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.

When Is the Best Time to Take Protein?

The best time to take protein supplements depends on your activity level, your personal goals, and the types of workouts you engage in. This article will provide you with specific, scientifically backed recommendations, and the reasoning behind that advice.

When taking protein supplements, people often wonder when exactly is the best time of day to consume them. Pre-workout? Post-workout? Is it okay to drink a protein shake before bed? Protein supplements can help people lose weight, build muscle, and recover from tissue damage due to injury or surgery. Because they’re so effective, most people want to be sure they’re utilizing protein the right way. So when is the best time to take protein? Short answer is: that depends on your health goals and the kinds of workouts you’re doing. For the longer answer and more detail, read on.

The Different Types of Protein Supplements

Protein is a source of energy for the body, essential for muscle growth, repairing damaged tissue, and preventing certain infections and diseases. Normal dietary protein comes from foods like meats, eggs, fish, dairy, grains, legumes, and seeds. Though animal products contain the most amount of protein, vegetables are sources of protein too, a fact well-known by those living a vegetarian or vegan lifestyle. Of the most popular protein powders on the market in fact, a significant portion are plant-based.

Plant-based proteins include:

  • Soy protein containing all nine essential amino acids.
  • Rice protein, which is lower in the essential amino acid lysine.
  • Pea protein, which has lower levels of the essential amino acid methionine and nonessential amino acid cysteine.
  • Hemp protein, which is low in lysine but high in fiber, and omega-3 and omega-6 fatty acids, both of which are essential, meaning your body can’t make them on its own, and needs to gain them from the foods you eat.

Dairy-based proteins include:

  • Whey protein, which is absorbed relatively quickly and contains all nine essential amino acids.
  • Casein protein from milk curds, also containing the essential amino acids, and with a slower digestion rate than whey (which is why people often take casein before they sleep, so it will digest throughout the night… more on that timing below).

Animal-based proteins include:

  • Egg protein powder made from pure egg white protein.
  • Creatine, which is not found in plants but can be synthetically created. Though it is an animal protein, depending on its origin source, it may nevertheless be possible for vegans to use creatine as a supplement.

These are among the most commonly known protein powders available to buy, but we here at the Amino Co. have also developed an essential amino acid (EAA) blend that isn’t lacking or low on any of the amino acids required for protein synthesis and new muscle growth. It also blends free-form amino acids with whey protein and creatine, a nonessential protein that nevertheless has great value as a supplement. These forms of protein are used to help those who want to build muscle rapidly, and can even benefit those with muscle, neurological, or neuromuscular diseases.

The Varied Uses of Protein Supplementation

From muscle building to weight loss, here’s a quick look at all that supplemental protein can do to benefit your body.

Exercise Performance and Recovery

Added protein has been shown to increase endurance during training and workouts, as well as reduce soreness and speed up post-workout recovery. The timing of your protein intake matters here, whether you’re eating high-protein foods or taking supplements. Read on to learn about workout-specific timing recommendations.

Muscle Building

Muscles can only be built when you have the proper amount of amino acids for protein synthesis, and when you’re consuming more protein than your body breaks down during workouts. Taking a protein supplement, especially one that contains all the necessary EAAs for muscle growth, can make a huge difference. Finding the right anabolic window, the period of time when the protein you take in will go directly to your muscles, is something the International Society of Sports Nutrition has done extensive research on, and we, too, will provide specific scientific reasoning below.

Muscle Loss Prevention

Muscle mass is lost not only during intensive workouts, but also naturally as we age. Each decade you live after the age of 30 brings with it a higher risk of losing muscle (anywhere between 3-8% per decade). Proper protein intake is not only valuable to athletes, bodybuilders, and anyone who works out regularly, but it’s also important for each and every one of us as we age. Most Americans reserve their protein more for dinner than breakfast (3 times the amount on average is the difference between the two meals), and could use a supplemental boost of protein first thing in the morning to shore up their protein stores and help prevent the loss of muscle mass due to aging.

Fat Loss Facilitation

Protein is filling enough to help curb hunger pangs and chemically contributes to appetite suppression by reducing the “hunger hormone” ghrelin. A high-protein diet raises your metabolism and increases levels of appetite-reducing hormones like peptide YY (PYY) and glucagon-like peptide-1 (GLP-1). More satiety means fewer calories consumed throughout the day, which quickly leads to safe, maintainable weight loss and the reduction of dangerous body fat.

The Enduring Power of Protein

Popular because they’re convenient and effective, protein powders and supplements are here to stay and can offer you a wide variety of options, from self-mix formulas and powders to ready-to-drink protein shakes. If you’ve got your preferred protein supplement ready to go, then it’s time to wonder: when should you drink protein?

The Best Time to Take Protein Depending on Your Workout

Depending on your goals and activities, there are recommended times to take protein for the greatest effectiveness for your energy levels and muscle-building needs. Here are specific recommendations based on different types of workout activity.

The best time to take protein supplements.

Aerobic/Cardiovascular Exercise

Best time to take protein: Pre-workout and post-workout

The amino acid leucine is one of the three branched-chain amino acids (BCAAs), and it promotes muscle recovery after workouts. Not only that, it activates protein synthesis, prompting new muscle to be built. One might think that due to leucine’s ability to boost endurance and stamina, one should take a BCAA supplement before a workout, but the science contradicts that idea. Not only are BCAAs only three of the nine essential amino acids needed to construct new muscle, leucine and the other BCAAs (isoleucine and valine) experience oxidative degradation during aerobic activity.

BCAAs are Insufficient Pre-Workout

Adding these limited amino acids before your workout, especially in the unbalanced form of BCAAs instead of a complete EAA formula, means that a greater percentage will be oxidized and used for energy instead of muscle building. Your body does not want to be out of balance, so a sudden overabundance of a few amino acids will cause the body to clean up and reduce them in order to maintain equilibrium.

Rather than risk burning off the protein you put in because your body is only looking for energy sources, it’s better to take a full measure of EAAs within the hour after your aerobic workout, when your body is looking for supplies to rebuild. Leucine will be there to prompt muscle protein synthesis, and the rest of the essential amino acids will all be included in the ideal ratio for generating new muscle growth.

EAAs are Effective Pre- and Post-Workout

That being said, taking a complete amino acid protein supplement before an aerobic cardiovascular workout (like a high-intensity interval training or HIIT class), not only provides the necessary ingredients for muscle building, but also helps fight fatigue in a way that only taking BCAAs can’t, by fueling your body with the amino acids that help produce dopamine and serotonin in the brain.

Whether you’re walking, cycling, running stairs, or jumping rope, start by taking your EAA supplement 30 minutes before your workout session. The biggest benefit comes when you take your EAA supplement within an hour after your workout, when your blood flow is strong and active. Not only will the amino acids rush in to replace damaged muscle fibers with new muscle, EAAs can also help calm unnecessary inflammation. That will help quicken your recovery, allowing you to feel only the good side effects of working out, like increased energy and light euphoria, instead of soreness and fatigue.

Resistance Exercise

Best time to take protein: Pre-workout, during, and post-workout

Research has shown that EAAs given 30 minutes before a resistance exercise workout prompt muscle protein synthesis much more effectively than consuming EAAs afterwards does. Taking a protein supplement before this type of workout helps prevent the breakdown of muscle protein during the activity, and also increases blood flow to the muscles, thus getting the amino acids quickly into the muscle where they’re needed.

Consuming EAAs after a resistance workout is not harmful by any means, as that method, too, will prompt the stimulation of muscle protein synthesis, but it’s not ideal to leave the consumption of EAAs until after your resistance training is complete. Our recommendation is to first and foremost take a complete protein supplement before a resistance workout, and if possible take them throughout and/or after as well to get the most benefit.

Bodybuilding

Best time to take protein: Pre- and post-workout, and also before bed.

Immediately before and after a weight-lifting workout, we recommend that you take 15 grams of EAAs each. An EAA supplement has been shown to have a faster effect on muscle protein synthesis than either whey or casein protein alone. However, our Amino Co. blend of free-form EAAs with whey and creatine support ensures that you get a fast dose of EAAs and that the EAAs from whey will digest more slowly as you work out, offering a steady supply to help prevent muscle breakdown. Creatine helps prevent catabolism by supplying faster energy than your body can naturally generate from muscle cell mitochondria. This means more energy for more reps, which ultimately means more work put in and more muscle gained.

An hour after your post-workout dose of EAAs, we recommend another 15-gram dose. On off days, continue taking these same doses, measured between meals instead of surrounding your workout. Lastly, it’s also recommended you take another 15-gram dose before bed to keep your muscles fed as you sleep and to help prevent muscle breakdown as much as possible. You work hard to gain your muscles, and we encourage you to protect those gains at every opportunity. Set your alarm to take one more dose around 4 am if you know you won’t have a problem falling back to sleep, that way your muscles never go hungry for fuel.

It should be noted here that bodybuilders aren’t the only ones who benefit from taking extra protein before bed. One study of 16 elderly men showed that those who consumed casein protein (which digests slowly) before bed had increased muscle growth over those who took a placebo, despite being less active individuals. When you’re sleeping, it’s the protein that counts, and not the activity.

Is There Any Downside to Taking Protein Supplements?

The majority of scientific studies into how our bodies process high amounts of protein show that you can safely consume plenty of protein without risk of harmful side effects. Unless your doctor advises against protein supplements or you have a known kidney issue like rhabdomyolysis, there is no need to worry about excessive protein intake; merely take your products as recommended and spread them throughout your day.

Timing Is Everything

At the end of the day, it’s true that people who work out need more protein, but even those with a less active lifestyle benefit from consuming extra protein for strength, for maintaining healthy weight levels, and for preventing the loss of muscle mass we all experience as we age.

Make a protein shake for breakfast, have another to curb your appetite between meals, and make another as a beneficial treat before bed. Know that the more regularly you take in balanced forms of protein like Amino Co.’s complete EAA blend, the more good you can do for your body. Whether you’re working out or not, upping your daily protein intake is safe and smart. Bulk up, slim down, and stay strong with protein!

BCAA vs. Creatine: What You Need to Know

BCAA vs. creatine: a comprehensive look to help you decide which you should choose, or whether you’d rather utilize a product that combines the two supplements for better energy, muscle strength, and protein synthesis.

If you spend enough time in the gym, you will eventually run across this question: BCAA vs. creatine, which supplement do you prefer? Before you can answer that question, you’ll need the information behind both BCAAs and creatine: what are they? What are the upsides and downsides to each? How can they help build muscle? Can they both be taken together? You’ll find the answers to all of those questions here, plus learn about the one ultimate supplement that perfectly marries the two together, so you never have to compromise for imbalance in your muscle-building nutrients.

BCAA vs. creatine: a comprehensive look.

What Is BCAA? What Is Creatine?

We’ll start with the definitions, and then move on to the differences between these two supplement options.

BCAA: Branched-Chain Amino Acids

A BCAA supplement is made up of branched-chain amino acids, specifically the three amino acids leucine, isoleucine, and valine. There are a total of nine essential amino acids, essential because you must eat or otherwise consume them to get them (other amino acids are produced in-house by your body). Leucine, valine, and isoleucine are essential amino acids.

“Branched-chain” refers to the molecular structure of these three specific amino acids. The chemical bonds branch off of the main structure.

Studies have shown that BCAAs help reduce muscle damage and soreness in post-workout recovery.

While it’s possible to get a sufficient amount of the BCAAs from your diet, for those who work out intensively, and/or for those on specific diets aimed to lose weight, it might be difficult to get the right amino acid balance, which is why some will chose a BCAA supplement in the hope that it will round out their nutrients. However, it should be noted here that muscle synthesis cannot take place without all nine essential amino acids, so a complete essential amino acid (EAA) supplement is preferable to a BCAA one—you cannot build muscle with only a third of the necessary ingredients.

To cut calories without having a negative impact on protein intake for muscle mass is important, and BCAAs are often taken to try to ensure there’s no interruption to protein synthesis while dieting. Even if weight loss isn’t your goal, the BCAAs gained from taking a complete EAA supplement might still help in that department by contributing to appetite control.

BCAAs have similar benefits to a whey protein shake, but with fewer calories. Moreover, the amino acid leucine is one of the two specifically ketogenic amino acids, another way that BCAA supplements contribute to fat loss (the ketogenic diet is all about burning off fat, and doing it both quickly and safely).

BCAA supplements are perhaps best suited for CrossFitters, bodybuilders, or rowers, but again, they are only a third of the essential amino acids, all of which are necessary for muscle building.

BCAA Quick Facts

  • BCAAs provide three of the nine essential amino acid building blocks of muscle tissue.
  • BCAAs help protect lean muscle and guard against muscle wasting.
  • BCAA supplements are a source of longer-term energy, and can help reduce exercise fatigue.
  • BCAAs help promote fat loss via appetite suppression and increased metabolism for burning calories.
  • BCAA supplements provide higher strength gains than whey protein does.
  • There are no harmful side effects reported from BCAA supplementation.

Creatine: The Energy Protein

Creatine is creatine monohydrate, the protein found in animal sources of meat like fish, poultry, pork, and red meat. Creatine contains two different amino acids, arginine and methionine, of which methionine is essential.

Unlike the weight-loss potential in BCAA supplements, taking creatine can lead to initial weight gain, as it causes some water retention in the muscles. Likewise, if you’re not drinking enough water while taking creatine, cramping can occur, meaning it’s more important than ever to stay hydrated while working out.

Researchers have stated that creatine might help lessen the effects of osteoarthritis, slowing the loss of bone mass as you age. Another unique benefit of creatine is its ability to deliver the rapid energy that is needed during fast muscle contractions (when sprinting, for example). That means creatine gives you longer endurance, which means more reps, which means more muscle growth. This is why creatine is best suggested for powerlifters or sprinters, and why it’s a part of our unique EAA blend (see below for further details).

Creatine Quick Facts

  • Creatine breaks down into phosphocreatine (CP), which provides rapid energy for muscle contractions.
  • Creatine causes the release of the anabolic hormone IGF-1, used in promoting muscle growth.
  • Creatine is a quick source of muscle energy, allowing for more reps.
  • Creatine use aids long-term bone strength for weight trainers.
  • Creatine increases strength during resistance training by up to 20%.
  • Some water retention and cramping is reported with the use of creatine, but the effects are short term.

BCAA vs. Creatine: Which Should You Use?

If you’re here to make a choice, now’s the time to review your fitness goals and how each of these products might influence them. Research suggests that BCAAs help to increase muscle mass for those doing resistance training. If your diet is low on protein intake, say if you’re vegetarian or vegan, BCAA supplements are a great way to promote muscle protein synthesis, but remember that they are also only a partial supply of the amino acids you need for muscle building.

Likewise, a study also showed that muscle strength increased up to 8% for those using a creatine supplement while resistance training. Creatine can provide rapid energy when the usual muscle cell energy supply of adenosine triphosphate (ATP) is slow to regenerate, and it goes a long way towards the kind of strength building and increase to muscular force that might be preferred by powerlifters.

Both supplements aid muscle recovery, both contain at least one essential amino acid, both help drive protein synthesis, both of them are good to take as pre-workout supplements for their benefits, and honestly, unless you have a specific reason to not take one of them, you may be thinking that you want to take both. Well good news for you then, because you can! In fact, we recommend that you do.

BCAA and Creatine Together

You may have noticed that there was no overlap between the amino acids from BCAA supplements and creatine supplements, which means taking both will not overdose you on any one amino acid. Rather than think of them as enemies in some competition for supplement supremacy, BCAAs and creatine can be two valuable players on the same team: your team. Nothing bad will happen to you if you combine them (they’re not baking soda and vinegar in a third grader’s science fair volcano or anything), and since they both aid sports performance, boost muscle building, help with fat loss, and ease muscle recovery, when taken together you may see improved results in all of those categories.

However, if you’re after a full roster of the essential amino acids, there are amino acid supplements that include all three BCAAs, plus the other muscle-building EAAs. Whether you’re looking into supplementation because you’re lifting weights or attempting to lose body fat or both, a protein powder with only partial, unbalanced amounts of amino acids just won’t do the trick.

A Complete EAA Blend

When it comes to muscle-building supplements, our blended EAA formula not only contains eight of the nine essential amino acids, including the BCAAs, but it also supplies them with the energy of creatine and the steady amino acid digestion that comes from whey protein supplements (derived from milk).

This supplement is scientifically proven to increase human muscle growth and can help prevent muscle breakdown in the elderly. It was also designed to contain the exact ratio of amino acids needed to build muscles without overtaxing your body with excessive or unnecessary amounts of any one.

When building muscle, you don’t want to show up with a partial supply of the building blocks of protein. Instead, you want a comprehensive EAA supplement that helps all the work you do weight training at the gym to pay off. Instead of a dose of BCAAs here or a dash of creatine there, we recommend you get the most out of all of the above with our combination of EAAs with creatine and whey protein support. If the question is BCAA vs. creatine, the real answer is the Amino Company’s blends: for balance, for building, for the best of both worlds and more.

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!

Best Amino Acids for Muscle Growth

The best amino acids for muscle growth tip the balance in favor of muscle protein synthesis. And making a complete protein requires adequate availability of each of the amino acids. Read on to find out the formulation of amino acids that is best for building muscle.

Before we get into the best amino acids for muscle growth, let’s first review the makeup of muscle. Muscle tissue is composed of a variety of proteins that are in a constant state of turnover—proteins that are no longer functioning well are being broken down and new ones are being produced. Muscle growth occurs when the rate of synthesis of new muscle protein exceeds the rate of breakdown.

Muscle protein is composed of 20 different amino acids hooked together in a specific order. Nine of the amino acids are essential amino acids (EAAs) and cannot be produced in the body. The other 11 are nonessential (NEAAs) and can be produced in adequate amounts within the body.

Muscle protein synthesis (the building of new muscle protein) involves a series of molecular events that result in the component amino acids being linked together in a specific order. For this reason, amino acids are often called the building blocks of protein. Making a complete protein, therefore, requires adequate availability of each of the amino acids. In that sense, there is no individual best amino acids for muscle growth, because they are all required to produce muscle protein. Rather, there are formulations of amino acids that are “best” for specific circumstances, such as building muscle.

Where Do Amino Acids Come from for Muscle Protein Synthesis?

When protein is broken down during muscle protein turnover, amino acids are released into muscle cells. Most of these amino acids become the precursors for the synthesis of new muscle protein. However, some of the amino acids from protein breakdown are released into the blood and delivered to other tissues and organs, and still other amino acids from protein breakdown are irreversibly oxidized/damaged. Therefore, the rate of reincorporation of amino acids from protein breakdown into newly synthesized muscle protein will always be less than the rate of protein breakdown. Without other sources of amino acids, a reduction of muscle protein and subsequent muscle loss occurs.

There are two ways to get the additional amino acids you need for muscle protein synthesis.

  1. They are produced in the body. (NEAAs can be produced in the body, so only a minimal amount must be consumed in the diet to meet all demands.)
  2. EAAs, on the other hand, cannot be produced in the body and must be consumed in the diet.

Research shows that consuming EAAs stimulates muscle protein synthesis and helps build muscle, but eating more NEAAs doesn’t add any further stimulus. When EAAs are consumed, the additional NEAAs required for the production of complete proteins are produced in the body. Ingesting EAAs, either as dietary protein or as amino acid supplements, shifts the balance between synthesis and breakdown of muscle protein to favor the net production of new muscle protein, which defines muscle gain.

What Are the Best Amino Acids for Muscle Growth?

Muscle protein is composed of a specific amount of each amino acid, hooked together in a specific order. In that sense, all the amino acids are equally important, as a shortage of any of them will stop the process of synthesis.

The EAA in shortest supply is called the limiting EAA. The availability of the limiting EAA will limit the rate of muscle protein synthesis, regardless of the availability of all the other EAAs and NEAAs. Therefore, you could say that the limiting amino acid in any formulation of EAAs is the most important.

This is the major problem with supplements that only have the branched-chain amino acids (BCAAs) leucine, isoleucine, and valine. Since the other essential amino acids are not provided, the rate of muscle protein synthesis is not improved. Because of this, BCAA supplements have been proven to provide a far smaller effect on muscle growth than a complete EAA formulation.

It is possible to gain insight into the amount of each EAA that is needed to avoid that EAA being the limiting EAA by looking at the requirements for the individual EAAs. By definition, NEAAs are not required in the diet, so when we talk about dietary requirements we are talking only about EAA requirements. The dietary requirement for each EAA differs. Here are the daily requirements for EAAs for adults as published by the Food and Agriculture Organization of the World Health Organization (FAO/WHO).

Best Amino Acids for muscle growth

The requirements are based on a number of factors, including the composition of total body protein. From the requirements shown above, it is clear that all EAAs are not “equal.” The requirements for leucine and lysine are the highest, while the requirement for tryptophan is quite low.

It could be argued that the best amino acids for muscle building parallel the individual requirements of the EAAs. Indeed, that is the basis for the official FAO/WHO grading of protein quality, called the Digestible Indispensable Amino Acid Score (DIAAS). Indeed, an EAA supplement that closely parallels this distribution will be an effective stimulant of muscle protein synthesis in any circumstance. The bottom line is that you need all the essential amino acids to have any effect on muscle mass, and any nonessential amino acid need not be included in a dietary supplement.

Leucine for Muscle Growth

There has been considerable research over the past 15 years that indicates that alternative mixtures of EAAs may be more beneficial in particular circumstances. Most of the research has centered on the EAA leucine. In addition to being the most abundant EAA in body protein, under certain circumstances, leucine can function to regulate molecular processes within the muscle cell. In those circumstances, it can be called a “nutraceutical.”

Leucine can activate the molecule called mTOR, which gets muscle protein synthesis started. Various conditions associated with progressive muscle breakdown and loss of muscle strength, such as cancer, heart failure, and aging, can suppress the activity of mTOR and associated molecules. When mTOR activity is limited, it may be preferable to increase the proportion of leucine to as high as 35% to activate mTOR. At the same time, activation of mTOR and associated molecules in the muscle cell is not sufficient to increase muscle protein synthesis. You also need an abundance of all EAAs to produce complete proteins. Therefore it is necessary to limit the proportion of leucine in an effective dietary supplement to below 40% so that sufficient amounts of the other EAAs can be included.

If extra leucine is added to a dietary supplement such as whey protein powder to capitalize on its action as a nutraceutical, then the remainder of the supplement should provide the other EAAs in proportion to their contribution to the composition of muscle protein. It seems logical that this would be dictated entirely by the composition of muscle protein, but it is not quite so straightforward.

The absorbed ratios of the different EAAs will not be directly reflected in the EAAs inside the muscle cells because some amino acids are transported into the cell faster than others. Lysine, in particular, is transported sluggishly into the muscle. When lysine is consumed, less lysine will enter the muscle cell than would be expected from the profile of the consumed EAAs. Consequently, to increase the lysine concentration inside the muscle cell in proportion to the lysine content of muscle protein it is necessary that lysine comprise 20% or more of the total EAAs consumed to achieve the maximal muscle-building effect.

Different Strokes for Different Folks

The most effective EAA supplement for muscle growth will have all the EAAs and roughly parallel the requirements cited above. However, alternative formulations may be “best” in different situations. For example, while a high proportion of leucine may be best for older individuals with heart failure, a disproportionate amount of leucine may not be needed by a young athlete after a resistance workout. This is because the resistance workout will activate mTOR and associated molecules, and if the proportion of leucine is in line with the composition of muscle protein (around 23%), then relatively more of all the other EAAs needed to produce complete protein can be included in the supplement.

Even the optimal formulation for exercise might vary, depending on when the supplement is consumed and the type of exercise. For example, endurance training causes a selective increase in leucine oxidation, in which case a supplement high in leucine would be optimal as a post-workout supplement following exercise to speed up muscle recovery.

If the EAA supplement is meant to be consumed as a pre-workout supplement for exercise performance, it may be formulated to optimize the concentrations of neurotransmitter precursor availability in addition to providing EAAs for muscle protein synthesis.

Regardless of the specific circumstance it is meant for, the “best” formulation will include all the EAAs and not just the BCAAs or specific amino acids like beta-alanine or arginine. A complete formulation will more effectively stimulate the production of new muscle protein than any individual or sub-group of EAAs possibly can.

Amino Acid Infusion: Is There an Advantage Over Oral Ingestion of Amino Acids?

Amino acids can be delivered either by intravenous infusion or oral ingestion. Both routes support protein metabolism in the body, as well as provide amino acids for other purposes. But what are the advantages and disadvantages of each?

The use of amino acid infusions to provide nutritional support to individuals incapable of eating a sufficient amount of dietary protein to meet nutritional requirements dates back to the 1960s. An amino acid infusion can either provide partial nutritional support or may be given as part of total parenteral nutrition (TPN). TPN provides all nutrition, including amino acids, carbohydrate, fat, and vitamin and minerals via intravenous infusion, or amino acid injections. But is there a significant advantage to taking amino acids intravenously over taking amino acids orally as a supplement?

Intravenous Amino Acids and TPN

Intravenous amino acids can provide nutritional therapy for protein metabolism (the breaking down and building up of proteins).

An amino acid infusion contains the amino acids with the greatest protein-stimulating effect. These include the essential amino acids leucine, isoleucine, lysine, valine, phenylalanine, histidine, threonine, methionine, and tryptophan, as well as the nonessential amino acids alanine, arginine, glycine, proline, serine, and tyrosine. These amino acids act as protein-building blocks, encouraging protein synthesis in muscle cells and preventing protein breakdown.

An amino acid injection is the administration of amino acids and other nutrients by way of parenteral nutrition. Parenteral administration utilizes routes outside the gastrointestinal (GI tract), such as intravenous routes. Enteral nutrition, on the other hand, is food or drug administered by way of the GI tract, such as with tube feeding.

Intravenous infusion of amino acids is used for patients who cannot take in food or nutrients through the enteral route (GI Tract). For instance, if gastrointestinal absorption is disrupted by inflammatory disease or obstruction, or if tube feeding is not providing adequate nutritional support.

Aminosyn® II is a popular amino acid injection given by way of peripheral vein or central vein infusion and used as a source of nitrogen in the short-term nutritional therapy of patients with adequate body fat who are unable to sustain oral nutrition. This type of amino acid infusion is also administered to help prevent or reverse negative nitrogen balance in patients who cannot take in nutrients via the enteral route.

Individuals who have had large portions of their intestines removed surgically can live indefinitely on total parenteral nutrition (TPN). A 15% amino acid injection can be administered by use of a central venous catheter or by peripheral vein. This amino acid infusion is coupled with vitamins, trace elements, electrolytes, and energy nutrients to provide the necessary nutritional support for weight maintenance or weight gain. In order for the amino acids from TPN to be adequately absorbed and utilized, energy requirements must be met. Energy is typically provided as a combination of dextrose to support carbohydrate metabolism and an intravenous fat emulsion that offers up essential fatty acids to protect against essential fatty acid deficiency and fulfill the dietary balance of fat and carbs.

TPN using amino acid injections can promote muscle protein synthesis, as well as meet other requirements for amino acids, including immune function and brain neurotransmitter synthesis.

The primary drawback to amino acid infusion as the sole source of amino acids from the physiological perspective is that the intestine atrophies. This is because some of the amino acid requirements of the gut are satisfied by direct uptake of amino acids from the digestion of orally ingested protein or amino acids. Atrophy makes the intestines more permeable to diffusion of bacteria and bacterial products from the gut into the body. Of course, if TPN is used because of the removal of the gut, this point is moot. If the intravenous infusion of amino acids is used alongside orally ingested protein, gut integrity will be maintained so long as the oral intake is sufficient.

Benefits of Amino Acid Infusion

The clinical benefits of amino acid infusion in patients who are incapable of ingesting adequate nutrition orally are well established. In addition, intravenous infusion of amino acids in individuals fully capable of ingesting amino acids orally is gaining popularity. The “selling point” of this therapy is that the exact concentrations of individual amino acids in the blood can be precisely controlled. This is promoted as particularly important to the relative concentrations of amino acid precursors of specific brain neurotransmitters. This approach is used in recovery from addiction, as well as for general support of protein metabolism in the body.

The premise of intravenous amino acid therapy is that the individual cannot get the full benefit from orally ingested amino acids, or that the intravenous infusion somehow confers special beneficial effects.

Advantages of Oral Ingestion of Amino Acids

The oral ingestion of amino acid solutions has advantages over amino acid infusion. There is no risk associated with oral ingestion, whereas intravenous infusion carries with it the risk of vein irritation. A health care provider is needed to perform the intravenous infusion, whereas free amino acids for oral consumption are relatively cheap and readily available.

It is possible to obtain a mixture of essential amino acids for oral consumption specifically designed for a particular condition, such as reaching your ideal body weight, whereas the options for intravenous infusion are much more limited due to the arduous procedure to obtain approval from the FDA.

There are also physiological advantages to the oral ingestion of amino acids over peripheral infusions. Most important of these is that the uptake and utilization of amino acid solutions by the intestines provides a direct source of essential nutrition.

Orally ingested amino acids are directly absorbed by the intestines and require no digestion. The amount of amino acids provided to the body by the two routes (oral and intravenous) are thus similar. Since orally ingested amino acids pass through the intestines, liver, and other organs before reaching the peripheral circulation, the peripheral plasma concentrations of amino acids reach higher levels when infused intravenously. Conversely, orally ingested amino acids provide more direct support of the internal organs.

Orally ingested and intravenously infused amino acids both stimulate muscle protein synthesis, which is the metabolic basis for muscle growth and strengthening. A clinical study of older individuals showed that muscle protein synthesis was stimulated in response to both intravenously infused as well as orally ingested amino acids. In addition, the profile of amino acid concentrations in the blood reflected the profile of the orally ingested amino acids, so there is no advantage to intravenous infusion in terms of supplying the proper balance of amino acids needed to synthesize neurotransmitters in the brain. Further, a clinical response was observed at dosage levels that are able to be consumed orally without much difficulty.

Side Effects of Amino Acid Injections

Amino acid infusions are now being marketed as a way to boost athletic endurance, protect against muscle loss, and even improve the health of the central nervous system. While amino acid solutions can indeed impart these benefits, amino acid injections were not originally developed for healthy individuals tackling body weight goals. Oral amino acid supplements, however, can help build muscle, sharpen cognitive function, and enhance athletic endurance, and there are no needles or doctors involved. It’s as easy as mixing an amino acid powder with water.

One of the biggest advantages of taking an oral amino acid supplement over an amino acid injection is that no special care is needed and there are no side effects to contend with.

Amino acid injections can cause the following adverse reactions:

  • Inflammation/redness at the injection site
  • Irritation
  • Nausea
  • Flushing
  • Fever
  • Allergic reactions
  • Weight gain
  • Jaundice
  • Urine changes
  • Weakness

Contraindications for amino acid injections are indicated for individuals in hepatic coma, with hepatic insufficiency, severely impaired kidney function or renal failure, or suffering from metabolic disorders due to compromised nitrogen utilization or hypersensitivity to one or more amino acids.

The Verdict

Amino acids can be delivered either by intravenous infusion or oral ingestion of amino acid solutions. Both routes support protein metabolism in the body, as well as provide amino acids for other purposes.

The intravenous infusion procedure has risks and costs that are avoided by oral ingestion, and the amino acid profiles in available intravenous infusion mixtures are limited. For these reasons, amino acid infusion should be used only in individuals who are incapable of ingesting amino acids or who have a limited capacity for absorption. Oral ingestion is the preferred route of delivery of amino acids in most circumstances.

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.

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.