Muscle Atrophy: Causes, Treatment and Prevention

Learn about what causes muscle wasting or muscle atrophy, and how best to prevent and treat this condition, including through the use of physical therapy, medical intervention, and staying active. 

Muscle atrophy is essentially muscle wasting: it’s what happens when your muscles waste away, frequently as a result of a lack of physical activity. This article will explore the causes and symptoms of muscle atrophy, as well as preventative steps people can take if they’re immobile or bedridden due to illness. Loss of muscle mass or muscle strength can be particularly devastating for those who are already in positions of compromised health, and so in an effort to help you maintain your quality of life, we’ve compiled the relevant information here.

Muscle Atrophy: Definition

Atrophy of the muscles occurs when a person is inactive for so long that their skeletal muscles (these are the muscles attached to your bones which literally make your skeleton move) begin to break down, and the muscle protein is cannibalized by the body. This can happen in small instances or large, catastrophic instances.

Muscle atrophy of the hand or forearm may occur if you spend weeks in a cast to heal a broken arm, which is why people in casts are given exercises to do while they’re immobilized to prevent protein degradation in their muscles and muscle wasting. Muscle atrophy of the legs or muscle atrophy of the thighs can happen on a much larger scale to those who become wheelchair-bound, either temporarily or due to becoming permanently paraplegic. In even more extreme cases, those who have been held as prisoners of war may have full-body muscle wasting due to confinement and malnutrition for significantly long periods, sometimes years.

Muscle atrophy is a decrease in muscle mass, either partial or complete, which is most commonly suffered when a person becomes disabled or their movements severely restricted. This makes it difficult or impossible to move the part of the body where the muscle has atrophied, and medical advice should be sought for solutions.

Muscle atrophy: causes, treatment, and prevention.

Muscle Atrophy: Causes

Significant decreases in activity levels can lead to muscle atrophy, and there are many situations where that can occur, causing what’s known as disuse atrophy. There are also instances of muscle atrophy due to medical conditions that inhibit the use of a body part, and even rarer causes like the muscle atrophy experienced by astronauts after relatively short periods (a few days) of weightlessness. Muscle atrophy in situations of being bedbound or ceasing intense physical training can come on in as little as 2 weeks. Some of the other causes of muscle atrophy are as follows.

  • Lack of physical activity
  • Advanced aging
  • Malnutrition
  • Stroke
  • Alcohol-associated myopathy
  • Burns
  • Temporary disabling injuries (broken bones, torn rotator cuff)
  • Permanently disabling injuries (severed spinal cord, peripheral nerve damage)
  • Prolonged corticosteroid therapy

Some of the diseases and medical conditions that can disrupt or restrict movement, thus leading to muscle atrophy, include:

  • Spinal muscular atrophy: A hereditary wasting disease of the limbs.
  • Osteoarthritis: Degeneration of bones and joint cartilage that leads to decreased movement.
  • Polymyositis: An inflammatory disease of the muscles.
  • Amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease): Compromises the nerve cells of the spinal cord.
  • Muscular dystrophy: A hereditary disease that causes muscle weakness.
  • Multiple sclerosis (MS): An autoimmune disease that destroys the protective sheathing of brain and spinal nerves.
  • Rheumatoid arthritis (RA): A chronic inflammatory disease of the joints.
  • Dermatomyositis: Inflammation of the skin and underlying muscle tissue.
  • Polio: A virus afflicting muscle tissue, which can lead to paralysis.
  • Cancer cachexia: The weight loss, lack of energy, and loss of appetite in someone undergoing cancer treatment.
  • Guillain-Barré syndrome: An autoimmune disease and form of polyneuritis, which leads to paralysis of the limbs.
  • Neuropathy: Nerve damage that results in loss of sensation or functioning.

Muscle Atrophy: Symptoms

Regardless of the cause, these are the symptoms that may alert you to possible muscle atrophy, after which a trusted medical professional should be sought for advice.

  • One of your limbs (arms, legs) appears markedly smaller than the other one.
  • You’ve spent a long time physically inactive (bedridden, hospitalized).
  • You’re experiencing noticeable weakness in one limb.

Not to be flippant about the subject, but there is some truth to the phrase “use it or lose it” when it comes to muscle. If you cannot move your muscles with regular physical activity, you will start to lose them.

Muscle atrophy pain may or may not be a symptom, as that depends on the cause of the atrophy. Many people will begin to lose muscle before they are aware it’s happening, and will have to rely on visual muscle size to realize they need medical attention.

Muscle Atrophy: Diagnosis

Once you’ve gotten in contact with a medical professional, the diagnosis may involve your full medical history, a review of any previous injuries, as well as an evaluation of your symptoms. Diagnosing the atrophy may also involve diagnosing the underlying medical condition, which may require blood tests, X-rays, MRIs, CTs, a nerve conduction study, or a muscle and/or nerve biopsy to find out what could be causing muscle atrophy if it’s not readily apparently (as it would be if you’d suddenly become bedbound).

Can Muscle Atrophy Be Reversed?

Depending on the cause, yes. There are some cases where a proper diet, exercise, and physical therapy can not only reverse muscle atrophy, but also prevent it from recurring. However, this will not be the case in some disease-related forms of atrophy, and it is important that you consult your doctor on what your expectations for muscle atrophy recovery should be in restimulating protein synthesis and rebuilding your muscles.

Muscle Atrophy: Treatment

Again, this will depend on the diagnosis of the cause, and also the severity of your muscle loss, but the treatments for reversible muscle atrophy may be as follows.

  • Physical therapy
  • Exercise
  • Ultrasound therapy
  • Dietary changes
  • Surgery
  • Electrical stimulation

If a lack of movement caused this condition, regaining movement will go a long way towards fixing it, and moderate exercise like walking, along with physical therapy, may be a way to regain muscle strength without needing surgery to fix skin, tendons, or ligaments too tight to begin moving again (as in cases of contracture deformity that could be caused by malnutrition or burn injury scar tissue).

Muscle Atrophy: Prevention

There are ways to prevent muscle atrophy before it happens, and ways to guard against it if you were fortunate enough to recover your musculature after one instance of muscle loss. If preventing muscle atrophy is in your control (and, of course, sometimes it will not be), here are a few ways to maintain muscle strength in adverse circumstances.

Stay Active

If you’re in recovery from a severe illness or have just come home from the hospital after a debilitating accident, it’s not as if you’ll take up jogging right away. However, movements as small as walking to your mailbox each day, or around the block, or up and down a single flight of stairs, can truly make the difference in the long run when it comes to maintaining your mobility.

Stay Nourished

Depending on your condition, this may be difficult, but when your body lacks the proper nutrition to stay running, it will start to catabolize your muscles for its needs, which is a form of self-cannibalization or destructive metabolism that literally eats away at your muscles. Make sure you’re getting proper protein, if not from whole foods, then in the forms of protein shakes or supplements, as every little bit may help.

In fact, supplementing with amino acids has been proven to help accelerate muscle recovery in times of sickness and illness and can help boost your muscle-building gains. To learn more about amino acid therapy for muscle atrophy, give this informative article, written by one of the world’s foremost amino acid researchers, a read.

Seek Physical Therapy

Physical therapy is particularly valuable for those with severe injury recovery (such as a car crash survivor) or a neurological condition, as therapists provide professional guidance on what, and how, and how often to stretch your body to build strength.

Try Passive Movement

Another way physical therapy can help you even before you have the strength to help yourself is with passive movement. Passive movement requires the therapist to gently move your legs and arms for you. This is how you can begin to recover from a very deep muscle deficit and build up strength and muscle again.

Preventative Measures

Not only will the above advice help prevent muscle atrophy, but it can also help discourage bedsores in those who are bedridden due to illness, and reduce the chances of developing dangerous blood clots in the limbs. Likewise, these movements may prevent muscle stiffness, retraction, and nerve damage. Consult a medical professional or licensed physical therapist for more advice.

Eliminate Atrophy

If you are in danger of muscle atrophy, take steps to make sure your protein intake and nutrients are sufficient, including the use of a supplement if necessary, like Amino Co.’s essential amino acid supplement, which contains all of the essential aminos required to build new muscle cells and structures. Also, make sure that you stay active, no matter in how small a way, to preserve your muscle function and prevent your muscles from falling into complete disuse. You cannot always control your body’s condition, but if the type of atrophy you fear is the type that’s preventable, it’s well worth the effort to maintain the quality of life and movement you’ve come to expect.

Most Popular Supplements for Muscle Growth

Learn the chemistry behind the traditional top supplements for muscle growth, and find out about the newest and most comprehensive supplement that’s about to revolutionize muscle building.

If you’re looking for supplements for muscle growth, you’ve probably already noticed that it’s a pretty crowded field. Different proteins and combinations and timing strategies get discussed, and before you know it you feel like you need about half a degree in chemistry just to build muscle at the gym! We’re streamlining the relevant information on muscle-building supplements, their pros and cons, so you can decide on the best supplements for your own fitness goals. If you’re in a rush, skip to the end, because there’s a new supplemental option that combines the best muscle growth nutrients you’ve ever known, all in one complete, balanced formula that will best all the rest. Read through to learn about the ideal muscle-building combo, a powerful protein trinity.

The First Steps Towards Muscle Building

Getting the most out of your workout involves taking a few first steps before you can start targeting muscle gain specifically. The first steps after taking up regular exercise are:

While supplements are not mandatory to reach these goals, they can be excellent aids to quicken your progress and maximize your protein intake without bringing unpredictable calories to your diet. Next up we’ll discuss the top supplements for muscle growth that you can choose from when attempting to gain muscle mass, and reveal a cutting-edge, scientifically-backed newcomer to the muscle-building supplement world.

Traditional Top Supplements for Muscle Growth

Over and above eating well and lifting weights, here are some protein and muscle-building supplements you can use to augment your workout goals, some of them more effective than others.

Top supplements for muscle growth and bodybuilding.

Carnitine

Carnitine is the general term for a group of amino acid compounds that include L-carnitine, acetyl-L-carnitine, and propionyl-L-carnitine. Carnitine is a transporter that moves long-chain fatty acids into mitochondria, where they’re oxidized or burned for energy.

A popular supplement for fat-loss, carnitine can also aid muscle growth by increasing blood flow to muscles, lessening muscle soreness, and increasing nitric oxide production, all of which improve your post-workout recovery. The combination of these benefits makes carnitine a strong asset for energy-boosting while you’re building muscles through exercise, especially when utilized in pre-workout and post-workout shakes. Though it doesn’t directly contribute to muscle building, it does provide valuable energy assistance, and improves performance during endurance athletics.

Pros

  • Aids athletic endurance by providing energy transport.
  • Helps ease muscle soreness and improve post-workout recovery.

Cons

  • Does not directly increase muscle, but instead aids in workout energy.
  • Carnitine is only a peripheral aid to individuals working to build muscle via exercise.
  • Carnitine would need to be taken alongside direct protein or amino acid supplements to be most effective.

Whey Protein Powder

A milk protein derived from whey, which is the watery part of milk that separates from the curd, whey protein is an excellent supplement affecting protein synthesis. With a high level of branched-chain amino acids or BCAAs, and including some amount of all nine essential amino acids (EAAs), this protein supplement digests relatively quickly and can help with rapid muscle building.

Whey protein can help increase blood flow due to its content of peptides, and is regularly consumed by bodybuilders immediately after their training sessions (within the hour). When choosing a whey protein, it’s recommended that you find a powder containing whey protein hydrolysates, which are proteins broken down for faster digestion.

Pros

  • Whey protein is a complete protein, containing all nine essential amino acids.
  • Whey protein is high in the branched-chain amino acids (BCAAs).

Cons

  • While whey protein is a fast-absorbing whole protein, free-form amino acids can be absorbed much more quickly.
  • Whey protein’s amino acid content is not optimally balanced, and a properly formulated essential amino acid supplement can have 3 times the effectiveness rate as a whey protein powder supplement alone.

Glutamine

Glutamine is an amino acid that not only helps build muscles by increasing the levels of the essential amino acid leucine in muscle fibers, but it also helps fight against muscle breakdown, and has been shown to play a significant role in protein synthesis.

Incidentally, glutamine can also be recommended for those with digestion issues (diarrhea or constipation), anxiety, cravings for sugar and/or alcohol, and those with poor wound healing.

Pros

  • Valuable as a precursor to the essential amino acid leucine.

Cons

  • Glutamine aids only one of the nine essential amino acids needed for muscle building, and so is far from being the most effective muscle-building supplement.
  • Glutamine is unnecessary if you’re taking a complete blend of essential amino acids.

Casein Protein Powder

Casein is the other milk protein that is derived from the curd of the milk and not the whey. Casein has a slower digestion rate than whey protein does, which makes it an excellent protein to take before bed, as it digests while you sleep and helps to prevent catabolism (which is to say destructive metabolism, a kind of self-cannibalism the body sometimes resorts to for energy).

Because increased calorie intake is also needed to build muscle, casein can help by being less filling than whey, allowing you to consume more alongside it. However, it’s also suggested that taking a combination of whey (or better yet free-form essential amino acids…read on!) and casein after a workout can help with muscle protein synthesis better than taking either one of them alone. Be advised that a casein protein product with micellar casein is the slowest-digesting form of casein readily available, and is your best bet when buying it as a supplement.

Pros

  • Casein protein has a slower digestion rate than whey, which can help prevent catabolism during sleep.

Cons

  • Works best when combined with stronger protein supplements like whey protein or free-form essential amino acids.

Beta-Alanine and Carnosine

Beta-alanine, an amino acid and key component of the dipeptide carnosine, aids in increasing carnosine levels and thus heightening muscle strength and muscle endurance. Higher levels of carnosine also increase the force of muscle contractions, and combining it with creatine (next on the list) has the greatest effect on losing body fat and gaining lean tissue, as was seen when the two were studied during a 10-week resistance training program conducted with collegiate football players.

Pros

  • Carnosine contributes to muscle endurance, leading to more powerful workouts, which can then translate to increased muscle.

Cons

  • Carnosine does not directly build muscle, but instead helps aid in workout endurance.
  • Carnosine is most effective in combination with proteins like creatine or free-form amino acids, and so is best as peripheral support for muscle building.

Creatine

Popularized as a workout supplement in the 1970s, creatine is made up of three amino acids—glycine, arginine, and methionine—and is vital for supplying the energy for muscular contraction. Creatine can be found in the forms reatine alpha-ketoglutarate (AKG), creatine monohydrate, and creatine malate. Creatine has been shown to increase the levels of insulin-like growth factor-1 (IGF-1) in resistance-exercise training, which is essential for stimulating muscle growth.

Creatine is converted to phosphocreatine (CP) in the body, which then provides energy for explosive exertions like heavy weight lifting or sprinting. The creatine-phosphocreatine system provides an increase in energy supplied to muscle cells when your body is using more ATP (adenosine triphosphate) than is being regenerated in the cells’ mitochondria. This increases your athletic endurance.

Pros

  • Provides energy for increased exercise performance, especially when you’re using more ATP than the mitochondria of your muscle cells can regenerate.
  • Creatine helps stimulate muscle growth.

Cons

  • Creatine is not most effective when taken alone, but is instead at its best when paired with an essential amino acid (EAA) supplement, where it will help provide the energy needed for increased muscle protein synthesis.

Nitric Oxide Boosters (Arginine)

Nitric oxide (NO) in the body serves to dilate blood vessels, thus allowing better blood flow to muscles, providing them with energy, nutrients, water, anabolic hormones, and oxygen—everything your muscles need to function, grow, and thrive. Nitric oxide boosters do not contain nitric oxide, but instead provide it via the amino acid arginine, which the body converts into nitric oxide.

Arginine supplements are often marketed based on their association with muscle growth, increased muscle strength, and loss of bodyweight. However, we recommend supplementing with citrulline to increase arginine, as arginine supplements don’t produce significant increases in blood arginine concentrations due to the liver’s effectiveness at clearing absorbed arginine. Citrulline, on the other hand, is converted into arginine by the kidneys, and the arginine is then released into the bloodstream; this more effectively increases your arginine levels. Additionally, there are no adverse effects associated with citrulline supplementation, while arginine consumption can sometimes lead to gastrointestinal discomfort.

Pros

  • Arginine in the bloodstream leads to more readily available amounts of nitric oxide, essential for muscle functioning.

Cons

  • Counterintuitively, arginine supplements are often ineffective at supplying useable arginine to the bloodstream.
  • Instead citrulline is recommended to supplement for an effective increase in arginine, and can be taken alongside or included in EAA and protein supplements for optimal muscle performance.

ZMA (Zinc, Magnesium Aspartate, Vitamin B6)

Supplementing the minerals zinc and magnesium aspartate along with vitamin B6 is sometimes important to bodybuilders because they become depleted during intense training and need to be specifically replaced. These nutrients are necessary for maintaining proper sleep and hormone levels, as testosterone particularly can be compromised by intensive training.

Athletes who take ZMA have been shown to have increased levels of IGF-1 and testosterone, both of which have an influence on muscle gains. ZMA is recommended to be taken before bed on an empty stomach, to allow for better uptake and to help improve sleep quality and the muscle recovery that sleep provides.

Pros

  • Can help correct vitamin and mineral deficiency caused by intensive weight training.

Cons

  • ZMA supplementation does not lead to direct muscle growth, but can be taken as needed alongside free-form amino acids or traditional protein contributions like whey or creatine, depending on your workout style and your body’s needs.
  • Not everyone will need the extra supplementation of ZMA.

HMB (Beta-hydroxy beta-methylbutyrate)

Beta-hydroxy beta-methylbutyrate or HMB is a molecule derived from the processing of the essential amino acid leucine, and helps protect against muscle protein breakdown. HMB is often recommended only for those who are beginning weight-training exercises, as the scientific results seen in those who are more experienced with muscle training are less significant. This is due to the fact that HMB is heavily reliant on a steady and abundant supply of EAAs to be effective. When the EAA supply dips down, so does the effectiveness of HMB; it cannot work alone.

Pros

  • HMB supplementation can be good for resisting extreme catabolic states, such as in individuals with critical wasting illnesses.

Cons

  • HMB without an excess supply of EAAs is only marginally effective.
  • EAA supplementation is also needed to derive maximum benefits from HMB supplementation.

Branched-Chain Amino Acids (BCAAs)

The branched-chain amino acids are a subcategory of essential amino acids, and are designated by the molecular structure of leucine, isoleucine, and valine. BCAAs make up 14% of the amino acids that reside in your muscles, and it’s been shown that taking a supplement of BCAAs during resistance-training exercise increases muscle strength, fat loss, and lean mass.

However, while research shows that leucine in particular stimulates muscle protein synthesis, and that together these three amino acids diminish cortisol (a catabolic hormone), increase energy, and reduce delayed-onset muscle soreness, BCAAs when consumed alone are not fully effective. All nine essential amino acids are needed to make new muscle, and in fact, the the rate of muscle protein synthesis is directly affected by the availability of all your essential amino acids—the more you have, the faster your rate of muscle synthesis, and the fewer you have, the slower the rate. Because of this, research actually shows that BCAAs when taken alone have little to no effect on the rate of muscle protein synthesis in humans.

Pros

  • BCAAs are valuable amino acids that can be taken to help some aspects of muscle building.

Cons

  • BCAAs are only three of the nine essential amino acids, and all essentials are needed to create new muscle.
  • BCAAs have little to no effect on muscle protein synthesis when taken alone.

An Essential Amino Acid (EAA) Blend: The New Top Muscle Growth Supplement

If BCAAs ever sounded good, you’ll probably be more interested in a complete EAA supplement. Our unique EAA supplement is an ideally proportioned blend that combines the strengths of whey protein, creatine, and the eight essential amino acids that contribute directly to muscle growth. With our EAA blend, you’ll not only get the BCAAs mentioned above, but also a full cocktail essential amino acid supplement. It contains the key factors that make whey protein and creatine effective too, giving you the best of every top effective traditional supplement on the market.

EAAs and Muscle Protein Synthesis

The human body is made up of about 20% protein, and amino acids are used to form our muscles, tissues, and organs (not to mention the hormones needed for cognitive and physiological function). The key to our muscle-building product that helps make it more effective than other supplements, and even some dietary sources of essential amino acids, is its absorption rate and digestibility.

The EAAs derived from dietary proteins have to be digested first and then absorbed, while free-form amino acids are absorbed more quickly and completely. With eight of the nine essential amino acids (minus tryptophan which is not necessary to supplement for muscle protein synthesis), the amounts of EAAs are maximized more than any naturally occurring protein can deliver.

EAAs with Whey Protein’s Support

While free-form EAAs provide faster absorption, an intact protein like whey provides for a longer absorption period, sustaining the supply of EAAs after the rapid absorption of the free-form EAAs. Designed to work in concert with one another, our muscle-growth supplement combines its EAA profile with a balanced inclusion of whey protein for steady, ongoing support of muscle protein synthesis.

EAAs and Creatine’s Energy

Because creatine-phosphate provides the energy for sudden bursts of physical activity like lifting heavy weights or sprinting, it’s included in the Amino Co.’s technology to provide the energy needed to convert EAAs into muscle via muscle protein synthesis. Instead of waiting for the mitochondria of muscle cells to metabolize ATP for energy, creatine covers the time gap when needed, completing the full circle required for ideal muscle building: the rapid essential ingredients, the long-haul supply, and the energy to put them to use.

The Amino Company Advantage

Our product is a unique, patent-pending blend of essential amino acids, whey protein, and creatine that outperforms all other supplements in increasing muscle mass. Good for increasing strength in the elderly and easy to include in drinks or smoothies, Amino Co. supplements are scientifically proven to be effective in muscle protein synthesis over any other supplement, food, or protein choice currently available.

The ABCs of Muscle Growth

On a first glance at muscle growth supplements, it looks like an alphabet soup of vitamins and molecules and chemistry notes, but the more knowledgeable you become about your own body’s strengths and needs, the closer you’ll approach a PhD’s level of understanding when it comes to which supplements best support your goals. Effectiveness is key, bolstered by practical results that can be not only felt, but also scientifically proven. In the end, you can see which supplement brings you the greatest value.

The strongest performers from the traditional list of muscle growth supplements have been brought forward to the new frontier: an EAA blend that brings the best of everything essential to building and maintaining new muscle. The Amino Company provides the full circle of quick, long-lasting, and energized EAAs for muscle building. When you take our unique blend, you’re guaranteed to have an optimally balanced formula designed specifically for human muscle growth (and not lab animals). With the Amino Co. on your team, you can reach higher heights of strength faster and more effectively than ever before!

What Are the Best Muscle Recovery Foods?

Wondering what muscle recovery foods are good for prevention and relief of delayed onset muscle soreness? This comprehensive list of foods full of healthy fats, amino acids, and natural sugars will support your workout and recovery goals.

After starting a new workout, you’re in for some growing pains. Delayed onset muscle soreness or DOMS can affect anyone, from those new to working out to elite athletes incorporating different exercises into their routines. Whenever you push your muscles, either with unfamiliar exercises or longer durations, you’re creating microscopic tears to the muscles, which then cause stiffness, soreness, and pain. Are sore muscles a good sign? Yes, in a sense, because it means you’re using your muscles in new ways that will eventually lead to a better fitness profile. But don’t fret! Eating muscle recovery foods can help ease the discomfort and may even help decrease muscle soreness in the first place.

Using food as your method of recovery and prevention may truly be the best road to take. The other suggestions to help muscle recovery either take extra time or come with other risks, and none of them can get in front of DOMS before it starts. Getting a massage after every workout would be great, but do you have the time, the money? Rest and ice packs are perfectly reasonable options too, but it’s the rest that might bother you if you’re really excited about a new workout and seeing results. Do you really want to take a couple of days off after every workout to let your muscles recover? It might not be a bad idea, but with the right foods pre- and post-workout, it might not be necessary either.

The last refuge to treat the ache and pain of muscle soreness is to use painkillers. Whether it’s over the counter fare you’d take for any pains (a wincing headache for example, or to relieve menstrual cramps), or prescription painkillers meant for more serious pains (a wrenched back or dental surgery). And these pain killers come with health-compromising side effects that are best avoided.

So what can you eat that will make a difference? Here are some foods you might want to include on the menu on gym days.

 Muscle recovery foods for prevention and relief.

Muscle Recovery Foods

Whether for their protein content, iron content, anti-inflammatory properties, or amino acids, these foods can help your muscles heal faster.

Cottage Cheese

Cottage cheese has around 27 grams of protein per cup, and is often a regular food in the fitness community for those without any dietary restrictions surrounding milk products. In fact, the casein protein found in cottage cheese curds (as opposed to the whey protein found in watery milk) are often isolated and used as a workout protein supplement. As a slow-digesting protein, casein can help build and rebuild muscle while you sleep if it’s your last snack before bed.

The essential amino acid leucine is also present in cottage cheese, and comprises around 23% of the essential amino acids in muscle protein (the most abundant percentage of them all). Foods with leucine can help you build muscle by activating protein synthesis, and the faster you rebuild your muscle, the faster your muscle repair and workout recovery!

Eat it plain, or combine cottage cheese with some of the other recovery foods on this list to stack the benefits. Cottage cheese can even be used in baked goods and pancakes or included in protein shakes—don’t be afraid to get creative.

Sweet Potatoes

Adding sweet potatoes to your post-workout meal can help replenish your glycogen stores after a tough workout. Sweet potatoes are a great source of vitamin C and beta-carotene as well, and are loaded with fiber which helps to control appetite and maintain healthy digestion and build muscle.

Sweet potatoes can be baked whole in the oven or on a grill, cut into fries, spiced with cinnamon, or made savory with garlic powder and pepper. Enjoy them at the dinner table or on the go: a baked potato wrapped in foil can join you just about anywhere.

Baking Spices

Speaking of what you can put on sweet potatoes, it turns out some baking spices are good for post-workout recovery as well. Not so much in the form of gingerbread cookies or cinnamon rolls, but a study showed that cinnamon or ginger given to 60 trained young women (between the ages of 13 and 25) significantly reduced their muscle soreness post-exercise. If you’re already having a sweet potato, make it a little sweeter with some cinnamon, add it to oatmeal, or put some in your coffee for the extra boost.

Coffee

Did we just mention coffee? Good news: coffee’s on the list too. Research suggests that about 2 cups of caffeinated coffee can reduce post-workout pain by 48%, and another study showed that pairing caffeine with painkilling pharmaceuticals resulted in a 40% reduction of the drugs taken. If you do need pharmaceutical pain relief, maybe coffee can help you minimize just how much you take—caffeine is a much less dangerous stimulant than pain pills.

Turmeric

Another spice on the list, turmeric contains the compound curcumin, which is an anti-inflammatory and an antioxidant, and has been shown to be a proven and reliable pain reliever. Whether it’s helping you with delayed onset muscle soreness or pain from an injury (workout-related or otherwise), turmeric eases both pain and swelling by blocking chemical pain messengers and pro-inflammatory enzymes.

As with the other spices, it can be easily added to baked goods, to coffee, and to oatmeal. With its beautiful golden color, you can even make what’s called “golden milk” or a turmeric latte by combining 2 cups of warm cow’s or almond milk with 1 teaspoon of turmeric and another teaspoon of ginger, and then sip your muscle soreness away.

Oatmeal

Speaking of oatmeal (and isn’t it nice that so many of these ingredients can be easily combined?), it, too, can help relieve muscle soreness. This complex carb gives you a slow and steady release of sugar, along with iron needed to carry oxygen through your blood, and vitamin B1 (thiamin), which can reduce stress and improve alertness. This is why oatmeal is a great way to start the day, but since it also includes selenium, a mineral that protects cells from free-radical damage and lowers the potential for joint inflammation, it’s a great food for those in high-intensity workout training as well (like, up to Olympic level training).

Use oatmeal as a daily vehicle for other healthy ingredients, including the spices on this list, and enjoy its reliable benefits.

Bananas

Easily sliced into oatmeal, included in smoothies, or eaten alone, not only are bananas a healthy way to replace sweets (frozen and blended they can even make a delicious ice cream alternative), bananas are also a great way to get much-needed potassium. Research suggests potassium helps reduce muscle soreness and muscle cramps like the dreaded “Charley horse” spasm that contracts your muscle against your will and might not let up until it causes enough damage to last for days. A banana a day could keep the Charley horse away, and is particularly delicious (and helpful) when paired with its classic mate: peanut butter.

Peanut Butter

The healthy fats and protein found in nut butters like peanut or almond butter can help repair sore muscles. A reliable source of protein for muscle building, with fiber for blood pressure aid, vitamin E for antioxidant properties, and phytosterols for heart health, peanut butter offers up a ton of benefit and is easy to eat anywhere. Make a sandwich, use it to help bind together portable protein balls filled with other ingredients, add it into smoothies, or just eat it from the jar with a spoon (no one’s judging).

Nuts and Seeds

If you’re a fan of protein balls, then you’re well acquainted with nuts and seeds, which are great additions to these protein-rich foods. While providing essential omega-3 fatty acids to fight inflammation, various nuts and seeds can provide you protein for muscle protein synthesis, electrolytes for hydration, and zinc for an immune system boost. Something as simple as a baggie full of almonds, walnuts, pumpkin, and cashews can help maximize your muscles. Mixing in seeds (sunflower, chia, pumpkin) adds a healthy density that can curb your hunger and satisfy your appetite for longer. They’re small but powerful assets in quick muscle recovery.

Manuka Honey

This is not your grocery store honey in its little bear- or hive-shaped bottle. Manuka honey comes from the Manuka bush in New Zealand, with a milder flavor than that of bee honey and a much thicker texture. It’s anti-inflammatory and rich in the carbs needed to replenish glycogen stores and deliver protein to your muscles. Drizzle it over yogurt or stir it into tea to gain its benefits.

Green Tea

Green tea is particularly helpful for muscle recovery purposes. With anti-inflammatory antioxidants, it makes an excellent pre- or post-workout drink to prevent muscle damage related to exercise, and also helps you stay hydrated.

Cacao

Cacao has high levels of magnesium, antioxidants, and B-vitamins, which reduce exercise stress, balance electrolytes, and boost immunity and energy levels. The antioxidant flavanols in cacao also help up the production of nitric oxide in your body, which allows your blood vessel walls to relax, lowering blood pressure and promoting healthy blood flow. Adding cacao powder to your high-quality protein shakes or a glass of cow/almond/coconut milk post-workout will bring you its benefits.

Tart Cherries

Tart cherry juice has been shown to minimize post-run muscle pain, reduce muscle damage, and improve recovery time in professional athletes like lifters, according to the Journal of the International Society of Sports Nutrition. Enjoy tart cherry juice as a drink, or include the dried fruit as a part of your own muscle-building trail mix with the nuts and seeds discussed above. It’s not the only fruit or fruit juice you might include either. The nutrients in fruits like oranges, pineapples, and raspberries can also help speed up your recovery.

Salmon

Rich with anti-inflammatory omega-3 fats, muscle-building protein, and antioxidants, salmon is an extremely efficient post-workout food. Not an option if you are vegan or vegetarian, of course, but for the meat eaters among us, or those on the Paleo diet, salmon can specifically help prevent delayed onset muscle soreness, reduce inflammation, and provide you with an abundance of the protein needed for muscle growth. Eat this protein within 45 minutes after working out for maximum effect, either grilled, cooked up in salmon cakes, or raw in the form of sushi or sashimi. All of the above goes for tuna as well, by the way—reasons you might become a pescatarian.

Eggs

If you are an omnivore or ovo-vegetarian, eggs are great way to gain protein first thing in the morning, and an even more effective food to have immediately post-workout to help prevent DOMS. Like cottage cheese, eggs are a rich provider of leucine, and like salmon, eggs contain vitamin D (in their yolks). For your convenience, eggs can be boiled and brought along for immediate consumption after your training. Boil a dozen at the start of each week during your meal prep, and have an easy protein source in the palm of your hand every other day of the week.

Spinach

Did we really get all the way to the end of the list without a vegetable? So sorry! Let’s fix that with spinach. A powerhouse of antioxidants, not only can spinach help prevent diseases like heart disease and various cancers, but it also helps you recover quickly from intense exercise. Spinach’s nitrates help to strengthen your muscles, and its magnesium content helps maintain nerve function. Spinach helps to regulate your blood sugar (in case you worry about the spikes you might get from the sweeter items on this list), and can be added to many dinners, snuck into smoothies, or eaten on its own either raw or sautéed in olive oil.

Resist Damage and Recovery Quickly

These foods help with recovery from DOMS and reduce the amount of soreness you get in the first place by providing your body with the proteins and nutrients it craves when you’re working out to the best of your ability.

A quick note before you go. In your quest for pain-free muscles, you’ll want to avoid:

  • Refined sugar: Just one sugary soda a day can increase your inflammatory markers, as can white bread and other products with refined sugar. Natural sugars don’t bring that kind of adverse effect, so get your sugar from whole foods instead.
  • Alcohol: The dehydration caused by alcohol requires its own special recovery, and will deplete many of your vitamins (especially B vitamins). Some research suggests that alcohol can interfere with how your body breaks down lactic acid, which would increase muscle soreness. If you’re on a mission to build muscle, it’s best to avoid alcohol.

If you’re eating pretty well and avoiding what you shouldn’t eat, but still find muscle soreness a burden after working out, there is always the option to supplement.

What is the best supplement for muscle recovery? Evidence shows that getting all your body’s essential amino acids in balance will help specifically with muscle sprains and pulls, so when supplementing, just make sure you cover the waterfront (rather than choosing one or two essentials and neglecting the rest). Other than that, a diverse diet can be had in choosing natural preventions and remedies for healthy muscle recovery.

9 Natural Remedies for Back Pain Relief

Few things can be as immediately disabling as back pain. Looking for back pain relief? Here are some natural remedies that can help get the pain off your back.

Few things can be as immediately disabling as back pain. Our backs are a delicate and complex structure of muscles, ligaments, joints, and bones. Back pain can be caused by a wide range of injuries, dehydration, inflammation, and certain underlying health conditions, and back pain relief can be difficult to come by.

Be it acute or chronic, back pain causes a reduction in physical activity, lost productivity at work, and overall poor quality of life scores according to a study published in the journal European Spine. 

Low back pain is incredibly common, not only in the United States but also globally. In fact, according to findings from the Global Burden of Disease 2010 study, low back pain is the leading cause of disability worldwide. Fortunately, there are effective natural pain management remedies that can help you enjoy life to the fullest.

Are You at Risk for Back Pain?

Nearly everyone will experience some type of back pain over the course of a year. According to a National Center for Health Statistics 2016 report, during 2012 more than 125 million adults in the United States had a musculoskeletal pain disorder. This staggering figure accounts for more than 50% of the U.S. adult population.

It must be noted that musculoskeletal pain is classified as pain related to nerves, tendons, ligaments, muscles, and bones, not just in the back. The Cleveland Clinic also puts fibromyalgia, arthritic pain, and carpal tunnel syndrome in the same category.

In the general population, researchers report the lifetime prevalence of back pain high at 85%. This surprising statistic comes from a comprehensive review conducted by researchers from the Department of Sports Medicine and Sports Nutrition in Germany.

This same review also found that in athletes, the lifetime prevalence can be as high as 94%, and it identifies rowing and cross-country skiing as sports with the greatest risk.

Of course, there are also risk factors for chronic pain conditions, such as occupations that increase your likelihood of suffering an injury to the back muscles or sustaining muscle pain. In a review of the National Health Interview Survey completed by the National Institutes of Health, the following occupations have the highest rate of low back pain—attributed directly to the job:

  • Construction and Extraction: 11.22%
  • Healthcare Practitioners and Healthcare Support: 10.61%
  • Personal Care and Service: 8.27%
  • Transportation and Moving: 7.74%

Your risk for developing back pain increases according to a cross-sectional study published in the Annals of the Rheumatic Diseases if you:

  • Are obese
  • Smoke
  • Are inactive
  • Have family members with chronic back pain

Types of Back Pain

Back pain can be classified as either acute or chronic. Acute back pain can last anywhere from 4 to 12 weeks, and generally does not require traditional medical intervention. However, when back pain persists or worsens for 12 weeks or longer, the pain is considered chronic, and a consultation with your health care provider is advised.

Pain in the back can present in the:

  • Lower back
  • Middle back
  • Upper back
  • Neck and shoulders
  • Glutes

Back pain can be described as:

  • Nagging
  • Radiating
  • Throbbing
  • Pinching
  • Mild
  • Moderate
  • Severe

Keeping a journal of your pain can help you find a successful treatment. Take note of the type of pain, severity, when it occurs and for how long, the location of the pain, and what you were doing when it occurred. These details can help your wellness team identify the best course of action to relieve your back pain naturally.

Common Causes of Back Pain

According to Weill Cornell Medicine’s Center for Comprehensive Spine Care, there is a wide range of injuries and medical conditions that can cause back pain. Their list includes:

Muscle injuries and muscle strains Vertebral fractures Pregnancy
Spinal stenosis, a narrowing of the spinal canal Scoliosis Obesity
Degenerative disc disease Tumors Anxiety
Pinched or compressed nerves Osteoporosis Smoking
Lack of physical activity Aging

The Center for Comprehensive Spine Care makes a special effort to identify the symptoms of thoracic back pain. This type of back pain occurs in the upper back and it may indicate a serious or even potentially life-threatening underlying condition. If you experience upper back pain and any of the following symptoms, seek medical attention immediately.

  • Fever
  • Unexplained weight loss
  • Deformity of the spine
  • Nerve pain in the lower body
  • Numbness or tingling in the legs or lower body
  • Severe stiffness
  • Severe constant pain
  • Changes in bladder or bowel function

9 Natural Remedies for Back Pain Relief

1. Fish Oil (2,000 milligrams a day)

Omega-3 fatty acids make an essential contribution according to the Harvard T.H. Chan’s School of Public Health. Omega-3s cannot be produced in the body; they must be consumed. The richest sources are coldwater fish, walnuts, and flax seeds.

Every healthy diet should include a variety of foods with these essential fats to reap their health benefits. However, when you are experiencing back pain, taking a high-quality supplement of 2,000 milligrams a day may be advised. In a landmark study conducted by the Department of Neurological Surgery at the University of Pittsburgh Medical center, fish oil was shown to be as effective and safer than NSAIDs in relieving back pain.

While omega 3s are well-tolerated in food, check with your doctor prior to taking a fish oil supplement if you have type 2 diabetes, take blood thinners, or have a bleeding disorder or a shellfish allergy.

2. Turmeric (1,000 milligrams a day)

Curcumin, the active ingredient in turmeric that fights inflammation and reduces pain, is one of the most effective natural compounds in the world. Researchers from the University of Texas M.D. Anderson Cancer Center’s Department of Experimental Therapeutics conducted a clinical trial that found that natural compounds including curcumin are more effective than aspirin or ibuprofen.

Curcumin’s health benefits extend beyond its anti-inflammatory properties. In fact, in a systematic review published in the Journal of Alternative and Complementary Medicine, researchers state curcumin is safe in doses up to 2500 milligrams a day and can be used to treat a wide range of conditions. Current clinical trials are focusing on curcumin’s ability to prevent cancer, fight cancer, and even make traditional cancer treatments like chemotherapy more effective.

Incorporating turmeric into your diet is easy. The small orange root is now readily available in most grocery stores. Just look for it near the fresh ginger. But please note, when using fresh or powdered turmeric, to get its full benefit, it must be combined with black pepper. Piperine, an essential compound in black pepper, makes it easier for the body to absorb curcumin.

Turmeric is easy to incorporate into salad dressings, stews and soups, and rice dishes for daily enjoyment. When you feel you need an extra boost of curcumin’s anti-inflammatory powers, sip on a turmeric latte. This delightful warm drink can be made with ingredients in your pantry—just don’t forget to add the black pepper!

3. D-Phenylalanine (1,500 milligrams a day, for several weeks)

D-Phenylalanine, or DPA, is one of the essential amino acids that is recognized for its power to reduce low back pain according to University of Michigan’s, Michigan Medicine. They report DPA decreases pain and can inhibit chronic pain in some cases. There are currently 48 clinical trials evaluating the safety and efficacy of phenylalanine on conditions like cystic fibrosis and PKU, as well as the levels needed for wellness.

To learn more about taking phenylalanine for back pain, check out this article.

4. L-Tryptophan (2-6 grams a day)

Tryptophan, most commonly associated with turkey “comas” on Thanksgiving, is another of the essential amino acids that can help when you are experiencing upper back pain, middle back pain, or lower back pain. Tryptophan plays a critical role in back pain relief by helping to repair muscle tissue that has been damaged. Additional tryptophan benefits include reducing anxiety and depression.

An important note about amino acid supplements: The balance of amino acids in your blood is a delicate one. Because certain amino acids hitch a ride on the same transporter for entry into the brain, increasing levels of one without increasing levels of the other can restrict access and adversely affect mind and mood. For this reason, it’s recommended to supplement with a complete essential amino acid blend formulated with an ideal ratio of aminos.

5. Collagen (2-5 grams a day)

A vital protein, and the most abundant in the human body, collagen is the substance that gives our skin, hair, ligaments, and tendons the fuel they need. If your joints creak or pop, you may not have enough collagen “greasing the wheel” between your joints. And that can increase the risk for joint deterioration that can cause arthritis and chronic back pain.

Collagen is recognized for improving skin health, hair health, IBS symptoms, cellulite, and muscle mass, and has even garnered a reputation as an effective treatment for joint disorders and osteoarthritis according to researchers from the University of Illinois’ College of Medicine. This study specifically points to the efficacy of collagen hydrolysate.

Think of collagen hydrolysate as gelatin. It is rich in amino acids, but it has been processed fairly extensively to make the proteins smaller and more easily absorbed. Seek a high-quality supplement from a reputable company to add to your diet. While generally considered safe, some mild side effects have been reported with collagen supplements, namely digestive upset and heartburn.

6. Acupuncture

A popular and time-tested holistic technique, acupuncture has been shown to improve chronic back pain. In a large-scale clinical trial, researchers from Memorial Sloan-Kettering’s Department of Epidemiology and Biostatistics evaluated the efficacy of acupuncture for back and neck pain, arthritis pain, chronic headaches, and shoulder pain. The researchers determined that acupuncture is effective for chronic pain and verified that acupuncture has more than a placebo effect.

7. Massage

Massage is known for relieving stress, anxiety, pain, and a variety of other health conditions. Professional athletes often turn to massage after a tough workout or game to help relieve sore or strained muscles. Massage therapists can target specific muscles, ligaments, tendons, and connective tissues that are causing back pain.

There are a number of massage modalities, with some dating back to ancient China. Depending on the root cause of the back pain, a licensed and experienced massage therapist might recommend a deep tissue, sports, soft tissue, or Shiatsu massage. Massage is believed to relieve low back pain by improving circulation, releasing tension, increasing endorphin levels, and improving range of motion. Understand that it may take multiple sessions to accomplish relief.

8. Capsaicin Cream

Made from the compound found in cayenne and other hot peppers that cause the burning sensation and taste, capsaicin promotes pain relief, particularly for back pain, according to a study published in the journal Molecules. Available both over-the-counter and by prescription, a topical capsaicin cream can provide immediate back pain relief.

It is important to purchase a high-quality product and apply it as directed on the packaging. In itself, capsaicin can create pain, but it can also relieve the discomfort and pain caused by soft tissue injuries, fibromyalgia, arthritis, and muscle pulls or strains. Researchers believe that the heat generated by the capsaicin works by activating pain receptors that cause the brain to release pain-fighting hormones.

9. DIY Pain Relief Rub

Beyond using heating pads to soothe muscle tension and back pain, you can whip up a quick DIY pain relief rub. For a quick DIY topical back pain reliever (that smells great too!) use the recipe below. This home remedy is perfect for relieving lower back pain after a hard workout or pulling weeds. When applied, it provides a cooling, yet invigorating effect because of the menthol in the peppermint oil.

DIY Pain Relief Rub

  • 5-7 drops peppermint essential oil
  • 5-7 drops lavender essential oil
  • 5-7 drops marjoram essential oil
  • 2 teaspoons freshly ground black pepper
  • 1/4 cup coconut oil or jojoba oil

Mix all ingredients together until well combined. Massage into sore muscles and joints daily, or as needed.

Natural remedies for back pain relief

6 Lifestyle Changes to Prevent Back Pain

1. Exercise Regularly

The more you move, the better. Regular exercise is important for keeping your strength, flexibility, balance, and cardiovascular health at their pinnacle. Low-impact exercise like walking, riding a bike, and swimming are good options when you have back pain.

In addition to weight management, regular exercise has been shown to help:

Aim for 180 minutes each week, or 30 minutes a day, of moderate, low-impact exercise to relieve back pain and discomfort. The other health benefits will help to prevent additional injury and improve cardiovascular function.

Natural remedies for back pain relief

2. Stay Hydrated

Drink at least 8 ounces of pure water for every 10 pounds of body weight to stay properly hydrated. When you are dehydrated, the natural lubrication in your spinal discs is depleted and can result in backaches and fatigue.

Kidney stones and urinary tract infections are more worrisome side effects of dehydration and can both cause back pain. According to the National Kidney Foundation, it is vital to drink enough water during workouts and periods of hot weather as prolonged or frequent dehydration can cause kidney damage.

3. Lift Heavy Items Properly

Avoiding back injury is the best way to prevent back pain. According to the Mayo Clinic, it is important to use proper lifting techniques to avoid back pain. The Mayo Clinic recommends:

  • Starting in a safe position
  • Maintaining the natural curve of your spine
  • Using your legs to lift the weight
  • Squatting instead of kneeling
  • Avoiding twisting

4. Practice Pilates

Joseph Pilates developed this practice of stretching and body conditioning while interned during World War I. The reformer, which is widely used in Pilates studios today, is modeled after the first equipment he developed in the internment camp using bunk beds, springs, and ropes.

Pilates is focused on increasing core strength and creating long fluid muscle groups. This practice can help prevent injuries to the back and provide back pain relief. If you do have back pain, medical research shows that a regular Pilates practice is a great way to strengthen your core to prevent low back pain. In the just-released results of a randomized controlled trial, 12 weeks of Pilates practice improved chronic back pain.

Most metropolitan areas have established Pilates studios where experienced instructors and reformers are available. If a studio is not available in your area, Pilates equipment, including reformers, are available for home use.

5. Tai Chi

This ancient martial art has been practiced for thousands of years. It is characterized by slow, precise, and controlled movements—a very different discipline than other martial arts that focus on explosive power. Tai chi epitomizes the mind-body connection, as every fiber of your being must be engaged for best practice.

According to Harvard Medical School, the health benefits of tai chi include aerobic conditioning, improved flexibility and balance, better muscle strength and muscle response, and a reduction in falls. Tai chi can be practiced by virtually anyone, in any health condition. It involves low-impact and slow-motion isolating muscle groups responsible for core strength, balance, and confidence.

6. Yoga

Millions of Americans practice a form of yoga. This practice combines deep relaxation, deep breathing, meditation, and strength-training postures that are mixed together in balance to create a discipline known for reducing pain and improving balance, flexibility, and strength.

According to Harvard Medical School, yoga’s proven health benefits include:

  • Reducing your risk of heart disease
  • Relieving migraines
  • Fighting osteoporosis
  • Alleviating the pain of fibromyalgia
  • Easing multiple sclerosis symptoms
  • Increasing blood vessel flexibility (69%!)
  • Shrinking arterial blockages

Regular yoga practice can help you prevent injury and back pain. And, if you have low back pain, a systematic review and meta-analysis focusing on the effectiveness of yoga and back pain showed that yoga is effective for both short-term and long-term relief of chronic low back pain.

Natural remedies for back pain relief

Precautions

As mentioned above, back pain accompanied by certain other symptoms can be a sign of serious underlying health conditions. If you experience back pain and any of the following symptoms, please consult with your physician immediately:

  • High fever
  • Chills
  • Dizziness
  • Numbness or tingling in any part of the body
  • Deformity of the spine
  • Unexpected weight loss
  • Extreme stiffness
  • Severe constant pain
  • Changes in bladder or bowel function

Back pain symptoms tend to recur, with studies showing a recurrence rate of somewhere between 24% and 80%. To protect against future episodes of back pain, learn to lift heavy items properly and build your core strength to reduce your risk of injury.

At the End of the Day

Back pain is costly. It affects productivity at work, health care costs, and most importantly your quality of life. Whether acute or chronic, when you are in pain, the only thing you can focus on is effective back pain relief. Whether it strikes as lower back pain, middle back pain, or as neck and shoulder pain, pain is pain and finding the natural back pain remedy to ease your pain and speed up the healing process is essential.

Once the root cause of your back pain is determined, natural lower back pain remedies and upper back pain remedies are available. The key is finding the combination of treatments that work for you. Whether it is a high-quality amino acid supplement, a DIY essential oil rub, yoga, or Pilates, you can improve your quality of life and relieve your discomfort.

What’s with HMB Supplements?

HMB has been shown to promote muscle gain in individuals who are working out. However, this muscle-promoting effect is dependent on adequate availability of essential amino acids (EAAs). HMB supplements without the support of EAAs just don’t cut it.

From hydroxymethylbutyrate to beta-hydroxy-beta-methylbutyrate (or β-hydroxy-β-methylbutyrate), HMB—a chemical produced when the body breaks down the amino acid leucine—is known by a variety of names. But what exactly are HMB supplements?

HMB supplements are promoted as nutritional substances that can help speed wound healing and support individuals with muscle-wasting diseases such as cancer and HIV. Proponents also tout HMB supplements (or HMB in combination with creatine monohydrate) as a way to slow the muscle wasting that comes with aging.

To be fair, research does support the presence of some beneficial effects of HMB. For example, it’s been shown to promote muscle growth in individuals who work out. However, it should also be noted that this muscle-promoting effect is dependent on the adequate availability of essential amino acids (EAAs).

In other words, HMB supplements in isolation, without the support of EAAs, have a minimal effect on muscle building.

How Does HMB Work?

HMB and the EAA leucine are closely linked, and it’s necessary to understand the relationship between them to understand how HMB works.

Leucine is the most abundant of the nine EAAs found in muscle protein. It also acts as a nutraceutical aid in turning on the body’s muscle-building switch. In fact, it’s one of the three branched-chain amino acids—the others being isoleucine and valine—that make up about a third of muscle protein. Some experts also propose that leucine turns on the process of protein synthesis (muscle building) via the action of HMB.

HMB is a metabolite of leucine, meaning it’s derived from the breakdown of leucine. In a series of step-by-step reactions, about 15% of the leucine present in blood is also irreversibly broken down to ammonia and carbon dioxide. This sequence of reactions by which leucine is reduced to its basic components is called a metabolic pathway.

But there’s more than one metabolic pathway involved in the breakdown of leucine. And it’s actually via a minor pathway that the leucine metabolite HMB is produced, yet it’s still proposed to be the active component of leucine. However, as leucine is being broken down by the body, only about 5% of it is broken down via the pathway that results in HMB.

Combine this with the fact that only 15% of leucine is broken down at any given time, and it’s clear that the amount of HMB produced by leucine breakdown makes up only a very small percentage of available leucine.

As a result, the concentration of HMB in body fluids is far less than that of leucine. And since results with dietary supplementation aren’t achieved unless the concentration of HMB is increased many times above the normal physiological level, it’s unlikely that leucine’s effects on muscle protein synthesis are, in fact, mediated by HMB.

However, when the availability of HMB is increased using dietary supplements, it seems to work as a nutraceutical in the same way leucine does in that it activates the molecular mechanisms involved in the initiation of protein synthesis.

Specifically, the increase in HMB concentration supplied by supplementation activates a molecule known as mammalian target of rapamycin, or mTOR.

The molecule mTOR plays a key role in controlling the initiation of protein synthesis. When mTOR is activated, a series of additional chemicals involved in the initiation of protein synthesis is activated as well. And when all of these molecules are switched on, the process of protein synthesis begins. Likewise, when mTOR is activated by excess levels of HMB, the process of protein synthesis is also stimulated.

A sustained increase in muscle protein synthesis should ultimately be reflected by an increase in muscle strength, function, and mass over time. However, the use of HMB alone does not result in an increase in protein synthesis.

In fact, any increase in protein synthesis resulting from HMB supplements will last only as long as there’s an adequate supply of EAAs. And once there’s a dip in the EAA supply, the effect of HMB stops as well.

HMB Needs EAAs to Work

If you activate mTOR but your body doesn’t have enough EAAs circulating in the bloodstream, then muscle protein synthesis will only be increased to a limited extent.

As stated earlier, muscle protein contains nine EAAs, each of them unique and each a vital component of newly produced proteins. Unlike the 11 nonessential amino acids, EAAs can’t be produced in the body and have to be obtained through dietary sources.

However, if you aren’t getting enough EAAs through protein-rich foods or EAA supplements, then your only source of EAAs is the protein already present in your body.

In this case, your body begins to break down its protein stores and release the component amino acids, including EAAs, for use by the cells of the body. However, under normal conditions, only about 85% of amino acids released in this manner are reincorporated into protein; the rest are lost to oxidation.

But let’s circle back to HMB.

To be effective on its own, HMB must increase the efficiency of EAA reutilization for protein synthesis. However, as we just indicated, that process is already 85% efficient, which means there’s a definite limit as to how much more efficient the recycling of EAAs back into protein can be.

Therefore, it becomes clear that dietary supplementation with HMB works only when there’s an excess amount of EAAs available. And an excess supply of EAAs can occur via only two mechanisms:

  • EAAs must be consumed at the same time as HMB
  • The rate of protein breakdown must be accelerated

However, an increase in protein breakdown would only undermine the beneficial effect of an increase in protein synthesis, as protein gain is the result of the balance between protein synthesis and breakdown. Thus, supplemental doses of HMB can only result in a sustained increase in the net gain of muscle protein if consumed at the same time as an abundant supply of EAAs.

Benefits of HMB Supplements

All this being said, there are still a few conditions—such as catabolic states involving rapid muscle loss—that may benefit from HMB supplementation. This is because protein breaks down much more rapidly in catabolic states such as critical illness or HIV.

This protein breakdown provides extra EAAs that would, under normal conditions, be oxidized. In these situations of increased EAA availability that occur during catabolic states, the anti-catabolic action of HMB may help maintain muscle mass and function and decrease the rate of muscle protein breakdown.

However, recommendations for catabolic states generally specify that HMB should be included as part of a multifaceted approach for muscle maintenance that also incorporates resistance training and a high-protein diet for EAA maintenance.

Exercise also accelerates muscle breakdown (via muscle damage that occurs as a natural part of muscle use) and EAA oxidation. Consequently, the use of supplemental HMB may result in improved performance by improving the reutilization of EAAs released by protein breakdown for the synthesis of new protein.

Is HMB Better Than EAAs Featuring Leucine?

The body’s response to dietary supplementation with HMB alone is similar to that resulting from supplementation with leucine alone.

Just as HMB requires the presence of elevated levels of all the EAAs, so, too, does leucine require the other EAAs to be effective. In addition, the body’s response is more robust when leucine is included as part of a mixture of all the other EAAs than when it (or HMB) is used alone.

Two studies performed in the same laboratory, using the exact same protocol, demonstrate this most clearly. In one experiment, the effectiveness of HMB was assessed, and in the other experiment, the effectiveness of a mixture of EAAs (containing about 40% leucine) was determined.

Both studies investigated how effective HMB and EAA supplements were, compared with a placebo, at diminishing the loss in muscle mass and function that normally occurs with inactivity.

The subjects tested were over the age of 65, and both lean body mass and performance on various physical function tests were measured before and after 10 days of strict bed rest.

In the first study, following 10 days of bed rest, participants were put through a strength training program for a period of 8 weeks. In addition, beginning 5 days prior to bed rest and lasting until the end of the rehabilitation phase, the control group received a placebo powder and the subjects in the experimental group received 1.5 grams of HMB twice daily in its calcium salt form, for a total of 10 weeks of supplementation.

In the second study, participants in the control group received a placebo, while subjects in the experimental group received 15 grams of EAAs 3 times a day throughout the entire 10 days of bed rest. However, in this study, neither group received any weight training.

When comparing the data collected on all the subjects included in these studies, it becomes clear that the major differences between HMB and EAAs can be seen in terms of the tests of physical function—all of which have been validated as representative of the normal physical requirements for activities of daily living in older adults.

While the placebo group had major impairments in all tests of physical function after 10 days of bed rest, those given EAA supplementation—but not HMB supplementation—had significantly improved outcomes.

For example, the time required for subjects to go from a standing position to the floor and back up again (floor transfer test) increased by approximately 40% in the placebo group. Floor transfer rate was also not significantly affected by HMB supplementation. However, the group given EAA supplementation shortened their floor transfer time by 6%.

In another example, the time required to walk up a flight of stairs increased by 18% in the placebo group. HMB once again had no beneficial effect on this response, but those receiving EAA supplementation showed virtually no increase in the amount of time it took them to perform this task.

Finally, the number of toe raises (test of foot flexibility) that could be completed in 1 minute was reduced by almost 80% in both the control group and the HMB supplementation group, whereas the loss of this function with bed rest was completely prevented with EAA supplementation.

These bed rest studies are the only direct comparison that’s been completed of the muscle-building effects and strength gains provided by dietary supplementation with HMB and a formulation of EAAs. Yet the results clearly demonstrate the beneficial effects of EAAs in preventing declines in physical function and fail to demonstrate any beneficial effect of HMB alone.

These results are also consistent with the fact that stimulation of protein synthesis requires the availability of excess amounts of all component amino acids—especially EAAs.

While HMB’s activation of mTOR and other molecules involved in the initiation of protein synthesis may result in a transient increase in muscle protein synthesis, this increase can’t be sustained at a rate sufficient to result in improvements in physical function.

The HMB Takeaway

HMB is widely promoted as a muscle-building molecule that stimulates protein synthesis. While in some cases HMB supplementation may provide benefits, direct comparison with EAA supplementation highlights the fact that any benefit provided by HMB is minimal.

Whatever molecular signaling occurs as a result of HMB supplementation can instead be achieved by taking an EAA supplement that contains leucine. The availability of all EAAs—which are not present in HMB supplements—in excess amounts is required for a sustained increase in protein synthesis, muscle cell growth, and body composition changes that result in greater lean mass versus fat mass.

Furthermore, combining HMB with EAAs would not be expected to be particularly helpful, as the EAAs would elicit the action of HMB on their own.

HMB Supplements

How Essential Amino Acids Can Prevent and Even Reverse Age-Related Muscle Loss

Muscle loss with aging is one of the inescapable characteristics of growing older. While age-related muscle loss is a normal part of the aging process, we can temper its effect with the nutritional support of essential amino acids.

Muscle loss with aging is one of the inescapable characteristics of growing older. While age-related muscle loss is a normal part of the aging process, we can temper its effect with the nutritional support of essential amino acids (EAAs).

It’s Never Too Early to Combat Age-Related Muscle Loss

There’s nothing wrong with embracing the mentality that 40 is the new 20, but don’t fool yourself into believing age is nothing more than a number. Growing older does come with certain physiological changes. Yet there’s no reason your golden years can’t be every bit as vibrant as your youth. And the sooner you acknowledge how the passage of time influences certain biological processes, the better off you’ll be.

As you grow older, age-related muscle loss, which scientists refer to as sarcopenia or age-related sarcopenia, begins to erode your lean muscle mass. This process likely begins earlier than you think. Once you reach the age of 30, you begin to lose between 3% and 8% of your overall muscle mass each decade. The rate of decline increases once you turn 60.

Understanding Anabolic Resistance

Muscle loss with aging occurs because as the years wear on, we lose the ability to make new muscle protein from dietary protein. The impaired ability to build new muscle protein is called anabolic resistance.

When your body enters an anabolic resistant state, it has trouble getting the motor started. The starter for the motor, in this case, is a factor inside the muscle cells called mTOR. mTOR starts the whole process of protein synthesis. The activation of mTOR begins a cascade of responses that ultimately result in the initiation of protein synthesis. Together these responses are called initiation factors.

In aging muscle, the reactivity of mTOR and the other initiation factors is blunted, and this is a basis of anabolic resistance.

The Vicious Cycle of Age-Related Sarcopenia

This ongoing loss of skeletal muscle mass leaves older adults with less control over their bodies. Age-related changes to your muscle tissue and muscle strength don’t just influence your ability to excel during a strength-training workout, they also make you more prone to falls and other types of injuries.

Age-related sarcopenia can kick off a vicious cycle: your muscle strength decreases, which limits your ability to carry out physical activity, which causes further muscle loss. Ultimately, this can result in what health care professionals refer to as frailty, a condition that leaves you extra susceptible to external stressors more hearty individuals would be able to navigate with few to no lasting consequences.

Researchers have identified age-related sarcopenia as the primary factor behind the frailty we associate with aging, such as an increased propensity to fall, compounded by a higher likelihood of suffering an injury such as a broken hip due to a fall and the decreased ability to heal in the aftermath of such an injury.

The more frail you become, the greater the impact of each stressor. As the adverse effects of minor illnesses and injuries accumulate, individuals find it more and more challenging to live independently. Increased frailty also heightens the risk of early death.

Muscle loss with aging is one of the inescapable characteristics of growing older. While age-related muscle loss is a normal part of the aging process, we can temper its effect with the nutritional support of essential amino acids (EAAs). It's Never Too Early to Combat Age-Related Muscle Loss There's nothing wrong with embracing the mentality that 40 is the new 20, but don't fool yourself into believing age is nothing more than a number. Growing older does come with certain physiological changes. Yet there's no reason your golden years can't be every bit as vibrant as your youth. And the sooner you acknowledge how the passage of time influences certain biological processes, the better off you'll be. As you grow older, age-related muscle loss, which scientists refer to as sarcopenia or age-related sarcopenia, begins to erode your lean muscle mass. This process likely begins earlier than you think. Once you reach the age of 30, you begin to lose between 3% and 8% of your overall muscle mass each decade. The rate of decline increases once you turn 60. Understanding Anabolic Resistance Muscle loss with aging occurs because as the years wear on, we lose the ability to make new muscle protein from dietary protein. The impaired ability to build new muscle protein is called anabolic resistance. When your body enters an anabolic resistant state, it has trouble getting the motor started. The starter for the motor, in this case, is a factor inside the muscle cells called mTOR. mTOR starts the whole process of protein synthesis. The activation of mTOR begins a cascade of responses that ultimately result in the initiation of protein synthesis. Together these responses are called initiation factors. In aging muscle, the reactivity of mTOR and the other initiation factors are blunted, and this is a basis of anabolic resistance. The Vicious Cycle of Age-Related Sarcopenia This ongoing loss of skeletal muscle mass leaves older adults with less control over their bodies. Age-related changes to your muscle tissue and muscle strength don't just influence your ability to excel during a strength-training workout, they also make you more prone to falls and other types of injuries. Age-related sarcopenia can kick off a vicious cycle: your muscle strength decreases, which limits your ability to carry out physical activity, which causes further muscle loss. Ultimately, this can result in what health care professionals refer to as frailty, a condition that leaves you extra-susceptible to external stressors more hearty individuals would be able to navigate with few to no lasting consequences. Researchers have identified age-related sarcopenia as the primary factor behind the frailty we associate with aging, such as an increased propensity to fall, compounded by a higher likelihood of suffering an injury such as a broken hip due to a fall and the decreased ability to heal in the aftermath of such an injury. The more frail you become, the greater the impact of each stressor. As the adverse effects of minor illnesses and injuries accumulate, individuals find it more and more challenging to live independently. Increased frailty also heightens the risk of early death. [infographic] How Muscle Loss Creates a Downward Spiral As your muscle strength decreases, it becomes more difficult to be physically active. This results in more lost muscle mass and strength, which can culminate in what health care professionals refer to as frailty. Frailty makes you more susceptible to stressors like illness and injury. The more frail you are, the greater the damage done by each subsequent stressor. Ultimately, it becomes more and more difficult for frail individuals to live on their own. Becoming increasingly frail also raises your risk of early death. [/infographic] While that all sounds grim, you have the ability to preserve—and even increase—your muscle mass as you grow older. Physical activity such as resistance exercise inarguably plays a vital role in preserving muscle mass as you age; however, nutrition will have just as strong—if not an even stronger—influence on your ability to preserve and build muscle. Optimizing Your Nutrient Intake to Combat Muscle Loss As you may be aware, when it comes to providing your muscle fibers with the optimized nutrition they need to maintain themselves and grow, protein is the macronutrient to prioritize. When you don't provide your body with enough protein, your body will lose the ability to keep up muscle mass and bone density. Determining your ideal protein intake can be challenging. Studies have shown that many factors affect the quantity of protein your body requires on a daily basis, such as: Age Gender Physical activity habits Muscle mass to fat ratio Keep in mind, too, that your muscle mass to fat ratio differs from your body mass index (BMI). It's entirely possible to be quite thin and still have high levels of fat compared to lean muscle, which increases the likelihood that you'll develop age-related sarcopenia. According to findings published in Current Opinion in Clinical Nutrition and Metabolic Care, eating between 25 grams and 30 grams of protein with each meal "maximally stimulates muscle protein synthesis in both young and older adults." The authors noted, however, that when elderly subjects consumed protein and carbohydrates together or ate less than 20 grams of protein per meal, that blunted muscle protein synthesis. Choosing the right protein sources will ensure each gram does the most work. When it comes to selecting protein sources, there's one element you should pay the closest attention to: their amino acid content. If you're aging and seeking to combat muscle wasting, you'll benefit the most from increasing your intake of an amino acid called leucine. Why Leucine Matters So Much Leucine, an essential amino acid (EAA) called a branched-chain amino acid (BCAA) because of its chemical structure, is one of the most important dietary regulators of mTOR activity. If the proportion of leucine in an essential amino acid mixture is increased to an amount that exceeds its normal contribution to the composition of dietary protein, that EAA supplement can then effectively activate mTOR in aging muscle. However, leucine alone is not enough. You may have noticed that I did not recommend taking a leucine supplement, but rather an amino acid supplement formulated to contain a higher concentration of leucine. That's because all nine essential amino acids need to be present in the proper proportion to produce new muscle protein. You can think of leucine as the quarterback of a football team—it may be the pivot point of how the team performs, but without the other players the team is not going to have much success. How the Other 8 Essential Amino Acids Contribute When you consume a large amount of the EAA leucine, you increase the rate at which leucine gets broken down since the body is designed to maintain steady levels of EAAs. And since the enzyme that breaks down leucine is also responsible for metabolizing the other two essential BCAAs, valine and isoleucine, they also get broken down at an increased rate. Consequently, the proportions of valine and isoleucine in an EAA formulation containing abundant leucine must also be increased. Lysine is another EAA with distinct characteristics—it is not transported into muscle as readily as other EAAs are. For this reason, the optimal profile of EAAs to maximally stimulate anabolic-resistant muscle includes proportionately more lysine than is reflected in the composition of muscle protein. So, even though it may seem logical to provide EAAs for a muscle-building supplement in a profile similar to the makeup of muscle, adjustments can be made to boost the signal and improve delivery of amino acids to overcome the anabolic resistance that results in muscle loss. The remaining five EAAs—phenylalanine, threonine, methionine, tryptophan, and histidine—also need to be included in a mixture of EAAs to maximally stimulate muscle protein synthesis. In order to include disproportionately high amounts of BCAAs and lysine, however, the proportionate contribution of these additional EAAs must be reduced below what occurs in muscle protein. [infographic] Building an Optimal Essential Amino Acid Blend to Address Age-Related Muscle Loss First and foremost, you'll want high concentrations of leucine, an EAA and BCAA. Leucine activates mTOR in aging muscle, helping to stimulate maintenance and growth. You'll also need all the other EAAs—think of leucine like a quarterback. No matter how skillful that player is, he still needs the rest of his team to win. For the best results, you'll want to increase the proportions of the other two essential BCAAs, valine and isoleucine. You'll also want to up the lysine content. To make room for these adjustments, you'll need to scale back on the amount of phenylalanine, threonine, methionine, tryptophan and histidine you include. [/infographic] The Science Behind How Essential Amino Acids Prevent and Reverse Age-Related Muscle Loss A wealth of research has been conducted on the link between amino acids and age-related declines in protein metabolism, muscle function, muscle growth, and more. The scientists behind one study set out to examine how an amino acid mixture enriched with leucine affected muscle protein metabolism in both young and elderly subjects. They found that ingesting the enriched EAA mixture resolved anabolic resistance in elderly subjects. The mixture of EAAs was 3 times more effective at stimulating muscle protein synthesis in older individuals on a gram-per-gram basis than was whey protein isolate, which is a very high-quality protein by traditional means of assessment. Another study showed that a specifically formulated EAA supplement decreased loss of muscle mass and strength that occurs with bed rest and recovery from hip replacement. This is especially relevant when it comes to preventing muscle loss associated with aging, as older individuals are more likely to experience extended hospitalization and more likely to suffer adverse consequences from the inactivity imposed by hospital stays. Yet another study demonstrated that daily supplementation with EAAs improved muscle mass and function in healthy, active elderly women. The authors wanted to determine whether essential amino acid supplementation improves post-absorptive muscle protein fractional synthesis rate, lean body mass, muscle strength, and other physiological processes. The randomized, double-blinded, placebo-controlled trial found that ingesting the essential amino acid blend stimulated the muscle protein fractional synthesis rate as well as IGF-1 protein expression. Overall, the authors concluded that EAA supplementation improved lean body mass as well as muscle protein synthesis and that it could be a means of offsetting the "debilitating effects" of age-related sarcopenia. [infographic] 5 Science-Backed Ways EAAs Offset Age-Related Muscle Loss Researchers have shown that an amino acid blend enriched with leucine resolved anabolic resistance in elderly subjects. An essential amino acid blend proved 3 times more effective at stimulating muscle protein synthesis than whey protein isolate. An EAA supplement reduced losses of muscle mass and strength related to bed rest. Daily supplementation with EAAs can improve muscle mass and function. Studies show that EAAs can improve lean body mass and muscle protein synthesis, making them a possible means of treating age-related sarcopenia. [/infographic] Key Takeaways to Help You Remain Healthy and Vital as You Age Experts from across the globe agree that both the loss of muscle mass and the loss of muscle strength are highly prevalent and important risk factors for disability and potential mortality as individuals age. This makes identifying treatments for age-related muscle loss a key priority when it comes not only to improving average life expectancy for older people, but also reducing health care costs and enhancing overall quality of life. Ensuring an optimal protein intake will form a foundational part of any successful strategy for maintaining muscle mass (and bone density!) as you age. The kind of protein you eat will be just as impactful as the amount. Leucine, an EAA and BCAA found in certain protein sources, makes uniquely significant contributions to the muscle maintenance and growth processes within the human body. Consuming amino acid supplements designed to contain higher concentrations of leucine (as well as certain other helper amino acids) can dramatically influence your body's ability to retain and increase lean muscle mass as you age. The difference between the effectiveness of EAAs and intact protein cannot be made up just by consuming more of the intact protein, because the optimal profile of EAAs will never be achieved with intact protein. If you're interested in learning more about the advantages of essential amino acid supplements compared to dietary protein sources, this article is an excellent place to start. And if you'd like a quick takeaway in a nutshell, here it is: when it comes to amino acids for muscle loss with aging, it’s a matter of quality, not quantity.

While that all sounds grim, you have the ability to preserve—and even increase—your muscle mass as you grow older.

Physical activity such as resistance exercise inarguably plays a vital role in preserving muscle mass as you age; however, nutrition will have just as strong—if not an even stronger—influence on your ability to preserve and build muscle.

Optimizing Your Nutrient Intake to Combat Muscle Loss

As you may be aware, when it comes to providing your muscle fibers with the optimized nutrition they need to maintain themselves and grow, protein is the macronutrient to prioritize. When you don’t provide your body with enough protein, your body will lose the ability to keep up muscle mass and bone density.

Determining your ideal protein intake can be challenging. Studies have shown that many factors affect the quantity of protein your body requires on a daily basis, such as:

  • Age
  • Gender
  • Physical activity habits
  • Muscle mass to fat ratio

Keep in mind, too, that your muscle mass to fat ratio differs from your body mass index (BMI). It’s entirely possible to be quite thin and still have high levels of fat compared to lean muscle, which increases the likelihood that you’ll develop age-related sarcopenia.

According to findings published in Current Opinion in Clinical Nutrition and Metabolic Care, eating between 25 grams and 30 grams of protein with each meal “maximally stimulates muscle protein synthesis in both young and older adults.” The authors noted, however, that when elderly subjects consumed protein and carbohydrates together or ate less than 20 grams of protein per meal, that blunted muscle protein synthesis.

Choosing the right protein sources will ensure each gram does the most work. When it comes to selecting protein sources, there’s one element you should pay the closest attention to: their amino acid content. If you’re aging and seeking to combat muscle wasting, you’ll benefit the most from increasing your intake of an amino acid called leucine.

Why Leucine Matters So Much

Leucine, an essential amino acid (EAA) called a branched-chain amino acid (BCAA) because of its chemical structure, is one of the most important dietary regulators of mTOR activity. If the proportion of leucine in an essential amino acid mixture is increased to an amount that exceeds its normal contribution to the composition of dietary protein, that EAA supplement can then effectively activate mTOR in aging muscle.

However, leucine alone is not enough. You may have noticed that I did not recommend taking a leucine supplement, but rather an amino acid supplement formulated to contain a higher concentration of leucine. That’s because all nine essential amino acids need to be present in the proper proportion to produce new muscle protein.

You can think of leucine as the quarterback of a football team—it may be the pivot point of how the team performs, but without the other players the team is not going to have much success.

How the Other 8 Essential Amino Acids Contribute

When you consume a large amount of the EAA leucine, you increase the rate at which leucine gets broken down since the body is designed to maintain steady levels of EAAs. And since the enzyme that breaks down leucine is also responsible for metabolizing the other two essential BCAAs, valine and isoleucine, they also get broken down at an increased rate. Consequently, the proportions of valine and isoleucine in an EAA formulation containing abundant leucine must also be increased.

Lysine is another EAA with distinct characteristics—it is not transported into muscle as readily as other EAAs are. For this reason, the optimal profile of EAAs to maximally stimulate anabolic-resistant muscle includes proportionately more lysine than is reflected in the composition of muscle protein.

So, even though it may seem logical to provide EAAs for a muscle-building supplement in a profile similar to the makeup of muscle, adjustments can be made to boost the signal and improve delivery of amino acids to overcome the anabolic resistance that results in muscle loss.

The remaining five EAAs—phenylalanine, threonine, methionine, tryptophan, and histidine—also need to be included in a mixture of EAAs to maximally stimulate muscle protein synthesis. In order to include disproportionately high amounts of BCAAs and lysine, however, the proportionate contribution of these additional EAAs must be reduced below what occurs in muscle protein.

Muscle loss with aging is one of the inescapable characteristics of growing older. While age-related muscle loss is a normal part of the aging process, we can temper its effect with the nutritional support of essential amino acids (EAAs). It's Never Too Early to Combat Age-Related Muscle Loss There's nothing wrong with embracing the mentality that 40 is the new 20, but don't fool yourself into believing age is nothing more than a number. Growing older does come with certain physiological changes. Yet there's no reason your golden years can't be every bit as vibrant as your youth. And the sooner you acknowledge how the passage of time influences certain biological processes, the better off you'll be. As you grow older, age-related muscle loss, which scientists refer to as sarcopenia or age-related sarcopenia, begins to erode your lean muscle mass. This process likely begins earlier than you think. Once you reach the age of 30, you begin to lose between 3% and 8% of your overall muscle mass each decade. The rate of decline increases once you turn 60. Understanding Anabolic Resistance Muscle loss with aging occurs because as the years wear on, we lose the ability to make new muscle protein from dietary protein. The impaired ability to build new muscle protein is called anabolic resistance. When your body enters an anabolic resistant state, it has trouble getting the motor started. The starter for the motor, in this case, is a factor inside the muscle cells called mTOR. mTOR starts the whole process of protein synthesis. The activation of mTOR begins a cascade of responses that ultimately result in the initiation of protein synthesis. Together these responses are called initiation factors. In aging muscle, the reactivity of mTOR and the other initiation factors are blunted, and this is a basis of anabolic resistance. The Vicious Cycle of Age-Related Sarcopenia This ongoing loss of skeletal muscle mass leaves older adults with less control over their bodies. Age-related changes to your muscle tissue and muscle strength don't just influence your ability to excel during a strength-training workout, they also make you more prone to falls and other types of injuries. Age-related sarcopenia can kick off a vicious cycle: your muscle strength decreases, which limits your ability to carry out physical activity, which causes further muscle loss. Ultimately, this can result in what health care professionals refer to as frailty, a condition that leaves you extra-susceptible to external stressors more hearty individuals would be able to navigate with few to no lasting consequences. Researchers have identified age-related sarcopenia as the primary factor behind the frailty we associate with aging, such as an increased propensity to fall, compounded by a higher likelihood of suffering an injury such as a broken hip due to a fall and the decreased ability to heal in the aftermath of such an injury. The more frail you become, the greater the impact of each stressor. As the adverse effects of minor illnesses and injuries accumulate, individuals find it more and more challenging to live independently. Increased frailty also heightens the risk of early death. [infographic] How Muscle Loss Creates a Downward Spiral As your muscle strength decreases, it becomes more difficult to be physically active. This results in more lost muscle mass and strength, which can culminate in what health care professionals refer to as frailty. Frailty makes you more susceptible to stressors like illness and injury. The more frail you are, the greater the damage done by each subsequent stressor. Ultimately, it becomes more and more difficult for frail individuals to live on their own. Becoming increasingly frail also raises your risk of early death. [/infographic] While that all sounds grim, you have the ability to preserve—and even increase—your muscle mass as you grow older. Physical activity such as resistance exercise inarguably plays a vital role in preserving muscle mass as you age; however, nutrition will have just as strong—if not an even stronger—influence on your ability to preserve and build muscle. Optimizing Your Nutrient Intake to Combat Muscle Loss As you may be aware, when it comes to providing your muscle fibers with the optimized nutrition they need to maintain themselves and grow, protein is the macronutrient to prioritize. When you don't provide your body with enough protein, your body will lose the ability to keep up muscle mass and bone density. Determining your ideal protein intake can be challenging. Studies have shown that many factors affect the quantity of protein your body requires on a daily basis, such as: Age Gender Physical activity habits Muscle mass to fat ratio Keep in mind, too, that your muscle mass to fat ratio differs from your body mass index (BMI). It's entirely possible to be quite thin and still have high levels of fat compared to lean muscle, which increases the likelihood that you'll develop age-related sarcopenia. According to findings published in Current Opinion in Clinical Nutrition and Metabolic Care, eating between 25 grams and 30 grams of protein with each meal "maximally stimulates muscle protein synthesis in both young and older adults." The authors noted, however, that when elderly subjects consumed protein and carbohydrates together or ate less than 20 grams of protein per meal, that blunted muscle protein synthesis. Choosing the right protein sources will ensure each gram does the most work. When it comes to selecting protein sources, there's one element you should pay the closest attention to: their amino acid content. If you're aging and seeking to combat muscle wasting, you'll benefit the most from increasing your intake of an amino acid called leucine. Why Leucine Matters So Much Leucine, an essential amino acid (EAA) called a branched-chain amino acid (BCAA) because of its chemical structure, is one of the most important dietary regulators of mTOR activity. If the proportion of leucine in an essential amino acid mixture is increased to an amount that exceeds its normal contribution to the composition of dietary protein, that EAA supplement can then effectively activate mTOR in aging muscle. However, leucine alone is not enough. You may have noticed that I did not recommend taking a leucine supplement, but rather an amino acid supplement formulated to contain a higher concentration of leucine. That's because all nine essential amino acids need to be present in the proper proportion to produce new muscle protein. You can think of leucine as the quarterback of a football team—it may be the pivot point of how the team performs, but without the other players the team is not going to have much success. How the Other 8 Essential Amino Acids Contribute When you consume a large amount of the EAA leucine, you increase the rate at which leucine gets broken down since the body is designed to maintain steady levels of EAAs. And since the enzyme that breaks down leucine is also responsible for metabolizing the other two essential BCAAs, valine and isoleucine, they also get broken down at an increased rate. Consequently, the proportions of valine and isoleucine in an EAA formulation containing abundant leucine must also be increased. Lysine is another EAA with distinct characteristics—it is not transported into muscle as readily as other EAAs are. For this reason, the optimal profile of EAAs to maximally stimulate anabolic-resistant muscle includes proportionately more lysine than is reflected in the composition of muscle protein. So, even though it may seem logical to provide EAAs for a muscle-building supplement in a profile similar to the makeup of muscle, adjustments can be made to boost the signal and improve delivery of amino acids to overcome the anabolic resistance that results in muscle loss. The remaining five EAAs—phenylalanine, threonine, methionine, tryptophan, and histidine—also need to be included in a mixture of EAAs to maximally stimulate muscle protein synthesis. In order to include disproportionately high amounts of BCAAs and lysine, however, the proportionate contribution of these additional EAAs must be reduced below what occurs in muscle protein. [infographic] Building an Optimal Essential Amino Acid Blend to Address Age-Related Muscle Loss First and foremost, you'll want high concentrations of leucine, an EAA and BCAA. Leucine activates mTOR in aging muscle, helping to stimulate maintenance and growth. You'll also need all the other EAAs—think of leucine like a quarterback. No matter how skillful that player is, he still needs the rest of his team to win. For the best results, you'll want to increase the proportions of the other two essential BCAAs, valine and isoleucine. You'll also want to up the lysine content. To make room for these adjustments, you'll need to scale back on the amount of phenylalanine, threonine, methionine, tryptophan and histidine you include. [/infographic] The Science Behind How Essential Amino Acids Prevent and Reverse Age-Related Muscle Loss A wealth of research has been conducted on the link between amino acids and age-related declines in protein metabolism, muscle function, muscle growth, and more. The scientists behind one study set out to examine how an amino acid mixture enriched with leucine affected muscle protein metabolism in both young and elderly subjects. They found that ingesting the enriched EAA mixture resolved anabolic resistance in elderly subjects. The mixture of EAAs was 3 times more effective at stimulating muscle protein synthesis in older individuals on a gram-per-gram basis than was whey protein isolate, which is a very high-quality protein by traditional means of assessment. Another study showed that a specifically formulated EAA supplement decreased loss of muscle mass and strength that occurs with bed rest and recovery from hip replacement. This is especially relevant when it comes to preventing muscle loss associated with aging, as older individuals are more likely to experience extended hospitalization and more likely to suffer adverse consequences from the inactivity imposed by hospital stays. Yet another study demonstrated that daily supplementation with EAAs improved muscle mass and function in healthy, active elderly women. The authors wanted to determine whether essential amino acid supplementation improves post-absorptive muscle protein fractional synthesis rate, lean body mass, muscle strength, and other physiological processes. The randomized, double-blinded, placebo-controlled trial found that ingesting the essential amino acid blend stimulated the muscle protein fractional synthesis rate as well as IGF-1 protein expression. Overall, the authors concluded that EAA supplementation improved lean body mass as well as muscle protein synthesis and that it could be a means of offsetting the "debilitating effects" of age-related sarcopenia. [infographic] 5 Science-Backed Ways EAAs Offset Age-Related Muscle Loss Researchers have shown that an amino acid blend enriched with leucine resolved anabolic resistance in elderly subjects. An essential amino acid blend proved 3 times more effective at stimulating muscle protein synthesis than whey protein isolate. An EAA supplement reduced losses of muscle mass and strength related to bed rest. Daily supplementation with EAAs can improve muscle mass and function. Studies show that EAAs can improve lean body mass and muscle protein synthesis, making them a possible means of treating age-related sarcopenia. [/infographic] Key Takeaways to Help You Remain Healthy and Vital as You Age Experts from across the globe agree that both the loss of muscle mass and the loss of muscle strength are highly prevalent and important risk factors for disability and potential mortality as individuals age. This makes identifying treatments for age-related muscle loss a key priority when it comes not only to improving average life expectancy for older people, but also reducing health care costs and enhancing overall quality of life. Ensuring an optimal protein intake will form a foundational part of any successful strategy for maintaining muscle mass (and bone density!) as you age. The kind of protein you eat will be just as impactful as the amount. Leucine, an EAA and BCAA found in certain protein sources, makes uniquely significant contributions to the muscle maintenance and growth processes within the human body. Consuming amino acid supplements designed to contain higher concentrations of leucine (as well as certain other helper amino acids) can dramatically influence your body's ability to retain and increase lean muscle mass as you age. The difference between the effectiveness of EAAs and intact protein cannot be made up just by consuming more of the intact protein, because the optimal profile of EAAs will never be achieved with intact protein. If you're interested in learning more about the advantages of essential amino acid supplements compared to dietary protein sources, this article is an excellent place to start. And if you'd like a quick takeaway in a nutshell, here it is: when it comes to amino acids for muscle loss with aging, it’s a matter of quality, not quantity.

The Science Behind How Essential Amino Acids Prevent and Reverse Age-Related Muscle Loss

A wealth of research has been conducted on the link between amino acids and age-related declines in protein metabolism, muscle function, muscle growth, and more.

The scientists behind one study set out to examine how an amino acid mixture enriched with leucine affected muscle protein metabolism in both young and elderly subjects. They found that ingesting the enriched EAA mixture resolved anabolic resistance in elderly subjects. The mixture of EAAs was 3 times more effective at stimulating muscle protein synthesis in older individuals on a gram-per-gram basis than was whey protein isolate, which is a very high-quality protein by traditional means of assessment.

Another study showed that a specifically formulated EAA supplement decreased loss of muscle mass and strength that occurs with bed rest and recovery from hip replacement. This is especially relevant when it comes to preventing muscle loss associated with aging, as older individuals are more likely to experience extended hospitalization and more likely to suffer adverse consequences from the inactivity imposed by hospital stays.

Yet another study demonstrated that daily supplementation with EAAs improved muscle mass and function in healthy, active elderly women. The authors wanted to determine whether essential amino acid supplementation improves post-absorptive muscle protein fractional synthesis rate, lean body mass, muscle strength, and other physiological processes. The randomized, double-blinded, placebo-controlled trial found that ingesting the essential amino acid blend stimulated the muscle protein fractional synthesis rate as well as IGF-1 protein expression. Overall, the authors concluded that EAA supplementation improved lean body mass as well as muscle protein synthesis and that it could be a means of offsetting the “debilitating effects” of age-related sarcopenia.

Muscle loss with aging is one of the inescapable characteristics of growing older. While age-related muscle loss is a normal part of the aging process, we can temper its effect with the nutritional support of essential amino acids (EAAs). It's Never Too Early to Combat Age-Related Muscle Loss There's nothing wrong with embracing the mentality that 40 is the new 20, but don't fool yourself into believing age is nothing more than a number. Growing older does come with certain physiological changes. Yet there's no reason your golden years can't be every bit as vibrant as your youth. And the sooner you acknowledge how the passage of time influences certain biological processes, the better off you'll be. As you grow older, age-related muscle loss, which scientists refer to as sarcopenia or age-related sarcopenia, begins to erode your lean muscle mass. This process likely begins earlier than you think. Once you reach the age of 30, you begin to lose between 3% and 8% of your overall muscle mass each decade. The rate of decline increases once you turn 60. Understanding Anabolic Resistance Muscle loss with aging occurs because as the years wear on, we lose the ability to make new muscle protein from dietary protein. The impaired ability to build new muscle protein is called anabolic resistance. When your body enters an anabolic resistant state, it has trouble getting the motor started. The starter for the motor, in this case, is a factor inside the muscle cells called mTOR. mTOR starts the whole process of protein synthesis. The activation of mTOR begins a cascade of responses that ultimately result in the initiation of protein synthesis. Together these responses are called initiation factors. In aging muscle, the reactivity of mTOR and the other initiation factors are blunted, and this is a basis of anabolic resistance. The Vicious Cycle of Age-Related Sarcopenia This ongoing loss of skeletal muscle mass leaves older adults with less control over their bodies. Age-related changes to your muscle tissue and muscle strength don't just influence your ability to excel during a strength-training workout, they also make you more prone to falls and other types of injuries. Age-related sarcopenia can kick off a vicious cycle: your muscle strength decreases, which limits your ability to carry out physical activity, which causes further muscle loss. Ultimately, this can result in what health care professionals refer to as frailty, a condition that leaves you extra-susceptible to external stressors more hearty individuals would be able to navigate with few to no lasting consequences. Researchers have identified age-related sarcopenia as the primary factor behind the frailty we associate with aging, such as an increased propensity to fall, compounded by a higher likelihood of suffering an injury such as a broken hip due to a fall and the decreased ability to heal in the aftermath of such an injury. The more frail you become, the greater the impact of each stressor. As the adverse effects of minor illnesses and injuries accumulate, individuals find it more and more challenging to live independently. Increased frailty also heightens the risk of early death. [infographic] How Muscle Loss Creates a Downward Spiral As your muscle strength decreases, it becomes more difficult to be physically active. This results in more lost muscle mass and strength, which can culminate in what health care professionals refer to as frailty. Frailty makes you more susceptible to stressors like illness and injury. The more frail you are, the greater the damage done by each subsequent stressor. Ultimately, it becomes more and more difficult for frail individuals to live on their own. Becoming increasingly frail also raises your risk of early death. [/infographic] While that all sounds grim, you have the ability to preserve—and even increase—your muscle mass as you grow older. Physical activity such as resistance exercise inarguably plays a vital role in preserving muscle mass as you age; however, nutrition will have just as strong—if not an even stronger—influence on your ability to preserve and build muscle. Optimizing Your Nutrient Intake to Combat Muscle Loss As you may be aware, when it comes to providing your muscle fibers with the optimized nutrition they need to maintain themselves and grow, protein is the macronutrient to prioritize. When you don't provide your body with enough protein, your body will lose the ability to keep up muscle mass and bone density. Determining your ideal protein intake can be challenging. Studies have shown that many factors affect the quantity of protein your body requires on a daily basis, such as: Age Gender Physical activity habits Muscle mass to fat ratio Keep in mind, too, that your muscle mass to fat ratio differs from your body mass index (BMI). It's entirely possible to be quite thin and still have high levels of fat compared to lean muscle, which increases the likelihood that you'll develop age-related sarcopenia. According to findings published in Current Opinion in Clinical Nutrition and Metabolic Care, eating between 25 grams and 30 grams of protein with each meal "maximally stimulates muscle protein synthesis in both young and older adults." The authors noted, however, that when elderly subjects consumed protein and carbohydrates together or ate less than 20 grams of protein per meal, that blunted muscle protein synthesis. Choosing the right protein sources will ensure each gram does the most work. When it comes to selecting protein sources, there's one element you should pay the closest attention to: their amino acid content. If you're aging and seeking to combat muscle wasting, you'll benefit the most from increasing your intake of an amino acid called leucine. Why Leucine Matters So Much Leucine, an essential amino acid (EAA) called a branched-chain amino acid (BCAA) because of its chemical structure, is one of the most important dietary regulators of mTOR activity. If the proportion of leucine in an essential amino acid mixture is increased to an amount that exceeds its normal contribution to the composition of dietary protein, that EAA supplement can then effectively activate mTOR in aging muscle. However, leucine alone is not enough. You may have noticed that I did not recommend taking a leucine supplement, but rather an amino acid supplement formulated to contain a higher concentration of leucine. That's because all nine essential amino acids need to be present in the proper proportion to produce new muscle protein. You can think of leucine as the quarterback of a football team—it may be the pivot point of how the team performs, but without the other players the team is not going to have much success. How the Other 8 Essential Amino Acids Contribute When you consume a large amount of the EAA leucine, you increase the rate at which leucine gets broken down since the body is designed to maintain steady levels of EAAs. And since the enzyme that breaks down leucine is also responsible for metabolizing the other two essential BCAAs, valine and isoleucine, they also get broken down at an increased rate. Consequently, the proportions of valine and isoleucine in an EAA formulation containing abundant leucine must also be increased. Lysine is another EAA with distinct characteristics—it is not transported into muscle as readily as other EAAs are. For this reason, the optimal profile of EAAs to maximally stimulate anabolic-resistant muscle includes proportionately more lysine than is reflected in the composition of muscle protein. So, even though it may seem logical to provide EAAs for a muscle-building supplement in a profile similar to the makeup of muscle, adjustments can be made to boost the signal and improve delivery of amino acids to overcome the anabolic resistance that results in muscle loss. The remaining five EAAs—phenylalanine, threonine, methionine, tryptophan, and histidine—also need to be included in a mixture of EAAs to maximally stimulate muscle protein synthesis. In order to include disproportionately high amounts of BCAAs and lysine, however, the proportionate contribution of these additional EAAs must be reduced below what occurs in muscle protein. [infographic] Building an Optimal Essential Amino Acid Blend to Address Age-Related Muscle Loss First and foremost, you'll want high concentrations of leucine, an EAA and BCAA. Leucine activates mTOR in aging muscle, helping to stimulate maintenance and growth. You'll also need all the other EAAs—think of leucine like a quarterback. No matter how skillful that player is, he still needs the rest of his team to win. For the best results, you'll want to increase the proportions of the other two essential BCAAs, valine and isoleucine. You'll also want to up the lysine content. To make room for these adjustments, you'll need to scale back on the amount of phenylalanine, threonine, methionine, tryptophan and histidine you include. [/infographic] The Science Behind How Essential Amino Acids Prevent and Reverse Age-Related Muscle Loss A wealth of research has been conducted on the link between amino acids and age-related declines in protein metabolism, muscle function, muscle growth, and more. The scientists behind one study set out to examine how an amino acid mixture enriched with leucine affected muscle protein metabolism in both young and elderly subjects. They found that ingesting the enriched EAA mixture resolved anabolic resistance in elderly subjects. The mixture of EAAs was 3 times more effective at stimulating muscle protein synthesis in older individuals on a gram-per-gram basis than was whey protein isolate, which is a very high-quality protein by traditional means of assessment. Another study showed that a specifically formulated EAA supplement decreased loss of muscle mass and strength that occurs with bed rest and recovery from hip replacement. This is especially relevant when it comes to preventing muscle loss associated with aging, as older individuals are more likely to experience extended hospitalization and more likely to suffer adverse consequences from the inactivity imposed by hospital stays. Yet another study demonstrated that daily supplementation with EAAs improved muscle mass and function in healthy, active elderly women. The authors wanted to determine whether essential amino acid supplementation improves post-absorptive muscle protein fractional synthesis rate, lean body mass, muscle strength, and other physiological processes. The randomized, double-blinded, placebo-controlled trial found that ingesting the essential amino acid blend stimulated the muscle protein fractional synthesis rate as well as IGF-1 protein expression. Overall, the authors concluded that EAA supplementation improved lean body mass as well as muscle protein synthesis and that it could be a means of offsetting the "debilitating effects" of age-related sarcopenia. [infographic] 5 Science-Backed Ways EAAs Offset Age-Related Muscle Loss Researchers have shown that an amino acid blend enriched with leucine resolved anabolic resistance in elderly subjects. An essential amino acid blend proved 3 times more effective at stimulating muscle protein synthesis than whey protein isolate. An EAA supplement reduced losses of muscle mass and strength related to bed rest. Daily supplementation with EAAs can improve muscle mass and function. Studies show that EAAs can improve lean body mass and muscle protein synthesis, making them a possible means of treating age-related sarcopenia. [/infographic] Key Takeaways to Help You Remain Healthy and Vital as You Age Experts from across the globe agree that both the loss of muscle mass and the loss of muscle strength are highly prevalent and important risk factors for disability and potential mortality as individuals age. This makes identifying treatments for age-related muscle loss a key priority when it comes not only to improving average life expectancy for older people, but also reducing health care costs and enhancing overall quality of life. Ensuring an optimal protein intake will form a foundational part of any successful strategy for maintaining muscle mass (and bone density!) as you age. The kind of protein you eat will be just as impactful as the amount. Leucine, an EAA and BCAA found in certain protein sources, makes uniquely significant contributions to the muscle maintenance and growth processes within the human body. Consuming amino acid supplements designed to contain higher concentrations of leucine (as well as certain other helper amino acids) can dramatically influence your body's ability to retain and increase lean muscle mass as you age. The difference between the effectiveness of EAAs and intact protein cannot be made up just by consuming more of the intact protein, because the optimal profile of EAAs will never be achieved with intact protein. If you're interested in learning more about the advantages of essential amino acid supplements compared to dietary protein sources, this article is an excellent place to start. And if you'd like a quick takeaway in a nutshell, here it is: when it comes to amino acids for muscle loss with aging, it’s a matter of quality, not quantity.

Key Takeaways to Help You Remain Healthy and Vital as You Age

Experts from across the globe agree that both the loss of muscle mass and the loss of muscle strength are highly prevalent and important risk factors for disability and potential mortality as individuals age. This makes identifying treatments for age-related muscle loss a key priority when it comes not only to improving average life expectancy for older people, but also reducing health care costs and enhancing overall quality of life.

Ensuring an optimal protein intake will form a foundational part of any successful strategy for maintaining muscle mass (and bone density!) as you age. The kind of protein you eat will be just as impactful as the amount. Leucine, an EAA and BCAA found in certain protein sources, makes uniquely significant contributions to the muscle maintenance and growth processes within the human body.

Consuming amino acid supplements designed to contain higher concentrations of leucine (as well as certain other helper amino acids) can dramatically influence your body’s ability to retain and increase lean muscle mass as you age.

The difference between the effectiveness of EAAs and intact protein cannot be made up just by consuming more of the intact protein, because the optimal profile of EAAs will never be achieved with intact protein. If you’re interested in learning more about the advantages of essential amino acid supplements compared to dietary protein sources, this article is an excellent place to start.

And if you’d like a quick takeaway in a nutshell, here it is: when it comes to amino acids for muscle loss with aging, it’s a matter of quality, not quantity.

The Relationship Between Energy and Amino Acids

Energy is one of the primary markers of health. When people are asked about their health, low energy is often a common complaint. What many people don’t realize, however, is that energy and amino acids go hand in hand.

Energy is one of the primary markers of health. When people are asked about their health, low energy is often a common complaint. Likewise, when people are asked to identify a benefit from a nutritional supplement, “improved energy” is often the first thing they report. What many people don’t realize, however, is that energy and amino acids go hand in hand.

Almost everyone, even the most energetic among us, desires more energy. So it’s no accident that energy drinks have become so popular. However, the concept of energy is somewhat vague. What does having energy really mean?

To understand the relationship between energy and amino acids, we must first distinguish between physical and mental energy. These two types of energy are clearly related, but distinct. By considering physical and mental energy separately, we can better understand the physiologic basis for each.

Energy and Amino Acids: What Fuels Our Bodies?

Physical energy requires not just fuel for our bodies but also all the necessary vitamins and cofactors—the inorganic substances needed for certain enzymes to carry out their functions—required to convert food to an energy form our cells can utilize.

Assuming all vitamins and cofactors are available, the energy necessary for physiologic functions is derived from combining carbohydrates, fats, proteins, and (in some cases) alcohol with oxygen in a process known as oxidation. These energy substrates—molecules acted on by an enzyme—can thus be considered the “fuel” of the body.

The major form of chemical energy in the body is a compound called adenosine triphosphate (ATP). Energy is released when ATP is broken down to adenosine diphosphate (ADP) and phosphate.

ATP is regenerated by the metabolism of the macronutrient (food required in large amounts for optimum nutrition) energy substrates mentioned above as well as by the oxidation of amino acids.

Chemical Energy and Mitochondria

The energy needed to perform physical functions such as exercise comes from the chemical energy stored in ATP. ATP is the universal fuel used by all cells.

In general, food is digested and absorbed as its basic components (glucose and other simple sugars, fatty acids, and amino acids), which are then used for structural needs, stored away, or oxidized for energy.

The oxidation of nutrients into chemical energy involves complex biochemical pathways. The Krebs cycle, named for its discoverer, Sir Hans Adolf Krebs—and also known as the citric acid or tricarboxylic acid (TCA) cycle—involves a series of chemical reactions in which carbon structures derived from carbohydrates, fats, and proteins are metabolized, with the production of ATP as a byproduct.

The TCA cycle operates inside mitochondria, which are specialized organelles within cells that are responsible for “digesting” nutrients and turning them into energy.

The energy and amino acid relationship.

Oxidation of Amino Acids for ATP Production

The majority of physical energy comes from the oxidation of fats and carbohydrates. However, every amino acid in the body can potentially be oxidized to produce ATP.

The amount of oxidation undergone by the essential amino acids (or EAAs)—the nine dietary amino acids that can’t be produced in the body and must be obtained from food—determines how much of each essential amino acid you need in a day.

The amount of protein synthesized by the body will decrease if a steady supply of EAAs is not maintained, leading to conditions such as muscle loss and impaired immune function. Therefore, any EAA that is oxidized must be replaced through the diet.

The oxidation of EAAs is important physiologically even though only a minimal amount of total energy production is derived from this process. For example, at rest, less than 10% of energy production comes from the oxidation of amino acids.

Exercise greatly increases the requirements for ATP, and part of that ATP comes from amino acid oxidation. This is one reason why the consumption of a number of whole foods and supplements, including whey protein, is recommended in the field of sports nutrition both pre-workout and post. However, amino acid oxidation does not increase uniformly during exercise.

Among the EAAs, there is a selective increase in the oxidation of leucine. However, even with the increase seen during exercise, leucine oxidation provides only about 3% to 4% of energy for ATP production. Yet leucine plays a crucial role in regulating protein synthesis and other metabolic processes, so extra leucine needs to be consumed after exercise to replace what was oxidized.

While amino acids, particularly EAAs, do not play a major role in overall energy production, there are a number of aspects of amino acid oxidation that are important for the body’s metabolic regulation. To understand the critical nature of EAA oxidation is to appreciate that the body regulates the availability of all EAAs at a relatively constant level.

Consuming a high-protein meal causes EAA availability to increase. This increased concentration of EAAs stimulates their oxidation and minimizes changes in EAA availability. By contrast, if you do not consume enough EAAs through your diet, metabolic adaptations occur that reduce the rate of EAA oxidation.

The oxidation of specific amino acids is important for the body. For example, the availability of certain amino acids depends on the oxidation of other amino acids.

Take tyrosine, for example. This amino acid is produced in the liver from the oxidation of the EAA phenylalanine. Maintaining an adequate amount of tyrosine in the blood is critical, as tyrosine is a precursor of the neurotransmitters dopamine, norepinephrine, and epinephrine.

Specific tissues and organs also have metabolic preferences for certain amino acids. Most prominently, glutamine (a nonessential amino acid) is a preferred substrate for the gut.

Amino Acids Augment Mitochondria

Only recently have we begun to appreciate the difference in energy levels the number of available mitochondria and their ability to operate at full capacity can make. Both amino acid supplementation and exercise are known to increase numbers of mitochondria and enhance their function.

By contrast, alcohol or drug use has been shown to induce mitochondrial defects by increasing oxidative stress and damaging mitochondrial genetic material—deoxynucleic acid, or DNA. When alcohol damages mitochondrial DNA, it impairs mitochondrial function, which further increases oxidative cell stress, leading to a vicious cycle of accumulating cell damage and decreased energy production over time.

Mental Energy: What Balances Our Brains?

Energy drinks typically contain caffeine (with a range of 6 to 242 mg of caffeine, according to Consumer Reports) and perhaps some B vitamins.

Whether used to help one wake up first thing in the morning or as an afternoon pick-me-up, these beverages clearly aid in sharpening concentration and increasing the body’s overall feeling of energy.

Surprisingly, when it comes to maintaining mental energy and focus, amino acids play as important a role as caffeine. In contrast to caffeine, however, amino acids impact mental energy by modulating neurotransmitters within the brain.

Many of the brain’s neurotransmitters are produced through the conversion of amino acids as they pass through the blood-brain barrier. In addition, two amino acids—glutamate and aspartate—are themselves considered neurotransmitters.

The interaction of neurotransmitters in the brain determines many aspects of behavior. To simplify a very complex system, the key determinant of mental energy is the balance between the neurotransmitters dopamine (excitatory) and serotonin (inhibitory).

The amounts of dopamine and serotonin in the brain are dependent on the availability of the precursors for their productionTyrosine is the amino acid precursor of dopamine, and tryptophan is the amino acid precursor of serotonin.

Tyrosine is also derived from the oxidation of phenylalanine. However, neither phenylalanine nor tryptophan is made in the body, as both are EAAs.

Increasing the amount of phenylalanine consumed in the diet will, via conversion to tyrosine, increase mental energy by increasing the amount of dopamine in the brain.

Conversely, increasing tryptophan consumption, such as through the use of the dietary supplement L-tryptophan, will induce a feeling of sleepiness or lack of energy by promoting serotonin production.

Amino Acid Balance and Mental and Physical Energy

Amino acids help support both physical and mental energy via a wide range of actions. While supplementation with individual amino acids may produce particular reactions, disrupting the body’s balance by consuming a single or small combination of amino acids may be counterproductive when it comes to other functions.

An amino acid supplement containing relatively high levels of phenylalanine (tyrosine is nearly insoluble and difficult to add to a dietary supplement) and low levels of tryptophan can provide mental sharpness and focus. However, an isolated increase in phenylalanine can also induce Parkinson-like symptoms in susceptible individuals.

Likewise, consumption of leucine can counter the accelerated rate of oxidation that occurs during exercise, but the use of leucine in isolation will activate the oxidation of valine and isoleucine, thereby limiting muscle protein synthesis.

Consequently, to replace the oxidized leucine and enhance post-workout muscle recovery, it is necessary to provide all three of the branched-chain amino acids, or BCAAs—leucine, isoleucine, and valine.

Finally, all EAAs must be available in sufficient quantities to stimulate muscle protein synthesis, which is the metabolic basis for increased muscle growth, strength, and function.

Hence, the gold standard approach for the maintenance of both mental and physical energy involves choosing a free-form amino acid formulation that takes into account not only the direct actions of the component amino acids but also the importance of maintaining a relative balance of EAAs to sustain maximal benefit.

Essential Amino Acid Supplements and Bariatric Surgery

Let’s take a look at the different types of bariatric surgery available, the benefits and risks of these procedures, and how amino acids can help you maintain the nutrition so important to your health both during recovery and long after this weight-loss procedure is over.

According to figures from the American Society for Metabolic and Bariatric Surgery (ASMBS), the number of Americans choosing to undergo bariatric surgery has risen steadily over the past several years, with over 200,000 undergoing the procedure in 2017 alone.

However, while the obesity epidemic leads more and more people to consider a surgical solution to excess weight, many may not realize that the physical changes to the digestive tract caused by bariatric surgery also result in changes to the body’s ability to absorb nutrition.

In this article, we’re going to take a look at the different types of bariatric surgery available, the benefits and risks of these procedures, and how amino acids can help you maintain the nutrition so important to your health both during recovery and long after the procedure is over.

Types of Bariatric Surgery

Bariatric surgery is performed on severely obese individuals who have not been able to lose weight with diet and exercise alone.

Generally, the procedure is not recommended unless you have extreme obesity, characterized by a body mass index (BMI) of 40 or greater, or a BMI of 35 and at least one obesity-related health problem, such as type 2 diabetes, high blood pressure, sleep apnea, or heart disease.

The surgery works by changing the shape of or removing portions of the stomach and (sometimes) small intestine. In the United States, three types of bariatric surgery procedures are most commonly performed:

  • Gastric bypass
  • Gastric banding
  • Gastric sleeve

Each type of surgery also has its advantages and disadvantages.

1. Roux-en-Y Gastric Bypass

The Roux-en-Y gastric bypass works by dividing both the top of the stomach from the bottom and the first part of the small intestine. The bottom end of the small intestine is then attached to the newly created pouch at the top of the stomach.

This procedure reduces both the amount of food the stomach pouch can hold at any one time and the small intestine’s ability to absorb calories and nutrients. This type of gastric bypass surgery is also typically not reversible.

2. Biliopancreatic Diversion with Duodenal Switch

In this second, more complicated form of gastric bypass, approximately 80% of the stomach is removed. The majority of the small intestine is then bypassed by connecting the end portion of the intestine to the duodenum.

Like the Roux-en-Y gastric bypass, this procedure works to reduce both stomach capacity and calorie and nutrient absorption. However, because it also carries with it more risks, the biliopancreatic diversion with duodenal switch is generally limited to people with a BMI greater than 50.

3. Laparoscopic Adjustable Gastric Banding

Gastric banding is a laparoscopic surgery in which an inflatable band, commonly known as a lap band, is placed around the upper portion of the stomach. When the band is inflated, it creates a small pouch that restricts the amount of food the upper portion of the stomach can hold.

4. Sleeve Gastrectomy

Gastric sleeve surgery actually makes use of the first part of the biliopancreatic diversion with duodenal switch, drastically reducing the size of the stomach until it’s shaped like a tube.

Benefits of Bariatric Surgery

Bariatric surgery can help patients avoid serious health problems by improving many of the health risks associated with severe obesity. These include:

In addition, the weight loss that results from bariatric surgery may improve mobility and reduce symptoms of arthritis, thereby increasing the ability to engage in physical activity.

Side Effects of Bariatric Surgery

Bariatric surgery also comes with both short-term and long-term risks. These include:

  • Infection
  • Acid reflux
  • Bowel obstruction
  • Dumping syndrome
  • Low blood sugar
  • Malnutrition
  • Diarrhea
  • Hernias

The Longitudinal Assessment of Bariatric Surgery (LABS) program of the National Institutes of Health (NIH) recruits bariatric surgery patients in order to track both short-term and long-term outcomes of surgery.

LABS has found that approximately 4% of individuals have at least one major adverse outcome within a month of surgery. The program has also shown no difference in adverse outcomes with different bariatric procedures.

Bariatric Surgery and Body Composition Changes

Bariatric surgery causes weight loss in most individuals, and the greatest percentage of that weight loss is a reduction in fat mass. However, it’s been demonstrated that lean body mass is reduced by approximately 20% as well.

This is an unfortunate finding, as lean muscle lays the foundation for successful weight loss and maintenance as well as optimal health.

However, the good news is that the addition of an amino acid supplement to the diet following bariatric surgery can minimize the loss of lean body mass.

Essential Amino Acid (EAA) Supplements and Weight Loss Following Bariatric Surgery

Weight loss following bariatric surgery is fundamentally governed by the same principles that govern any other weight-loss program—that is, weight is lost due to a negative energy balance.

In other words, the amount of energy you consume throughout the day must be less than the amount of energy you expend. And since calories are the unit of energy we’re talking about here, a negative energy balance simply refers to a caloric expenditure that’s greater than caloric intake.

However, losing weight isn’t as simple as dropping pounds. If it were, it wouldn’t matter whether those pounds were in fat or muscle.

But you want to lose fat and preserve muscle, so weight loss must be focused on losing just the fat. After all, that’s the definition of successful weight loss.

Unfortunately, when you reduce the number of calories you eat, you potentially negatively affect muscle mass in two ways.

Protein Intake

If you don’t change the composition of your diet, your protein intake is going to be cut in half along with your caloric intake. To avoid this, you need to keep your protein intake high so you can preserve lean muscle mass during weight loss.

But to do this, you have to double the percentage of calories you’re taking in as protein just to maintain the same amount of protein you normally eat.

For example, if you consume 25% of your calories as protein, to keep protein levels constant during weight loss, 50% of the calories you eat need to be protein.

And given that most forms of protein provide at least half their calories as carbohydrates and/or fats, that means your entire diet may have to be composed of foods from the protein food group.

Muscle Protein Synthesis

In addition to the negative effects on protein intake, a negative energy balance also makes it much harder to maintain the same rate of muscle protein synthesis when calories are cut.

In the human body, protein is constantly being built up and broken down. And we’ve known for more than a hundred years that the amount of protein needed to maintain this balance between protein synthesis and protein breakdown is influenced by energy intake (in the form of nutrition), which fuels the energy cost of protein synthesis.

However, when you reduce the number of calories you eat, muscle protein is inevitably lost. And this is the fundamental challenge of maintaining muscle mass when you’re losing weight.

How does all this play out in light of the negative energy balance created by bariatric surgery?

Muscle can only be preserved following bariatric surgery if enough essential amino acids (EAAs) are available to stimulate muscle protein synthesis to a degree sufficient to maintain muscle mass. And the most effective and practical way to accomplish this goal is by increasing dietary EAA intake.

Bariatric surgery is for severely obese individuals who have not been able to lose weight by calorie restriction.

The loss of lean body mass—and muscle mass, in particular—is dramatic following bariatric surgery.

This undesirable effect reflects, in part, an impaired ability to digest intact protein (the “whole” form of protein we ingest via food sources, made up of strings of individual amino acids connected to one another, as opposed to the separated amino acids found in free-form amino acid supplements) effectively, especially in the first few weeks after surgery.

In addition, patients who go through any surgical procedure may develop anabolic resistance. When this happens, intact protein loses its normal effectiveness in stimulating muscle protein synthesis.

Unlike intact proteins, such as meat and eggs, free EAAs are extensively digested and absorbed even after bariatric surgery, so their effect on muscle protein turnover is fully retained.

The fact that free-form EAAs can be formulated to overcome anabolic resistance is another potential advantage of relying on EAA-based nutrition following bariatric surgery.

How Many EAAs Are Needed to Maintain Muscle Mass After Bariatric Surgery?

You need to consume at least 1.2 grams of protein per kilogram of body weight each day to maintain muscle mass during weight loss. So, if you weigh 350 pounds, you need to eat 190 grams of protein, or about 400 grams of protein food sources such as meat, fish, and dairy products.

That’s about 2,000 kilocalories just from protein food sources alone!

Add to this the fact that the normal total caloric intake during weight loss following bariatric surgery is about 1,200 kilocalories per day, and it’s clear the numbers don’t add up.

You just can’t get enough protein from food sources to maintain lean mass.

This is particularly relevant when we’re talking about weight-loss surgery, as the amount—and sometimes type—of food bariatric surgery patients are able to eat after the procedure is limited.

Thankfully, this disadvantage can be remedied by supplementing with a free-form EAA formula. Not only have EAAs been proven to help you lose the fat, but they can also ensure you retain that all-important muscle.

Let me explain how this works.

Based on our earlier example—and given the normal proportion of EAAs in high-quality dietary proteins—a protein intake of 190 grams per day would translate to about 80 grams of EAAs.

However, in the early stages after surgery, it may not be feasible to eat more than 50 grams of protein per day, or about 20 grams of EAAs.

In this scenario, your diet would be 60 grams short of enough EAAs to maintain lean body mass, so to make up the difference, you’d need to consume 60 grams of EAAs in the form of a dietary supplement.

And this is as simple as taking a 15-gram dose of EAAs 5 times a day. In fact, a recently published study showed that 5 × 15 grams of EAAs was sufficient to maintain lean body mass during weight loss.

As your ability to obtain protein from food sources increases with time, the amount of supplemental EAAs required to maintain muscle mass will decline, but an intake of at least 30 grams of EAAs will ensure continued maintenance of muscle mass.

If you think you or a loved one may be a candidate for weight-loss surgery and would like more information on the different procedures available and what to expect before, during, and after surgery, I encourage you to visit the ASMBS website.

And if you’re already preparing to undergo bariatric surgery, I recommend exploring essential amino acid supplementation to support your nutritional intake during recovery and beyond.

Evidence Shows Using Amino Acids for Surgery Recovery Leads to Improved Outcomes

Injury and surgery place a similar type of stress on the body, and essential amino acid therapy can help mitigate this stress and accelerate muscle recovery. An essential amino acid supplement with abundant leucine can slow the net loss of muscle protein.

Surgery can be a life-saving necessity, but it places significant strain on the human body. Developing a proactive plan for navigating the post-surgery healing process can help surgical patients avoid—or at least mitigate the effects of—pitfalls such as protein-energy malnutrition, the loss of lean body mass, and systemic inflammation. High-quality scientific research indicates that essential amino acids can offset the physical stress caused by surgery and accelerate the recovery process. To understand the benefits of amino acids for surgery recovery, you must first have an understanding of the role amino acids play in the body.

Dietary supplements of essential amino acids are the most important aspect of nutritional therapy for recovery from injury or surgery.

It’s no secret that amino acids make vital contributions to your overall health and well-being, particularly when it comes to the growth and repair of muscle tissue.

There are two general types of amino acids: essential amino acids and nonessential amino acids. Both are necessary, but because your body can produce nonessential amino acids, you do not need to monitor your intake in the same way you must do for essential amino acids that must be obtained either from the food you eat or from supplements.

Researchers have found that a subgroup of essential amino acids called branched-chain amino acids (BCAAs) increase the body’s ability to  synthesize protein, regulate the rate of muscle tissue breakdown, repair muscle tissue, and transport fuel into muscle cells.

The Toll Surgery Takes on the Body

Think of surgery as a controlled injury. If you are hurt in a car crash, for example, you can go from perfectly healthy to seriously injured in a matter of seconds. The same is often true in the case of surgery.

When going in for elective surgery, you typically feel fine as the anesthesia is administered, but when you wake up, you feel roughly as if a truck ran over you. And even if an underlying pathological condition necessitates surgery, the stress of the surgery itself increases the challenge of rehabilitation.

Although the exact nature of the stress on the body may differ, the body’s response to either the controlled injury of surgery or an uncontrolled injury involves the same fundamental elements. The path to recovery can be nearly identical whether you are healing from an injury or from surgery.

Why People Lose Muscle Mass and Function During Recovery

Whether you are severely injured or recuperating from surgery, one thing’s for sure—you are going to lose muscle mass and function. It’s inevitable. Recovery requires some degree of inactivity, and inactivity means the muscles aren’t maximizing their movement and performance capabilities. This makes a decline in muscle mass and function inescapable. What you can control, however, is the degree of decline. It does not have to be substantial (more on that in a moment).

The detrimental effects of inactivity on muscle mass and function are well established. If you’ve ever had a broken limb put in a cast, you’ve seen the effects firsthand. When it’s time to remove the cast, you’re greeted with the startling withered look of a limb unused. Even if you have been working out the rest of your body, the limb that has remained inactive will show visible signs of decline. An event such as heart surgery that physically limits activity has the same effect as casting a broken limb but on the whole-body level.

The muscle loss triggered by inactivity is amplified by your body’s overall physiological response to injury, which we call the catabolic state. A catabolic state occurs in response to severe injury or illness and is characterized by whole-body protein loss, mainly due to increased breakdown of muscle proteins. The catabolic state can last anywhere from a week to several months.

Anyone who is interested in muscle building for functional or aesthetic reasons knows that failure to consume an adequate supply of nutrients—in particular, protein—slows the body’s rate of muscle protein synthesis, resulting in the loss of a certain amount of muscle. When your body enters the catabolic state, the loss of muscle mass and strength occurs at a much faster rate than it occurs in the absence of key nutrients.

The Physiological Processes Behind Muscle Loss

The simplest way to encapsulate the processes that result in muscle loss is to state that when the rate of muscle protein breakdown exceeds the rate of muscle protein synthesis, we lose muscle mass. Our bodies just can’t make enough new muscle protein to offset the rapid rate of muscle breakdown.

When our bodies enter a catabolic state, the rate of muscle protein breakdown shoots way up. It is not unusual for the rate of protein breakdown to increase by more than threefold!

A large increase in the rate of protein breakdown releases a flood of amino acids into the muscle cells. This increased availability of amino acids stimulates the rate of muscle protein synthesis. Unfortunately, the increased synthesis is not enough to balance the increase in breakdown. The net result is a large increase in the loss of muscle protein.

How Hormones and Inflammation Drive the Catabolic State

The catabolic state following surgery, injury, or illness stems from a variety of underlying factors.

First, a flood of stress hormones, most prominently epinephrine, norepinephrine, and cortisol, activate the sympathetic nervous system. You have likely heard this referred to as the fight-or-flight response.

Next, inflammation kicks in. There are two types of inflammation, and their impact on the body is quite distinct. Local, acute inflammation arises at the site of injury or surgery. This type of inflammation can be quite beneficial in the early phase of wound healing. When local inflammation lingers too long, however, it can begin to inhibit tissue repair.

Systemic inflammation, also called long-term, chronic inflammation, has no identifiable benefits. In fact, this type of inflammation can escalate the catabolic state in the whole body, increasing the severity of associated muscle loss.

To better understand the impact systemic inflammation can have on the body, let’s examine that process in the context of a severe burn injury to the leg. A local response at the site of tissue injury would result in a decline in muscle protein synthesis and a loss of muscle mass and strength to the injured leg. A systemic response, however, disrupts muscle protein metabolism in the unburned leg to nearly the same extent as it does in the leg that sustained the severe burn injury.

Furthermore, the consequences of a catabolic state extend beyond muscle loss. Your appetite decreases, making it more difficult to consume the nutrients required to fuel muscle protein synthesis. Metabolic changes transpire, too, such as reduced sensitivity to the action of the hormone insulin. Insulin resistance may persist for months after other symptoms of the catabolic state have resolved.

Using Amino Acid Therapy to Help Your Body Heal

Loss of muscle mass and strength after injury or surgery delays recovery and an individual’s return to normal activity. In severe cases, or in elderly individuals with little reserve, muscle loss can be a direct contributor to mortality.

In all cases of injury and surgery, the speed and extent of recovery to normal functional capacity is determined in large part by how much muscle has been lost. Injury or surgery causes muscle loss at a rate so fast that consequences can be evident in a matter of days. If you can decrease the amount of muscle you lose, you can accelerate the time it takes you to recover. A balanced essential amino acid supplement can help tremendously with both those goals.

How Essential Amino Acids Decrease Muscle Loss

In order to decrease muscle mass losses during the recovery period, you must counteract the changes to your body’s protein metabolism processes.

After an injury (including the controlled injury of surgery), an alteration in muscle protein metabolism transpires, limiting the normal stimulatory effect of dietary protein on muscle protein synthesis. The lack of responsiveness of muscle protein synthesis to the normal stimulatory effect of dietary protein is called severe anabolic resistance.

The Crucial Role Played by mTOR

Anabolic resistance in the catabolic state occurs because of a molecular factor called mTOR inside the muscle cell. Under normal conditions, mTOR activates muscle protein synthesis, however, anabolic resistance in the catabolic state decreases mTOR activity. In order for muscle protein synthesis to return to optimal levels, mTOR activity must be escalated. Once this occurs, other intracellular molecules involved in initiating protein synthesis respond by escalating their activity levels as well.

So, how do we get mTOR up and running? By supplementing with a complete blend of free essential amino acids formulated with a relatively high proportion of leucine.

Perhaps you’re wondering: why not get leucine from the diet? One of the biggest therapeutic challenges presented by the catabolic state that arises after surgical procedures, injuries, or severe illnesses is reduced appetite. Loss of appetite makes it difficult to take in the dietary protein needed to offset increased muscle protein breakdown and help prevent muscle decline. For many, taking a well-formulated amino acid supplement is a desirable alternative to attempting to eat a sufficient amount of leucine-rich dietary protein.

Then there’s the fact that free leucine activates mTOR more efficiently than leucine contained in intact protein. This is because free leucine does not require digestion and is therefore absorbed more rapidly. Free leucine reaches a higher peak concentration in blood more rapidly than when leucine is consumed as part of an intact dietary protein that must be digested before the constituent amino acids can be absorbed. During the catabolic state, therefore, consuming a mixture of free essential amino acids with abundant leucine slows the net loss of muscle protein more effectively than either intact protein in a meal or meal replacement beverages do.

Once mTOR is activated by leucine, an increased availability of a full balance of all the essential amino acids is necessary to stimulate protein synthesis. Single amino acid therapy with leucine, or a combination of the three BCAAs, just won’t do it. Thus, although leucine is the key to overcoming anabolic resistance, consumption of leucine alone is not sufficient to stimulate muscle protein synthesis.

Dietary supplements of essential amino acids are the most important aspect of nutritional therapy for recovery from injury or surgery.

In addition to providing precursors for making new muscle protein, if enough essential amino acids are consumed, concentrations will rise high enough to inhibit muscle protein breakdown and stimulate protein synthesis.

In this way, essential amino acid nutritional therapy during the recovery period following surgery can help you return to full function by protecting against muscle loss. Taking an essential amino acid supplement can:

  • Activate mTOR
  • Provide amino acid precursors needed to make new muscle
  • Inhibit the breakdown of muscle
  • Improve the net balance between muscle protein synthesis and breakdown

A stimulation of muscle protein synthesis and inhibition of muscle protein breakdown is the metabolic basis for restoring muscle mass and strength.

Key Scientific Evidence on Using Amino Acids for Surgery Recovery

Much of the work done on how best to preserve lean body mass in the wake of major surgery has been focused on protein breakdown and amino acid oxidation. The manipulation of hormones involved in the development of the catabolic state, as well as the stimulation of insulin and insulin-growth factors, has also been a major priority.

Decreasing the release of so-called catabolic hormones as well as insulin resistance in post-surgery patients has been shown to both lower rates of whole body protein breakdown as well as to minimize decreases to muscle protein synthesis. A key element of this, researchers have found, is providing the correct balance of nutrients.

According to findings published in Anesthesiology, delivering an infusion of amino acids to patients can actually reverse the catabolic state. Previous studies demonstrated that amino acid infusions can decrease whole body protein breakdown and increase protein synthesis, resulting in a positive protein balance.

A research team led by scientists from the Department of Anesthesia at the McGill University Health Centre in Montreal enrolled patients scheduled to undergo colon resection, a surgical procedure that involves a hospital stay. On the second postoperative day, all patients received a solution of 10% amino acids. Levels of whole body leucine and glucose were measured, and blood samples were taken to analyze levels of hormones including cortisol, glucagon, and insulin.

The scientists found that the infusion of amino acids resulted in a positive protein balance as well as other beneficial metabolic effects. Their findings showed that the amino acids suppressed protein breakdown by over 25%, and that 12-16% of amino acids made available from proteolysis were redirected toward protein synthesis. “The infusion of amino acids in the current study caused an average increase in protein balance of 36.7 μmol · kg−1· h−1,” the authors wrote. They concluded that even the short-term use of amino acids after surgery can inhibit protein breakdown while stimulating protein synthesis.

A separate study carried out by a team based in Oregon and published in the June 28, 2018 issue of the Journal of Bone and Joint Surgery focused specifically on how amino acids impact post-surgical muscle volume loss.

The double-blind, placebo-controlled, randomized trial enrolled adult patients undergoing total knee arthroplasty (TKA), also known as total knee replacement surgery. The authors’ goal was to determine whether supplementing with amino acids during the perioperative period—which includes time spent in the hospital prior to as well as after surgery—can mitigate muscle atrophy.

Study participants ingested either 20 grams of essential amino acids (EAAs) or a placebo twice daily for 7 days prior to their procedures and for 6 weeks following them. Magnetic resonance imaging was used to measure quadricep and hamstring muscle volume at the time of enrollment and at the study’s conclusion. Data on functional mobility and strength came from patient-reported outcomes.

Compared with the placebo group, participants who took EAAs experienced significantly smaller losses of mean quadriceps muscle volume in the leg on which the operation was performed as well as their other leg. A greater muscle-volume-sparing effect was seen for the hamstrings of individuals who took EAAs than for those in the control group as well. The authors concluded that EAA supplementation is a safe way to reduce the loss of muscle volume for patients undergoing TKA.

Strategies for Preserving Muscle Strength and Function During Recovery

Even if you’re able to use amino acids to alleviate or avoid the the short-term catabolic state that follows physical trauma, your body will enter a depleted state marked by significant muscle loss. This will be evident in overall body weight loss—how many times have you heard that the only good thing about someone’s injury or surgery was that they lost weight?

As recovery continues, the lost weight will be gradually regained. However, without diligent adherence to an exercise and nutrition program, the lost muscle weight will be regained as fat. To return to your daily activities in the best possible health, it is crucial to replace the lost weight with new muscle, not fat. In this article, I go deeper into how amino acids can fuel good weight after a serious illness, injury, or surgery.

For our purposes here, I’ll provide an overview of best practices related to exercise and nutritional strategies to rebuild muscle during recovery.

Be Sure to Prioritize Exercise

At the outset of recovery, your capacity for exercise will be limited. Even so, it is essential to engage in both aerobic and resistance exercise as soon as possible.

Depending on the specifics of your situation, it may be advisable—or even mandatory—for you to engage in a structured physical therapy program. Whether or not that is the case, at some point in your functional recovery process, it will be vital to devise your own approach to reintroducing physical activity.

Aerobic exercise can take any form—walking, elliptical, cycling, swimming, and so on—as long as the option you choose elevates your heart rate to 120 beats per minute or above. As you regain your fitness, your speed and the amount of distance you cover will increase.

Some moderate stretching may also be needed to regain range of motion. As strength returns, work up to the recommended guideline of 150 minutes a week of aerobic exercise. However, because most of your cardio output recovery will be walking as opposed to more strenuous aerobic activity, it’s advisable to increase to 5 hours per week of aerobic exercise in addition to resistance sessions.

Resistance exercise is the most important type of exercise for rebuilding muscle. Machines are optimal for resistance workouts, particularly at the outset. The loss of muscle function in the catabolic state impairs coordination, and the possibility of injury is greater with free weights. Machines provide specificity in terms of the muscles involved in any exercise, and this may be of particular importance when addressing specific areas affected by injury or surgery.

The weight lifted should be progressively increased as strength returns. Most individuals will find that they regain lost strength in a shorter period of time than that required to originally gain that strength. The amount of resistance used should be adjusted accordingly. A general guideline is to increase the resistance by 10% per week, but progress may be more rapid in the first few weeks of recovery.

Make a Post-Surgery Nutrition Plan

Nutrition plays a crucial role in recovery. Eating a balanced diet featuring ample high-quality protein is essential. However, that alone will not ensure you regain more muscle than fat.

The single most important aspect of nutritional therapy during the recovery period will be essential amino acid supplementation.

Essential amino acids are the active components of dietary proteins. Balanced essential amino acid supplements stimulate muscle protein synthesis to a greater extent than any naturally occurring protein food source.

Essential amino acid supplements work synergistically with exercise to provide a greater stimulus than either produces on its own. To maximize the beneficial effects of each element, you should take essential amino acids 30 minutes before an exercise session as well as immediately following the session.

When consuming essential amino acids without accompanying physical activity, the greatest effect will be when taken between meals. That said, there is no wrong time to take an essential amino acid supplement. If you miss the optimal dosing window, simply take your EAA supplement at your earliest opportunity.

For more information on a balanced amino acid supplement created for recovery after injury or surgery, check out our Amino Company blends.

BCAAs and EAAs—Which Amino Acid Supplement Is Right for You?

If you search for “essential amino acids” on Google you will see many sites advertising branched-chain amino acids (BCAAs), and others advertising essential amino acids (EAAs). You may be left wondering: Are BCAAs and EAAs the same thing? If not, what’s the difference? Which is right for you?

Discussions of amino acids are rife with acronyms, but the two most common just might be BCAAs and EAAs.

If you search for “essential amino acids” on Google, the top results will be filled with sites proclaiming the health benefits of branched-chain amino acids, or BCAAs. And you’ll also discover just as many sites where prominent experts in sports nutrition claim that BCAAs are worthless and the true heroes of the amino acid world are essential amino acids, or EAAs.

Understandably, you may be left wondering about the differences between BCAA supplements and EAA supplements. With all the strident advertising claims, it can be quite challenging to determine the basic facts about both types of amino acids, let alone which supplement option will be right for you.

Essential Amino Acids (EAAs) Explained

Essential amino acids (EAAs) belong to a broader class of amino acids involved in protein synthesis and fittingly referred to as proteinogenic amino acids. One of the primary ways your body uses these amino acids, which have been nicknamed the building blocks of protein, is for muscle growth.

The class of proteinogenic amino acids can be split into two primary subcategories: essential amino acids (EAAs) and nonessential amino acids. Nine amino acids have been classified as essential because the human body cannot synthesize these on its own, meaning you must obtain them from dietary protein sources or nutritional supplements. The nine essential amino acids are:

Leucine Lysine Tryptophan
Isoleucine Threonine Histidine
Valine Phenylalanine Methionine

While the nonessential amino acids undeniably contribute to your overall health and well-being in crucial ways, the human body can produce them from a combination of essential amino acids, carbohydrates, and fats, rendering them comparatively nonessential.

EAAs play a variety of important roles in the body, including acting as precursors for the production of brain neurotransmitters and supporting immune function. However, as I mentioned above, the main role of EAAs is as constituents of proteins, including muscle protein.

Since all proteins in the body are continually broken down and re-synthesized, an adequate supply of all the EAAs is required or body protein will be lost. Most of the EAAs in body protein that is released as a result of protein breakdown are available for reincorporation into protein. However, approximately 15% of the EAAs released from protein breakdown are oxidized, which means they are irreversibly lost. The EAAs that are oxidized must be replaced through your diet since they cannot be produced in the body.

Branched-Chain Amino Acids (BCAAs) Explained

Branched-chain amino acids (BCAAs) exist as a subcategory of essential amino acids. The three branched-chain amino acids—leucine, isoleucine, and valine—got their name because of their distinctive, branch-like chemical structures.

When it comes to BCAA benefits, leucine dominates. Researchers have proposed that leucine holds a variety of regulatory roles in the body. Initial interest in the unique qualities of leucine concerned its primary role in stimulating muscle protein synthesis, or the building of new muscle tissue. We can trace this interest back to a 1975 study published in the Journal of Clinical Investigation that demonstrated leucine’s capacity to stimulate protein synthesis in isolated rat muscle.

Then in 1988, two scientists named Garlick and Grant conducted studies with rats to explore the possibility that the same effect could be elicited in a living creature. Their findings showed that a mixture of BCAAs could increase the muscle protein synthesis response to insulin.

The next major advance came in 2000 when the Journal of Nutrition published a study that investigated the potential mechanism by which leucine acts as a stimulator of muscle protein synthesis. The study authors showed that leucine ingestion stimulated muscle protein synthesis in rats and that the increase in synthesis was accompanied by the activation of several molecular factors (including the mTOR pathway) within the muscle cell that are required for initiation of the process of protein synthesis.

Researchers refer to these factors collectively as the initiation factors, and the entire molecular processes involved in the initiation of protein synthesis as anabolic signaling. The takeaway, at this point, was that leucine can activate anabolic signaling.

But an interesting phenomenon occurred when humans entered the research picture. When scientists began to study the beneficial effects of leucine on human subjects, it became evident that providing leucine alone disrupted the balance of plasma amino acids. Most notably, increased availability of leucine not only caused increased oxidation of leucine but the accelerated oxidation of the other two branched-chain amino acids as well.

Because providing leucine alone created isoleucine and valine deficiencies, supplement companies typically formulate their proprietary blends of BCAAS to contain all three amino acids even though no special qualities of either valine or isoleucine have been identified.

Based on both historic and recent studies, we now have a good grasp of what happens when humans take branched-chain amino acid supplements. Scientists have shown that taking between 2 and 4 grams of leucine as part of a complete BCAA dietary supplement may positively influence a variety of physiological endpoints, including increased muscle mass, improved recovery from exercise, and enhanced mood and cognitive performance during prolonged exercise.

There is no doubt that leucine can be considered a nutraceutical, a designation that honors its regulatory effects beyond its role as one of the building blocks of body proteins. It’s clear that increasing the amount of leucine you consume each day can help you to build muscle and optimize your exercise performance, among other benefits.

What You Should Know About Muscle Protein Synthesis

As I briefly noted in the section on EAAs, one of the major contributions amino acids make in the human body is the stimulation of muscle protein synthesis.

In fact, researchers have discovered that the availability of the essential amino acids determines the rate of muscle protein synthesis. That means that the smaller the number of available EAAs, the slower the rate of muscle protein synthesis, and the larger the number, the faster the rate.

Every time you eat a food that contains all nine essential amino acids, or take an EAA supplement, you stimulate muscle protein synthesis. The degree of stimulation of muscle protein synthesis by EAAs depends on the dose. The more EAAs ingested, (with a maximum threshold of 15 grams), the greater potential for building muscle. Conversely, if EAAs in the blood drop below a certain level, then your muscle-building potential becomes compromised. You can learn more about this process in my book, A Guide to Amino Acid and Protein Nutrition: Essential Amino Acids for Everyone.

The most important takeaway about the relationship between amino acids and muscle protein synthesis is that all the essential amino acids are required to make new protein. This can best be understood by thinking about how proteins are made.

Each protein in the body is a long string of amino acids linked together in a specific order. Protein is produced by hooking together amino acids one by one in the order dictated by messenger RNA in the cell. If a point is reached where the next amino acid due to be incorporated into the chain is not there, production of the protein will stop.

Where Do the Amino Acids for Protein Synthesis Come From?

The proteins that make up your muscles constantly break themselves down and then build themselves back up. The muscle breakdown process releases amino acids, which your body then recycles and uses for the synthesis of new proteins. In the basal state, the resting metabolic state of the body in the morning after 12 hours of fasting, amino acids released by muscle breakdown serve as the main source of amino acids for protein synthesis. Regardless of your metabolic state, approximately 85% of the amino acids released by muscle protein breakdown are re-used in the protein synthesis process.

There are two ways to increase the rate of protein synthesis: either you find a way to more efficiently reutilize the amino acids from protein breakdown, or you make more essential amino acids available by increasing your consumption of EAAs.

The bottom line? The simplest and most effective way to ensure that all the EAAs will be available for muscle protein synthesis in the optimal ratios is to increase your intake of essential amino acids.

BCAA or EAA Supplements—Which Are Better for Muscle Growth and Muscle Repair?

Now it’s time to get down to brass tacks and settle the question of EAAs vs. BCAAs. To do so, let’s review what we’ve discussed so far. All three branched-chain amino acids—leucine, valine, and isoleucine—are also essential amino acids. They’re also all components of muscle protein. Plus, leucine can increase the efficiency of protein synthesis by activating the initiation factors. So, does that mean increasing your intake of leucine with a BCAA supplement is the best way to achieve desirable health outcomes like the stimulation of the synthesis of new muscle protein?

Not quite. Remember, if only BCAAs are consumed, they are limited in their ability to stimulate muscle protein synthesis. That’s because all the EAAs are required for a complete protein to be produced, and in the basal state, the only source of EAAs is from protein breakdown. Since most of those EAAs are already reincorporated, the maximal increase in protein synthesis is limited by the availability of the other EAAs. For this reason, research has shown that taking BCAAs alone has either no effect or a minor effect on the rate of muscle protein synthesis in human subjects.

There is no question that BCAAs are important for many functions in the body, including protein synthesis. However, the full benefit of BCAAs cannot be achieved if they are taken by themselves, because you cannot make a complete protein out of just three amino acids. The maximal effectiveness of the BCAAs is only achieved when they are taken along with the other six EAAs. Only a mixture of all the EAAs can provide a sustained stimulation of muscle protein synthesis. The nonessential amino acids in protein can be made in the body and are therefore not required in a dietary supplement.

A non-scientific analogy might be helpful in understanding the difference between BCAAs and EAAs. Think of EAAs like different players on a football team. In this analogy, leucine is the quarterback that calls the signals and is the most important player on the team—what team wins without a good quarterback? However, a team of just quarterbacks wouldn’t be very successful, and neither is an amino acid supplement made up entirely of grams of leucine.

All the positions on the team have an essential role to play, and without enough players for each position, the team will fail. Similarly, all the EAAs are required for the effects of leucine to translate to increased production of muscle protein. Consumption of a dietary supplement containing a balanced mixture of all the EAAs that includes a generous proportion of leucine is necessary for maximal results.