benefits for stimulating muscle protein synthesis, so you likewise don’t need to worry that you are taking too small of a dose to elicit beneficial results. The recommended dosages are meant as guidelines; if you find successful results with a different dose, stick with it.

The Effect of Protein and Amino Acids on Bone Health

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein. Dietary protein and amino acids are as important for bone building as they are for muscle building.

A large part of our lean body mass is the skeleton, which includes all the mineralized bones and the structural and mechanical support of cartilage and tendons.

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein (20-30%!). Therefore, it is logical that dietary protein and amino acids are as important for bone building as they are for muscle building.

Similarities Between Muscle and Bone

There are many similarities between muscle and bone in terms of the way they function and the purposes that they serve. Just as muscle is a reservoir for amino acids that circulate in the blood and replenish other body proteins and chemicals, bone is the storage form for calcium and phosphorous, two minerals that are vitally important for many of the chemical reactions that occur in the body.

As with amino acids, the blood level of these minerals is tightly controlled and there is a complex system involving hormones and other chemical messengers to regulate the release and uptake of calcium and phosphorus from bone. This continual “remodelling” is analogous to muscle protein turnover, although a bit slower. It takes approximately ten years for the entire bone mass to turn over.

Another similarity between muscle and bone is the “use it or lose it” paradigm. Just as muscle atrophies with lack of physical activity, bone also weakens and loses density without mechanical stress and weight-bearing activity.

What Are Bones Made Of?

Unlike the bleached white, hollow, rock-hard bone you see on the anatomy lab skeleton, living bone contains connective tissues (such as the endosteum or periosteum), a network of nerves and blood vessels, with the marrow at the center. If you think about what bones are put through in the course of daily activities (in particular, sports or vigorous physical labor) then it makes sense that bones need to be very strong and somewhat flexible.

Bone is made of crystals of mineral bound to protein, a composite which provides both strength and resilience. Collagen, assembled as a structure of long thin rods that contain three intertwined protein chains, makes up a good amount of bone protein. Calcium and phosphate combine (termed hydroxyapatite) and then bind in an orderly manner to the collagen matrix. Other proteins in bone provide additional strength and also play a role in binding minerals during bone formation.

Of the 30% of bone composed of organic compounds, 90-95% is collagen. Individual collagen molecules contain three polypeptides of about 1000 amino acids per chain with a high glycine and hydroxyproline content. The amino acids arginine and methionine are also important cartilage-forming substances.

As with muscle, having all the amino acids (essentials aminos, in particular) available in the correct balance is important for optimal bone development and maintenance. Amino acids also influence bone metabolism indirectly due to their role in the synthesis of growth hormones and growth factors that are involved in bone development and remodelling.  

The Importance of Amino Acids to Bone Health

Protein and amino acids are clearly important nutrients for bone health. Despite the solid evidence supporting this statement, there is a lot of misinformation out there regarding the relationship between dietary protein (animal proteins in particular) and bone health.

Early studies showed that higher intakes of dietary protein were associated with increases in urinary calcium excretion. It was further proposed that animal proteins, rich in sulfur-containing essential amino acids, could “acidify” the blood, thereby leaching calcium from the bone to neutralize the acid. While this theory is still widely disseminated, particularly by proponents of plant proteins, the science has long since explained and moved beyond the long-standing dogma that animal protein consumption results in a mild acidosis promoting the increased excretion of calcium. The original investigators set out to determine the source of the increased calcium and found that the higher protein intake actually increased absorption of calcium in the diet, and that the increased excretion of calcium in the urine merely reflected that increase in calcium uptake.   

This observation helped to explain why, in other studies looking at people’s level of protein intake and bone status, there always appeared to be a beneficial effect of higher protein intake on bone health. In fact, in a different study in which women were fed dietary protein at and below 0.8 g/kg (the RDA), the low protein intake was associated with a reduction in intestinal calcium absorption and a condition called hyperparathyroidism. Secondary hyperparathyroidism occurs when the calcium level is abnormally low, so the parathyroid gland secretes more hormone to try to increase calcium blood levels. The long-term consequences of these low-protein diet-induced changes in mineral metabolism are not known, but such a diet could be detrimental to skeletal health. Recent epidemiologic studies demonstrate reduced bone density and increased rates of bone loss in individuals habitually consuming low protein.

Optimizing the Musculoskeletal System

It is important to recognize that the bones, joints, and muscles are the key parts of an integrated musculoskeletal system. The relationship between muscle and bone is essential for modelling and remodelling, processes that increase bone strength and mass.

We know that weight-bearing exercises serve to increase not only muscle strength but also bone strength, and even obesity or a high body weight provides a direct mechanical force on bones.

Osteoporosis is usually a concern as individuals age and the maintenance of adequate bone strength and density with aging is highly dependent on the maintenance of adequate muscle mass and function. Interestingly, from a diet and exercise perspective, many of the same factors that build strong muscles; amino acids, dietary protein, insulin growth factor, and testosterone, also positively affect bone. Strategies to optimize muscle mass, strength, and function provide the same benefits to bone.

Bones thrive on nutrient-dense diets and healthy physical activity.  Here are some specific strategies to optimize bone health.

  1. Calcium is obviously vital for bone health but so are some other mineralsmagnesium and phosphorus in particular.  
  2. Vitamin D is essential for proper bone growth and remodeling. Other trace nutrients that play a role in bone metabolism include copper, boron, iron, zinc, vitamin A, vitamin K, vitamin C, and B vitamins.
  3. Dietary protein and essential amino acids are extremely important for bone health and density since they are part of the building material for living bones.
  4. Low-protein diets and insufficient essential amino acids can also indirectly weaken bones by altering hormones that are responsible for regulating the retention and loss of calcium from bones.
  5. Weight-bearing exercise (running, tennis, basketball, etc.) helps develop strong bones. The mechanical force stimulates bones to grow denser.
  6. Resistance exercise makes not just strong muscles but also strong bones. The torque placed on the bone from the muscle pulling on it stimulates the bone to grow bigger and denser.
  7. Family history is a factor in your risk for osteoporosis. While we can’t change our genetic makeup, we can double down on healthy lifestyle behaviors during “peak bone-building years” (teens and young adulthood) to optimize bone mass and lay in good reserves for later on in life.

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein. Dietary protein and amino acids are as important for bone building as they are for muscle building.

Amino Acids for Weight Loss: Boost Your Metabolism!

We all know the importance of diet and exercise for weight loss. There is, unfortunately, no magic weight-loss pill. There are, however, some pretty miraculous organic compounds that prime your body for weight-loss and help boost your metabolism. Amino acids for weight loss are a safe and natural way to support your weight-loss efforts.

We all know the importance of diet and exercise for weight loss, as well as a sustained commitment to losing weight and keeping it off. There is, unfortunately, no magic weight-loss pill that can shed the pounds and keep them off for good. There are, however, some pretty miraculous organic compounds that prime your body for weight-loss and help boost your metabolism. Amino acids for weight loss are a safe and natural way to support your weight-loss efforts.

Boost Your Metabolism

Our bodies are constantly burning carbohydrates, fats, and proteins to provide the energy for all the reactions that are continuously ongoing, 24 hours a day. The sum total of the energy utilized by all these reactions is called the basal metabolic rate.

The basal metabolic rate refers to the rate of energy production when you are inactive and not absorbing food. The best time to determine your basal metabolic rate is when you are sleeping. The same basic metabolic functions that determine the basal rate of energy expenditure also proceed when you are active. During the day, your total metabolic expenditure is the sum of your basal rate (which occurs continuously) and the energy you expend throughout your daily activities. When weight-loss promos and articles feature the appealing words “boost your metabolism,” they are really just saying “increase your basal metabolic rate.”

Here’s how it works: if your basal metabolic rate doesn’t match the calories you eat in a day, you will lose weight. Expressed differently, if you can rev up your basal metabolic rate (i.e., boost your metabolism), you will lose weight even if you maintain the same caloric intake. Great news for those of us who don’t want to have to eat fewer calories.

There are two major contributors to the basal metabolic rate.

  1. Reactions involved in maintaining a proper balance between sodium and potassium levels in the blood and inside the cell, and reactions that use energy, such as making glucose.
  2. The energy cost of protein turnover. It is difficult to do much about the first, but you can definitely increase the rate of protein turnover and boost your metabolism.

What Is Protein Turnover?

The thousands of proteins in your body are continuously being produced and degraded. That’s protein turnover!

Energy, in the form of ATP, fuels protein turnover—both the process of tearing protein down and the process of building protein back up. Anywhere from one-third to one-half of our basal energy production is used to fuel protein turnover. The exact amount of energy used for protein turnover depends on how much muscle you have (the amount of protein in the rest of the body is pretty constant between individuals) and how fast muscle protein is turning over.

The most effective way to boost your metabolism is to increase your muscle mass. A 10-kilogram difference in muscle mass, with everything else constant, is about a 35,000-kcal difference in energy expenditure over a year. Since about 3,500 kcal is stored in 1 pound of fat, a 35,000-kcal difference in energy expenditure translates to a gain or loss of 10 pounds of fat over a year. As we age, we inevitably lose muscle mass and put on fat. It’s easy to see why when we do the math!

What Is the Best Way to Build Muscle Fast and Increase Muscle Protein Turnover?

Exercise and protein/essential amino acid intake are the best ways to build muscle fast. Exercise increases muscle protein turnover for many hours post workout, and can, over a period of time, help you build muscle mass. However, don’t expect major changes in muscle mass from exercise alone—you must increase the amount of protein and essential amino acids you consume to significantly affect mass.

Increasing dietary protein/essential amino acid (EAA) intake is the key to boosting your basal metabolic rate. Doing so will stimulate muscle protein turnover and increase muscle mass over the long term.

Dietary protein, and EAAs in particular, stimulate muscle protein turnover in two respects.

1. Supplementing your diet with EAAs has been shown to increase the basal rate of muscle protein turnover. More energy is used to fuel the increase in muscle protein turnover, thereby giving a persistent “boost” to your metabolism. Check out the results in the figure below.

We all know the importance of diet and exercise for weight loss. There is, unfortunately, no magic weight-loss pill. There are, however, some pretty miraculous organic compounds that prime your body for weight-loss and help boost your metabolism. Amino acids for weight loss are a safe and natural way to support your weight-loss efforts.

2. The second aspect of increased dietary protein and EAA intake boosting your metabolism is their influence on diet-induced thermogenesis.

Your metabolic rate goes up about 10% for a couple of hours after you eat a meal containing dietary protein or you consume an EAA supplement. The amount of increase depends on how much protein you eat with the meal or how many grams of EAAs you take. This response has been studied for many years and is called diet-induced thermogenesis.

Diet-induced thermogenesis refers to energy lost as heat after you eat protein. Diet-induced thermogenesis is only activated by dietary protein or EAAs, as neither dietary carbohydrate nor fat have much effect on metabolic rate. When you consume dietary protein or an EAA supplement, your metabolic rate increases because energy is used to digest the protein and absorb the resulting amino acids. A meal containing dietary protein or an EAA supplement increases the metabolic rate by stimulating the rate of protein synthesis in the body, particularly in muscle, since the process of synthesis requires energy.

Diet-induced thermogenesis of dietary protein actually lessens the caloric impact of protein. Calories are classically determined by combusting the food source in a device that measures the energy released. In the case of protein, 4 kcal/g of protein are normally released by combustion, so the caloric-equivalency of protein is traditionally 4 kcal/g. In other words, you can calculate how many protein calories are in a meal by multiplying the grams of protein by 4 kcal/g. However, since the digestion of protein increases metabolic rate approximately 10%, the net caloric intake from the protein component of the meal is actually 10% less than determined by the traditional approach, or 3.6 kcal/g.

Why not just stimulate diet-induced thermogenesis with dietary protein? Because consuming EAAs increases protein turnover more than any dietary protein can, and therefore EAAs have a greater impact on diet-induced thermogenesis. Take a look at the following figure.

EAAs require less work in the intestines to be absorbed, so it may take less energy for the body to digest EAAs than it does for the body to digest intact protein on a gram-per-gram basis. Even so, EAAs stimulate protein synthesis about three times more than intact protein does, and, therefore, cause a greater increase in diet-induced thermogenesis.

Why Use EAAs to Boost Metabolism Rather than Drugs?

The stimulation of protein synthesis by the ingestion of EAAs is an entirely natural biological process without any known adverse effects. Long-term consumption will result in an increase in muscle mass and other health benefits, including a boost to your metabolism, not possible with drug therapy.

Are You Getting Enough Sulfur?

Sulfur is the 3rd most copious mineral in the body, hanging out mostly in our bones, skin, and muscles. According to a recent review, a significant proportion of the population isn’t getting enough sulfur, especially seniors. In this article we’re helping you up your sulfur intake.

After calcium and phosphorus, sulfur is the third most abundant mineral element in the body, with large amounts (almost half) located in the bones, skin, and muscles. Sulfur is an integral component of a wide variety of processes, from protein synthesis to cartilage maintenance to detoxification. And a deficiency in the mineral has even been linked to heart disease and diabetes. So if you’ve never given much thought to this important substance, maybe it’s time you started asking yourself if you’re getting enough sulfur.

Where Do We Get Sulfur?

The majority of the sulfur in our bodies comes from dietary protein, yet only 2 of the 20 amino acids normally present in protein actually contain sulfur. One of these sulfur-containing amino acids—or sulfur amino acids, as they’re also known—is methionine, which can’t be synthesized in the body and has to be supplied through the diet. And while the other amino acid, cysteine, can be synthesized in the body, the process requires a steady supply of sulfur.

The rest of the sulfur our bodies use comes from inorganic sulfates, such as iron sulfate, chondroitin sulfate, glucosamine sulfate, and magnesium sulfate (Epsom salts), and the organic sulfur found in foods like broccoli, garlic, and kale. In addition, it’s estimated that we obtain approximately 10% of the sulfur in our diets from our drinking water.

Sulfur’s Role in the Body

Sulfur plays an important role in the human body and is required for literally hundreds of physiologic processes. For example, sulfur helps give shape to proteins and thus determine their function—as in the case of the keratin that makes up hair, skin, and nails. Likewise, it’s also critical for the integrity of cartilage and other connective tissues.

Sulfur is required for the formation and proper functioning of enzymes—the catalysts for nearly all chemical reactions within cells. Without sulfur, various functions, including digestion and metabolic processes, would be compromised.

Sulfur is necessary for the conversion of thiamine and biotin and the synthesis of glutathione, which is considered the body’s master antioxidant, as it regenerates other antioxidants. In addition, glutathione is important for boosting the immune system and preventing the damage caused by reactive oxygen species, such as free radicals.

What’s more, sulfur is a vital component of proper insulin function and glucose metabolism and plays a role in preventing diabetes.

Causes of Sulfur Deficiency

According to a review published in the journal Nutrition & Metabolism, a significant number of Americans suffer from a deficiency of sulfur. Although this study focused mainly on older adults, who often eat less and consume fewer sources of protein, sulfur deficiency is thought to be widespread.

This is because modern farming practices have resulted in the depletion of sulfur in the soil, which has, in turn, led to reduced sulfur content in many of the foods we eat.

The combination of sulfur depletion in the soil, decreased consumption of protein, reliance on processed foods, and the destruction of sulfur compounds through the cooking process can result in the perfect recipe for a sulfur deficiency. In addition, our bodies can store only limited amounts of sulfur, and we need to replenish our stores daily.

Taken together, the possibility of a sulfur deficiency is real for many of us. And such a deficiency may:

Getting Enough Sulfur Through Diet and Supplementation

While the probability is great that many—if not most—of us lack sufficient levels of sulfur, it’s possible to increase our intake through both our diets and the use of dietary supplements.


One of the best ways to make sure you’re getting enough sulfur is to ensure you’re eating a wide variety of sulfur-rich foods. Good sources of dietary sulfur include:

Meat Seafood
Eggs  Sweet potatoes
Poultry Dairy products
Asparagus Broccoli
Cauliflower Cabbage
Coconut Bananas
Watermelon Nuts
Tomatoes Wheat germ
Avocados Bok choy
Brussels sprouts Onions
Kale Garlic


Due to the depletion of sulfur in our soils, dietary sources of sulfur may still be inadequate to meet the body’s needs. Fortunately, sulfur can be obtained through supplementation as well.

Perhaps the most popular form of supplemental sulfur is methylsulfonylmethane, or MSM. Touted for its ability to reduce symptoms of chronic inflammation and aid in pain relief, MSM has been shown in studies to be beneficial in the treatment of arthritis.

In one study, MSM was demonstrated to improve pain and physical function in people with arthritis. And in another study, a combination of MSM and glucosamine sulfate was shown to significantly improve signs and symptoms of arthritis.

As discussed earlier, one of the principal sources of sulfur is the essential amino acid methionine, which must be obtained from the diet. In addition to increasing sulfur intake, this amino acid also promotes the formation of collagen and cartilage and has anti-inflammatory, antioxidant, and analgesic properties.

Methionine is also essential for the absorption and bioavailability of selenium and zinc. Moreover, it aids in the detoxification and removal of heavy metals such as lead and mercury and helps the liver metabolize fats.

Another excellent source of sulfur is N-acetylcysteine (NAC)—a modified form of cysteine. Like cysteine, NAC aids glutathione synthesis. It may also be helpful in treating chronic obstructive pulmonary disease (COPD) and other respiratory disorders due to its ability to thin bronchial mucus.

In addition, NAC has shown benefit in the treatment of addictions, compulsive behaviors, and mental illnesses like schizophrenia and bipolar disorder.

Interestingly, you can also boost your body’s sulfur levels by taking an Epsom salt bath 2 to 3 times a week. As mentioned earlier, Epsom salts are composed of magnesium sulfate—an inorganic form of sulfur—and soaking in a bath of these salts is an effective way of absorbing sulfur.

Another way to ensure you’re getting sufficient sulfur is by making certain you’re spending some quality time in the sun. Believe it or not, when your skin is exposed to the sun—without sunscreen—sulfur is produced in the form of vitamin D and cholesterol sulfate.

Sulfur is one of the most important substances in the body, yet it receives very little attention, and depleted soils, processed foods, and cooking help ensure that most people are probably deficient in this vital mineral.

So if you’re concerned about a lack of sulfur in your own diet, make sure you’re eating plenty of sulfur-containing foods, and consider supplementation when necessary.

Can Amino Acids Cause Weight Gain?

Is it possible that amino acids cause weight gain? Let’s explore this question and see if we can find the answers you seek.

When you ingest amino acids—the building blocks of protein—your body uses them to make both enzymes and proteins as demands require. Any leftover amino acids then follow various metabolic pathways. Some are converted into glucose and used as energy. Others become glycogen and are stored in the liver and muscle tissue for future energy use. And still others are turned into fat and stored in fat cells. But is it possible that amino acids cause weight gain? Let’s explore this question and see if we can find the answers you seek.

Amino Acids Are Low in Calories

Amino acids contribute 4 calories for every gram of protein you consume. Which means if you take 4 grams of an amino acid supplement, you’re consuming only 16 calories. Moreover, beneficial effects of essential amino acid supplements have been demonstrated with doses less than 4 grams. So if you’re worried about the number of calories in your diet, you can choose to supplement with a simple 4-gram, 16-calorie dose.

You also get amino acids from the dietary protein you eat. However, the calorie load from dietary protein intake is significantly higher. For example, let’s say you choose to get your 4 grams of essential amino acids from a high-quality whole food source such as pasture-raised meat. In this case, you’ll be getting an extra 100 calories a day compared with the 16 calories you would be getting from the amino acid supplement.

However, when it comes to weight gain, it’s important to monitor the number of calories you’re ingesting and compare that to what your body needs. To determine how many calories you should eat each day based on your sex, height, and activity level, you can use this online calculator, which is based on the Mifflin-St Jeor equation for estimating calorie requirements.

Amino Acids for Fat Loss

Far from causing weight gain, amino acids can actually help boost the production of hormones that burn fat and promote weight loss. One such hormone is the growth hormone somatotropin (STH). STH activates protein synthesis—and therefore muscle building—as well as fat burning.

Studies show that obese and overweight individuals tend to have low concentrations of STH. However, certain amino acids have been shown to increase levels of STH, most notably arginine, methionine, and glutamine.

Moreover, a 2011 study published in The Journal of Nutrition that focused on middle-aged adults from East Asian and Western countries showed that individuals with a higher intake of branched-chain amino acids (BCAAs) have a lower prevalence of obesity and are not as overweight.

Researchers attributed this effect to the BCAA leucine—which can increase energy expenditure and thereby decrease both body weight and body fat—as well as the ability of BCAAs to lessen the effects of insulin resistance and improve glucose tolerance (the measure of how well your body processes blood sugar).

So Do Amino Acids Cause Weight Gain?

After examining the evidence, my answer to this question would have to be no. I don’t think amino acids will cause you to gain weight unless you eat too much protein—such as excessive amounts of animal protein or whey protein powders, protein shakes, or other types of protein supplements, which can be high in calories—and don’t burn off the excess amino acids.

However, I do think amino acids will help you maintain and even build muscle tissue. And this may cause moderate weight gain because muscle weighs more than fat. But that would still leave you with a better body composition, improved body mass index (BMI), and leaner, more toned figure. And who’s going to argue with that?

I don’t think amino acids cause weight gain, unless you are eating an ultra-high-protein diet and not burning off the excess amino acids. I do think amino acids are helping you maintain and build muscles, which may cause moderate weight gain, but a better body mass index (BMI) and leaner, more toned figure.