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.

The Best Animal Sources of Essential Amino Acids

What are the best animal sources of amino acids? Not all animal products contain the same amount of protein—and different cuts of the same meat contain different amounts of amino acids. Each tissue may have a different amino acid composition, determined by the specific function of the organ.

Animal products are the best sources of protein because they contain all the nine essential amino acids: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. For this reason, they are called complete proteins.

Amino acids form proteins, and our bodies need proteins to survive and thrive because they are involved in most biological processes. Protein gives structure and strength to the muscles, tendons, tissues, and organs in our bodies. The amount of protein that we need depends on our weight. For example, per kilogram of body weight for an adult, the recommended protein intake is 0.8 grams daily.

Not all animal products contain the same amount of protein—and different cuts of the same meat contain different amounts of amino acids. Each tissue may have a different amino acid composition, determined by the specific function of the organ.

In the journal The Amino Acid Composition of Animal Tissue Protein, the author presents the results of a study undertaken to determine the quantity of 10 amino acids in six soft organs of beef and the muscle tissues of a variety of cold and warm-blooded animals. The experiment analyzed the amino acid composition of the protein mixtures of 10 muscle meats (beef, veal, lamb, pork, chicken, turtle, codfish, salmon, frog legs, and shrimp) and six beef organ tissues (liver, kidney, brain, heart, stomach, and lung). The results show that these various classes of animals do not differ widely in their amino acid composition—the only significant difference was found in the presence of lysine. The organs, while showing some similarity to the muscle tissue in composition, show low lysine contents. This study highlights the importance of eating a varied diet of both animal- and plant-based protein to ensure adequate consumption of dietary amino acids.

Dietary Amino Acids

So, what are the best animal sources of amino acids?

Beef

Beef is an excellent source of protein, but different cuts have different quantities of amino acids and saturated fat. The way the animals are raised impacts the nutritional quality of the meat, so steer clear of industrially raised livestock and opt for grass-fed animal sources. The different parts of the cow also have different flavors; some of them are more tender and flavorful, others are quite tough. Round and back leg are the leanest cuts of beef, and they are perfect grilled. Lean cuts of beef provide about 31 grams in each 3-ounce serving—fattier cuts of meat are lower in protein per gram. Hindquarters have a similar amount of protein and saturated fat content, but should be marinated overnight for enhanced flavor. Beef derived from the lower loin is also low in fat and a good source of protein, but can be very tough.

Different cuts of beef not only have differing amounts of protein, but they also differ in terms of the digestibility. Digestibility determines how much of the protein in beef actually gets into the body.  For example, the digestibility of ground beef is greater than that of flank steak. The quality of a protein food source depends not only on the protein and essential amino acid content, but also on the digestibility of the protein.     

Pork

Pork is another good source of protein, but certain cuts contain a significant amount of fat. The leanest cuts of pork are found in the hindquarters and the lower half of the pig—ham comes from these areas. Eighty-five grams of ham contain around 19 grams of protein and 2.2 grams of saturated fat, while 85 grams of pork tenderloins contain 24 grams of protein and 1.3 grams of saturated fat.

Eggs

Just one egg has about 6 grams of protein. Egg whites might not be the best part of the egg in terms of flavor, but they are the leanest source of animal protein—a single egg white contains 3.6 grams of protein and no fat. Egg whites have approximately half the amount of protein found in eggs, plus magnesium, potassium, and riboflavin, while the yolks contain many essential vitamins.

White Meats

White meats such as chicken and turkey are excellent sources of essential amino acids, and they contain less fat and cholesterol. A 3-ounce serving of chicken or turkey breast has about 28 grams of protein. Chicken breast is the leanest source of chicken, but turkey is a better alternative if you’re concerned about consuming too much saturated fat—85 grams of roasted turkey breast has 26 grams of protein and a saturated fat content less than 0.5 grams.

Shellfish and Fish

Shrimp and scallops contain all the essential amino acids. Eighty-five grams of shrimp provide 20 grams of protein and zero saturated fat, and 85 grams of steamed scallops contain 17 grams of protein and only 0.2 grams of saturated fat. Fish is also an excellent amino acid-rich food. A 3-ounce serving of halibut, tuna, or salmon provides about 22 grams. Cold-water fish like rainbow trout contains amino acids and is also rich in omega-3 fatty acids, making it a win for your health. Eighty-five grams of this fish baked contain 20 grams of protein with a saturated fat content of 1.3 grams.

What are the best animal sources of amino acids? Not all animal products contain the same amount of protein—and different cuts of the same meat contain different amounts of amino acids. Each tissue may have a different amino acid composition, determined by the specific function of the organ.

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. As sleep can get affected by physical and mental disorders, amino acids can be helpful in treating insomnia. Read on for the best amino acids for insomnia.

If you’re like many other adults, you’ve spent more than one night tossing and turning with sleeplessness.

According to the American Academy of Sleep Medicine, 30 to 35% of adults in the United States have brief symptoms of insomnia, 15 to 20% have a short-term insomnia disorder that lasts less than three months, and 10% have a chronic insomnia disorder, which occurs at least three times per week for at least three months.

Insomnia impacts energy level, mood, and health.

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. As sleep can get affected by physical and mental disorders, amino acids can be helpful in treating insomnia. Read on for the best amino acids for insomnia.

Chronic Insomnia

Chronic insomnia is usually a result of stress, life events, or unhealthy habits. Treating the main cause might cure this condition, but the process can last for years. Common causes of chronic insomnia include:

  • Stress

Stress can be at the root of many chronic disorders, including insomnia. Anxious thoughts related to work, finances, or family can keep the mind active at night, making it difficult to fall asleep. Stressful life events or trauma, such as the death of a loved one or a job loss, can also cause chronic insomnia.

  • Schedule Change

Your body can adjust to different schedules if you give it some time, but it might not react well to sudden changes such as travel across multiple time zones or work shifts that keep on changing. Your sleep-wake cycle and metabolism might get affected—and disrupting your body’s natural cycles can lead to insomnia.

  • Irregular Habits

Poor habits related to sleep include an irregular bedtime schedule, over-stimulating activities before bed, and using your bed for work, eating, or watching TV. All electronic devices used just before bed can affect your sleep cycle, especially if you read upsetting news or watch violent movies.

  • Eating Habits Before Bedtime

You can have a light snack before bedtime, but overeating, and too close to bedtime, does not leave enough time for your digestive system to process the food. You might have a hard time falling asleep because you feel physically uncomfortable while lying down, experience heartburn, or backflow of acid.

  • Medical Conditions

Chronic anxiety, panic attacks, and post-traumatic stress disorder may disrupt sleep—insomnia often appears as a side effect when the person has mental health disorders. Examples of other medical conditions that can cause insomnia include chronic pain, cancer, diabetes, heart disease, and asthma.

  • Medications

Several medications can affect sleep. Some prescription drugs such as antidepressants, medications for asthma and blood pressure, and many over-the-counter medications including some pain and allergy medications contain caffeine and other stimulants.

  • Sleep Disorders

Sleep disorders that might affect sleep include sleep apnea, which causes you to stop breathing throughout the night, and restless legs syndrome, which causes unpleasant sensations in your legs and an almost irresistible desire to move them.

  • Caffeine, Nicotine, Alcohol

All caffeinated drinks are stimulants, and drinking them in the evening can make it hard to fall asleep. Nicotine is also a stimulant that can interfere with sleep. Alcohol, a depressant, may sometimes help you fall asleep, but it prevents deeper stages of sleep and often causes awakening in the middle of the night. Addictions to these substances can cause chronic insomnia.

Amino Acids for Sleep

Conventional drugs should be used with caution in the treatment of insomnia because many of them contain properties that can cause undesired effects. A balanced supply of nutrients is key for a healthy body and mind. Amino acids affect our bodies and minds because they make up proteins, which are needed in most of the biological processes in our bodies. As sleep can get affected by physical and mental disorders, amino acids can be helpful in treating insomnia. But how exactly? And what are the best amino acids for insomnia?

Glutamine Stops Stress and Calms The Mind

Glutamine balances the immune system and helps with stress, depression, and anxiety.

This amino acid provides energy to the immune and intestinal cells. Studies show that levels of glutamine in the body are lower during times of physical or psychological stress—and cells do not have the fuel to properly function. During times of stress and tension, it is important to use supplementation of glutamine to help the cells in your body. The immune and intestinal cells, in particular, need high levels of glutamine as they divide and renew themselves at higher rates.

People with mental disorders often have a deficiency of glutamine. This amino acid increases the production of GABA (gamma aminobutyric acid), which is the most important inhibitory neurotransmitter of the brain. By increasing GABA, glutamine acts as a natural sedative in the brain. GABA brings peace of mind, balance in stressful situations, improved concentration, and restorative sleep.

Tryptophan Induces Sleep

Studies show that tryptophan (often called L-tryptophan, denoting the chemical structure) can help patients who have insomnia. A metabolic endproduct of tryptophan, 5HTP (5-hydroxytryptophan), boosts feelings of well-being, connection, and safety, by increasing production of the feel-good hormone, serotonin. Serotonin, like all neurotransmitters, transmits signals between nerve cells. Changes in the level of serotonin in the brain can alter mood and affect sleep. In addition to helping you sleep better, tryptophan can potentially reduce problems associated with sleep apnea or insomnia.

Glycine Improves Sleep Quality

Studies evaluated the effects of glycine on daytime sleepiness, fatigue, and performances in healthy subjects. The experiment aimed to reduce sleep to 25% less than the usual sleep time for three consecutive nights, and the participants took 3 grams of glycine before bedtime. A visual analog scale (VAS) and a questionnaire were used to evaluate results. The data showed a significant reduction in fatigue and sleepiness, despite the fact that participants got less sleep.

Oftentimes, amino acid therapy is based on administration of a single free amino acid. For example, you take L-tryptophan (or 5HTP) to increase serotonin in the brain.  The caution is to avoid mega-dosing or over-using a supplement. The body strives very hard to maintain a balance in all things and amino acids, in particular, are very tightly regulated.  A better strategy is to use a balanced essential amino acid mixture to ensure availability of the particular amino acid needed by the body and the brain. Amino acids for insomnia are beneficial and safer than pharmacologic approaches because they do not cause physical or psychological dependence.

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.

Diet

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

Supplementation

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?

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.

When you ingest amino acids, your body uses them to make enzymes and proteins as needed. Any leftover amino acids follow various metabolic pathways. Some are converted into glucose and used as energy. Others become glycogen and are stored in the liver and muscle for future energy use. And still others are turned into fat and stored in fat cells.  

However, should you worry that the amino acid supplement you’re taking is causing weight gain? Let’s explore.

Amino Acids Are Low Calorie

Amino acids contribute 4 calories for every gram of protein you consume. So, 4 grams of an amino acid supplement is only 16 calories. Beneficial effects of essential amino acid supplements have been demonstrated with doses less than 4 grams, so if you’re worried about calorie consequence, then you can 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 is significantly more. Consider this: 4 grams of essential amino acids from a high-quality dietary protein such as pasture-raised meat contributes 100 calories to your daily intake compared to just 16 calories from your amino acid supplement.

When it comes to weight gain, it’s important to monitor the number of calories you’re ingesting with your body’s energy needs. To determine how many calories you should eat each day based on your gender, height, and activity levels, use this online calculator from healthline.com based on Mifflin-St Jeor equation for estimating calorie requirements. 

Amino Acids for Fat Burning

Far from causing notorious weight gain, amino acids can help boost the production of hormones that help burn fat. One such hormone is the growth hormone (somotropin, STH). STH activates protein synthesis as well as fat burning. Studies show that obese and overweight individuals tend to have low concentrations of STH. Certain amino acids have been shown to increase levels of STH; most notably, arginine, methionine, and glutamine.

A 2011 study published in The Journal of Nutrition showed that individuals with a higher intake of branched-chain amino acids (BCAAs) had a lower prevalence for obesity or being overweight. The study focused on middle-aged adults from East Asian and Western countries. Researchers attributed the effect to the BCAA leucine, which can increase energy expenditure, as well as the ability of BCAAs to improve glucose tolerance (how well your body processes glucose, or sugar).

So, 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 help you maintain and build muscles, which may cause moderate weight gain (muscles weigh more than fat!), but a better body mass index (BMI) and a leaner, more toned figure.