The reasons why muscles wither with age is a problem that is intriguing a growing number of scientists. Drug companies are trying to develop drugs that can build muscles or forestall their weakening, while food companies are exploring nutritional products with the same objective.

Both doctors and patients need to be more aware that muscle deterioration is a major reason the elderly lose mobility.

According to the New York Times:

"... [S]arcopenia [age-related loss of muscles] affects about 10 percent of those over 60, with higher rates as age advances ... Causes of the loss of muscle mass or strength might include hormonal changes, sedentary lifestyles, oxidative damage, infiltration of fat into muscles, inflammation and resistance to insulin."

The best approach to restoring or maintaining muscle mass and strength is exercise. I would recommend trying Peak Fitness, a term I am coining to represent a comprehensive exercise program that includes far more than typical cardio training. The major change is that once or twice a week you do peak exercises, in which you raise your heart rate up to your anaerobic threshold for 20 to 30 seconds, and then you recover for 90 seconds.

You would repeat this cycle for a total of eight repetitions. We call it "peak fitness" because if you graph your heart rate, you will see that it peaks 8 times during the workout. One of the major reasons I am so enthusiastic about peak fitness is that it can actually increase your growth hormone level. This dramatically improves your muscle tone, and has many other beneficial effects as well!

---

By Ori Hofmekler

One of the most common fitness approaches has been failing miserably. Most people typically attempt to get "less fat" or "less unfit" rather than lean and fit. Most aim at getting "less unhealthy" rather than healthy. Perhaps you too have become accustomed to accept failure as the norm?

Our society is now getting fatter and sicker than ever in spite of the ever growing number of dieters and people who exercise regularly. Something is very wrong with our physical state and most of us aren't even aware of it.

The purpose of this article is to expose the misinformation and fallacies associated with common fitness strategies and present the true fundamental principles upon which human physical conditioning should be based.

My point: human fitness is not a random collection of exercises and it isn't about eating less junk food or popping megadoses of vitamins. Your fitness is created and maintained by a well-defined system. It is rooted in your biology and it's programmed in your genes. Human fitness is based on specific rules, and you need to know how to follow these rules.

Please understand that you possess genes that preserve and develop your muscles, and incredibly, these same genes also extend your life. Your body has an inherent muscle building mechanism that can be activated at any age. And there is no need to force your body to do anything that it isn't programmed for.

The truly exciting news is that there is no need for:

• Drugs or pills
• Wasting time on prolonged gym classes or hours of boring aerobic sessions
• Shoving in freaky amounts of protein all day long

But to turn on your muscle building mechanisms, you need to know what to do. You need to learn what the real triggers of your muscles are, and you need to know how to use these triggers.

So what are these triggers?

What are the facts, and where is the truth?

Facts: Certain nutrition and training protocols have been shown to build muscle, sustain health and promote longevity, whereas other protocols have shown to waste muscle, shatter health and shorten life. But due to a lack of true knowledge, most of us have no clue what to do.

We're largely unaware of what we're doing wrong and we don't even know what we're doing right.

Truth: Cutting through the misinformation and false theories which are so prevalent today, it's becoming more and more critical for us to know who we really are as a species.

You need to know what triggers your body to thrive, what triggers your muscles to develop and what causes them to degrade. When you know how to use the right triggers, you can unleash innate mechanisms that can literally transform pain to power, weakness to strength and sickness to health.

What Triggers Your Body to Thrive?

Your body is equipped with a highly sophisticated metabolic system, committed to one single mission: keeping you alive. And especially keeping you alive during times of adversity. It's amazing how well we're programmed for adversity. Your body is like a "stress converter". It turns pain to power.

Hunger, hardship and pain are the real triggers of your body. This may seem quite alarming for most people today, but nevertheless it's the truth. Challenging your body with these primal triggers is what forces it to adapt and improve. That's the premise of the Pain to Power principle.

Accumulating evidence indicates that your body thrives when challenged with nutritional and physical stress. Indeed both hunger and physical hardships have shown to benefit human survival. And the benefits you get from hunger and hardship seem to be deeply rooted in your biology.

The Pain to Power Principle

The lack of food apparently triggers a survival mechanism that helped humans endure times of food scarcity. And along similar lines, intense exercise bouts benefit you by triggering a primal mechanism that enabled early humans to endure extreme physical hardship.

These inherent mechanisms are part of the human survival apparatus. When triggered, they help you compensate by increasing energy production efficiency, improving body composition, increasing strength and increasing the capacity to resist fatigue and stress. Your survival requires challenge and action. The biological rule is as plain as it's bold:

Actively Survive or Passively Die!

It is now known that the human body evolved to better survive when challenged properly. Both your brain and muscle develop only when adequately stimulated. Yes, we often need to go through painful experiences to develop a skill. That's how soldiers, athletes, doctors and musicians are made. Pain comes with the territory. And the lack of mental or physical hardship can lead to stagnation and degradation.

Indeed, when passive, sedentary or "moderately" challenged, your body goes into waste. And the consequences include muscle degradation, excessive fat gain, chronic disease and a shortened life span.

Aging for instance, is a tissue wasting process.

Can you block this process?

You're certainly equipped with the means to counteract aging, but modern lifestyle and fitness systems are not designed for that.

What's Wrong with Your Fitness?

Nowadays, we don't need to hunt, fight or flee to survive, and hardly do we need to endure hunger. Virtually everything your early ancestors had to struggle for is now readily accessible. But this is the core of the problem.

We have been shifting away from our species' original program, and away from the necessity to actively survive. Typically our bodies are inadequately challenged. And the very stressors that had made our species thrive in the first place, don't apply to us today. These days, humans live "safely" like farm animals. And most of us are overfed and overweight.

So, What's the Solution?

To reclaim your fitness you need to know how to trigger the biological mechanism that preserves and builds your muscles.

Muscle retention is the most critical element of human fitness. Skeletal muscle plays key biological roles in keeping you strong, functional and healthy. Besides force production for physical movements, the muscle participates in the regulation of glucose and lipid metabolism and insulin sensitivity. And it protects you against obesity, diabetes and cardiovascular disease.

Muscle wasting such as due to lack of adequate exercise, disease or aging, leads to the loss of physical capacity, loss of physical shape and increased risk for chronic disease.

So how do you turn on your muscle building mechanism?

To trigger your innate muscle building mechanism you need to apply the appropriate physical and the nutritional triggers. Both of them are important. If you overlook one of them (by applying the physical triggers, say, without the nutritional triggers), your progress will be compromised.

To understand how all this works in practice, let's first take a look at the body's innate muscle building mechanism.

The Mechanism that Preserves and Builds Your Muscles

New developments in the field of human muscle biology have begun to unravel cellular mechanisms that regulate muscle protein synthesis and breakdown. The key muscle building mechanism in all mammals is a complex protein, part of the insulin pathway, called mTOR (mammalian target of rapamycin).

When activated, mTOR signals your muscle to increase protein synthesis. And when it's inhibited, your muscle protein synthesis shuts down, and protein breakdown increases. Note that it's the ratio of protein synthesis/protein breakdown that dictates whether you build or waste muscle.

There are three primary activators of mTOR in your muscle:

1. Growth factors and insulin
2. Amino acids
3. Mechano-overload (such as with weight lifting)

During exercise your mTOR is totally inhibited, but it's reactivated right after exercise and further enhanced by amino acids and insulin. With proper nutrition after exercise, mTOR boosts your muscle protein synthesis to a level that exceeds the rate of protein breakdown, leading to a positive protein balance in the muscle and a net gain of muscle mass.

Interestingly, mTOR responds to fasting in a similar way.

When your body is in a fasting state, mTOR is inhibited and upon feeding, it's reactivated and your muscle shifts from a catabolic to an anabolic state. Accumulating evidence indicates that both exercise and fasting initially cause muscle protein breakdown, but both stimulate protein synthesis after exercise and after feeding, respectively.

It seems that the same mechanism that inhibit protein synthesis during exercise and fasting, contributes to the stimulation of muscle protein anabolism right after.

The Window of Opportunity

mTOR is highly receptive to hormonal stimulation, particularly to insulin and IGF-1 (insulin-like growth factor-1). Note that IGF-1 production is stimulated by growth hormone and intense exercise but it needs insulin interference to finalize its actions. And all this comes into play during the recovery period after exercise.

Right after exercise, insulin can potentially kick in while IGF-1 is already at a peak level. That's the perfect time to feed the muscle and promote muscle gain. Indeed, the post exercise period has been recognized as "the window of opportunity".

Now that you know what triggers the mTOR, let's see what disrupts it.

What Disrupts Your Muscle Building Mechanism?

Since mTOR is part of the insulin pathway, it can be seriously disrupted due to insulin resistance. That's why diabetes is typically associated with muscle wasting. And that's why high glycemic diets (with their insulin shattering effects) are potentially detrimental to muscular development.

You can see why our typical Western diet that is largely based on refined carbohydrate food, has been failing to support your physique. Other disruptors of mTOR include caffeine, nutritional deficiencies and myopathy (muscle inflammatory disease). Note that caffeine inhibits mTOR in a similar manner to exercise.

Meaning: you can have your coffee before exercise but not right after.

So what kind of physical and nutritional triggers activate your mTOR?

Physical Triggers to Build Your Muscle -- Hint it is NOT Aerobics

Researchers have been finding that the main physical trigger for your mTOR is mechano-overload. Mechano-overload is a physical impact that can be achieved by "killer" strength, speed and push & pull drills. Intense killer drills turn on your mTOR to increase protein synthesis in your myofibrils (muscle fibers) and eventually lead to increased muscle size.

In technical terms, the mechano-overload impact on your muscle triggers the release of a cellular compound called phosphatydic acid, which in turn activates your mTOR. Note that moderate exercise and aerobics can't do this. They lack the intensity needed to yield this impact.

Aerobic training affects mainly your mitochondria (the cellular energy facility) but hardly affects your myofibrils. And even though aerobics yields some cardiovascular benefits, it fails to build muscle mass. And quite often, chronic prolonged aerobics drills can actually lead to loss of muscle size and diminished strength.

So is aerobics bad for you?

Researchers in the area of muscle biology and aging have been finding growing evidence that prolonged aerobics training increase the risk of oxidative damage in the muscle. This type of training causes overwhelming accumulation of free radicals in your muscle, which eventually increase the risk of oxidative damage in your tissues (myofibrils and mitochondria). And this risk of oxidative damage becomes increasingly higher as you get older.

On the other hand, intense exercise protocols which are inherently short, have shown to lower this risk. The short intense exercise protocol gives the muscle the time it needs to recuperate and counteract oxidative stress without depleting its antioxidant pool. And again, short intense exercise yield the right impact needed to trigger your mTOR and increase muscle mass.

But there is more to it.

The mechano-overload impact of intense exercise works directly on your fast muscle fibers, the type IIB and the type IIA. It's the fast muscle fibers that enable you to be strong and fast, and they have the largest capacity to generate force and gain size.

You need them when you climb stairs, carry heavy grocery bags, chop wood or move furniture. And if you lose that physical capacity, you lose your ability to live independently.

But the fast muscle fibers are most prone to damage and wasting and they're particularly prone to degradation during the aging process. And only intense exercise can trigger the mechanism that keeps these fibers intact.

Note that the physical triggers are only part of the equation. To build muscle, the physical triggers must be combined with the right nutritional triggers. Inadequate nutrition may lead to loss of muscle size and power regardless to how we exercise.

So what kind of nutritional triggers are needed?

The Nutritional Triggers for Muscle Growth

The main nutritional triggers for mTOR are essential amino acids and particularly the amino acid leucine. Studies reveal that intravenous administration of amino acids increase the rate of muscle protein synthesis after exercise and simultaneously lower the rate of muscle protein breakdown. Dietary protein seems to be the primary factor in muscle nourishment.

Researchers worldwide believe that the diet protocol that benefit human fitness most, is the high protein low carbohydrate diet.

Recent studies have been reporting substantial benefits of the high protein low carbohydrate diet on muscle conditioning and weight loss. A key element in this diet regimen appears to be the high intake of the amino acid leucine, which is part of the branch chain amino acids (leucine, isoleucine and valine).

Besides the stimulation of muscle protein synthesis, leucine has also shown the capacity to modulate insulin and blood sugar. But to further understand how leucine and amino acids regulate muscle buildup, we need to briefly review the role of dietary protein.

The Role of Dietary Protein in Increasing Muscle Growth

The role of dietary protein is to provide the 20 naturally occurring amino acids and especially the nine indispensible/essential amino acids.

Each amino acid has a unique requirement as a building block for body proteins. But some amino acids participate in additional metabolic roles. Most notable among them are the branch chain amino acids, and particularly leucine. Note that besides stimulation of your mTOR, leucine serves as a substrate for your muscle fueling when dietary carbohydrates are not available.

Let's take a closer look at leucine's actions.

Leucine and Muscle Protein Synthesis

Unlike other amino acids, which serve mainly as building blocks for muscle protein, leucine also signals your muscle to increase protein synthesis. Incredibly, leucine has shown to stimulate your muscle protein synthesis, even during times of food restriction or after prolonged physical hardship.

It is the sheer increase in circulating leucine concentration which triggers the mTOR.

On the cellular level, leucine stimulates phosphorylation of an inhibitory protein 4E-BP1 (4E-binding protein 1). And the removal of this inhibitory protein activates initiation factors to induce muscle protein synthesis.

Researchers believe that this unique role of leucine in the regulation of muscle protein synthesis is consistent with the sparing of lean body mass seen with high protein diets during weight loss.

Note that the highest concentrations of leucine and branched chain amino acids (BCAA) are found in dairy products; particularly quality cheese and whey protein. And even though leucine is relatively abundant in our food supply, it is often wasted as an energy substrate or used as a building block rather than an anabolic agent.

This means that to establish the right anabolic environment, you should try to increase leucine consumption beyond maintenance requirements.

But beware that only FOOD BASED leucine can benefit your muscles without side effects. Using leucine as a free form amino acid can be highly counterproductive.

Intravenous administration of free form amino acids including leucine has shown to cause severe hyperglycemic reactions and insulin resistance. Apparently, when free form amino acids are artificially administrated, they rapidly enter the circulation while disrupting insulin function, and impairing your body's glycemic control.

This proves again that we're programmed to benefit from whole food nutrition only.

So how much leucine in the form of foods, NOT supplements, do you need to consume for getting results?

Based on nitrogen-balance measurements, the requirement for leucine to maintain body protein is 1-3 grams daily. And to optimize its anabolic pathway, it has been estimated that leucine requirement should be about 8g - 16g daily.

The following chart presents leucine content in common foods:

Leucine Content in food / per 100g

Whey Protein Concentrate	8.0g
Raw Cheddar Cheese	3.6g
Lean Beef	1.7g
Salmon	1.6g
Almonds	1.5g
Chicken	1.4g
Chick Peas	1.4g
Raw Eggs	1.0g
Egg Yolk	1.4g
Sheep Milk	0.6g
Pork	0.4g
Cow Milk	0.3g

This means that to get the minimum 8 gram leucine requirement for anabolic purposes, you need the following amounts of food:

• a pound and a half of chicken
• three pounds of pork
• over a pound of almonds (over 3000 calories)
• over a pound and a half of raw eggs (16 eggs)
• half a pound of raw cheddar cheese

and remarkably, only 3oz of high-quality whey.

As you can see, whey protein supplementation can effectively allow you to get the minimum leucine you need to build muscle without consuming freaky amounts of food and calories.

Note that the anabolic impact of leucine is proportional to its availability and is dependent on its circulating levels. In other words, the more leucine you consume from food, the better chances for anabolic impact you get.

But there is one more factor that can dictate whether you gain or lose muscle mass. And that's the glycemic factor.

The Glycemic Factor

As noted, the triggering of your mTOR to increase muscle mass requires healthy insulin and glucose homeostasis. Any impairment in the regulation of blood glucose and insulin activity could inactivate your mTOR and jeopardize your muscle protein synthesis.

Studies have reported that dietary protein has beneficial stabilizing effect on insulin levels when entering the circulation from ingested food. In other words, protein food benefits your body's glycemic control. And furthermore, protein serves as a perfect fuel during times of fasting and intense physical hardship.

Protein is Your Perfect Fuel During Intense Training

Amino acids can serve as the ideal muscle fuel during intense exercise. But note that your body uses only certain amino acids for muscle fueling.

As a general rule, a large percentage of dietary amino acids are oxidized before even reaching your circulation. Nearly 100 percent of dietary glutamate and glutamine and nearly 40 percent of phenylalanine are removed during the absorption process, largely by oxidative degeneration.

But the exception to this pattern of protein degradation are the branch chain amino acids (BCAA), with over 80 percent of dietary content of leucine, valine and isoleucine reaching circulation.

It seems that the body spares these amino acids for one purpose: Muscle fueling.

Scientists now know that BCAA and leucine reach your muscle directly to serve as emergency fuel. BCAA contribute carbon to synthesize glucose via the alanine glucose cycle. Called gluconeogenesis, this process converts BCAA into alanine and glutamine which then serve as carbon donors to the production of glucose.

And all this without spiking insulin.

It has been reported that the alanine-glucose cycle accounts for 40 percent of endogenous glucose production during prolonged exercise. Gluconeogenesis occurs mainly in the liver and it grants a perfect supply of glucose to the muscle tissues during fasting and exercise. Your liver releases to the muscles exactly the right amount of glucose needed.

This fueling mechanism is so efficient that it persistently keeps blood sugar from overspiking or overplummeting. In other words, amino acids serve as PRIMARY FUEL during times of intense physical or nutritional stress. They could be the ideal fuel for athletes engaged in non-aerobic drills including weight lifters, wrestlers and mixed martial artists.

That's the right fuel to prevent "hitting the wall".

It's plausible that we evolved to possess this perfect protein fueling mechanism during primordial times when humans were engaged in extreme physical hardship while being on a frugal diet that was primarily low glycemic, devoid of grains and sugar. In fact, this fueling system benefits us only when we're deprived of dietary carbs.

High carb meals shut down this primal fueling mechanism and your body shifts instead to the less effective carbohydrate fuel.

So is Carbohydrate Fuel Bad for You?

Endurance athletes such as long distance runners can certainly benefit from complex carb loading. For aerobics training, complex carbs are certainly a viable fuel. However, there is growing evidence that the human body has not evolved to do well on a high carbohydrate diet. And as we age, we tend to further lose our tolerance to carbohydrate food and particularly to the glycemic load.

Recent studies reveal that the addition of simple carbohydrates to protein supplement negated the anabolic impact of the protein, and blunted muscle protein synthesis in a group of healthy people over 60. These are the facts and we can't afford overlooking them.

One of the major problems with today's fitness is the ignorance towards muscle fueling. We have been shifting away from the primal low glycemic fat/protein fuel into the high glycemic carbohydrate fuel and again, we pay the consequences with ever growing rates of diabetes, obesity and related disorders.

To retain and improve your physical shape, you must shift back to the low glycemic fuel foods you were originally programmed for. And by all means, you should minimize the consumption of high glycemic foods and avoid all sport nutrition and diet products (bars and powders) that are high in sugar or refined carbs.

How Can You Translate All this into Practice?

More studies are needed to fully elucidate the role of nutrition and exercise in supporting your health and physical condition. As for your fitness, there are obviously additional topics which must be addressed.

• How should you combine food?
• What's the right meal timing?
• And how much should you eat per meal?
• When do you need fast assimilating protein?
• And when do you need slow assimilating protein?
• What is the best protein food for your muscle?
• And what's the best protein blend?
• How does the muscle fueling system work?
• Who needs carb fuel?
• Who needs fat fuel?
• Why is training complexity so critical?
• What training regimen protects your neuro-muscular system from degradation?
• How long and how often should you train?
• Can you improve your muscle fibers quality?
• Can you possibly develop a hybrid super muscle fiber?
• And could you adjust our diet/training protocol to counteract aging and prevent muscle wasting?

Obviously there isn't enough space here to cover all this. Nonetheless, we can still draw some important conclusions based on the information in this article.

Following are practical guidelines to the right physical and nutritional protocols.

The Physical Protocol

Train intensely in short intervals. The short intense exercise intervals protocol has shown to improve body composition (build muscle, burn fat) more than the prolonged moderate exercise and aerobics. It has also shown to help counteract muscle aging by retaining fast muscle fibers and increasing the capacity to perform intense, physical tasks.

Avoid long aerobic cardio sessions.

• Incorporate strength and speed exercises with intense push and pull drills to maximize the mechano-overload impact on the muscle. Keep increasing your exercise intensity (weight load, speed and complexity) as you progress to keep your muscles adequately challenged.
• Work your whole body rather than body parts. Isolation exercise have a limited and often limiting effect on your progress.
• Incorporate minimum rest between intervals. This will force your body to improve its durability and strength at the same time.

Remember to keep challenging your body. To do that, rotate your exercise routine; change the order of your exercises and add new elements to your drills.

Incorporate drills that mimic fight or flight activities, such as punches, kicks and sprints. Like other species, we're inherently programmed to improve our physical capacity and resiliency to stress by unlocking this primitive survival apparatus within us.

Avoid moderate exercise. Moderation is fatal to muscular development. High intensity programs like CFT (Controlled Fatigue Training) and Peak 8 are ideal to help improve your fitness level.

The Nutritional Protocol

Follow a high protein, low glycemic diet. Keep a high ratio of protein/carbohydrates to improve body composition.

Here are a few other key points:

• Increase your intake of leucine rich foods such as high quality whey protein, raw cheese and organic, pasture-raised eggs.
• Increase the gap between meals to potentiate the anabolic effect of each meal. Remember, fasting stimulates a substantial peak in muscle protein synthesis when feeding is resumed.
• Feed your muscle with quality whey protein after exercise. Make sure the whey protein is derived from grass fed cows and is cold processed. Note that whey protein is the fastest to assimilate among all protein foods. Its anabolic impact after exercise is unmatched. Whey protein is also ideal for muscle fueling before exercise. It has the highest content of leucine and BCAA among all foods.

For best results, incorporate at least two recovery meals after exercise / 20g-30g protein per meal. 20g is about the threshold amount of protein needed to grant maximum utilization efficiency without wasting nitrogen.

Keep 1-3 hours gap between meals (depends on meal size).

Make all your muscle meals low glycemic. Avoid protein bars and powders made with added sugar. Note that mixing whey protein with low glycemic fruits such as berries is ok. This will not cause a substantial increase in the glycemic load of your meal. 

Ideally you should have your whey (recovery meal) about 30 min after training. This is about the time when your muscle is most recipient to assimilating nutrients and protein. Feeding after exercise comes with another bonus: increased metabolic adaptation efficiency to deposit protein in the muscle and burn fat.

A recent article in the Journal of Physiology (Nov 2010) indicated that exercising while fasting and then eating a meal, promotes weight loss and muscle gain. That’s In comparison with eating the same meal before exercise which had shown to  cause fat gain and less protein deposit in your muscle. The researchers reported that the increased muscle protein synthesis in the muscle as observed in people who exercise while fasting and then ate a meal, has to do with increased insulin sensitivity and the activation of the muscle mTOR (the mechanism that builds muscle).

Simply put: Eating after training helps you lean down while gaining muscle mass. Which is unlike eating before training.

As for the sugar content of Miracle Whey, the 5 grams sugar are naturally occurring mostly in the dairy. These sugars are low glycemic and have minimum effect on your insulin.

The maltodextrin content should be labeled as naturally occurring  digestive resistant maltodextrin, which Is a non-digestible fiber. This is just another name for a water soluble fiber (long chain saccarides) that naturally occur in maize and other plants. That fiber has shown to help lower blood sugar and blood lipids. And it also works as a pre-biotic food to support health gut flora. Probiotics are essentially important for the digestion and utilization of protein. In fact, probiotics increase the biological value of the protein.

As for the total carbohydrate content, it actually includes the fiber content which is registered as a carbohydrate.

Miracle Whey is low glycemic, high-protein whey meal, specifically designed to yield maximum biological value and best protein utilization, particularly after exercise. .

Additionally:

• Increase your intake of antioxidants from fruits and vegetables to support your muscle antioxidant defenses and allow recuperation and buildup.
• Stay away from any product made with added fructose. Fructose is the worst fuel for your muscles.
• Start your morning with a whey protein meal to cover your minimum leucine requirement. This will allow all additional protein meals to become increasingly anabolic (by releasing extra leucine for anabolic purposes).
• Use whey meals as a primary source of protein during the day to grant maximum protein/leucine loading efficiency with minimum digestive stress.
• Have your slow assimilating proteins (eggs, cheese, fish or meat) at night to grant a steady release of leucine and a long lasting anabolic impact during the sleeping hours.
• One way to spare leucine for anabolic purposes is by adding coconuts' MCT (medium chain triglycerides) to a whey protein meal. MCT has shown the capacity to swiftly convert to energy without spiking insulin and without the need for bile acid digestion. MCT can help shift leucine's pathway from fueling into muscle building.
• Keep your diet clean from chemicals, pesticides and preservatives to minimize the metabolic stress on your body. Accumulated metabolic stress and toxicity present major obstacles to muscle recuperation and buildup.

Final Note

Life isn't just about looking hard and feeling strong. And often you get too busy to pay attention to how you eat or exercise. Nevertheless, with the right knowledge and practice, you can become increasingly efficient in restoring and improving your physical shape even when your available time is scarce.

The protocols suggested here can fit any lifestyle. Even 10 minutes of intense exercise can still yield positive results while you're on a super busy schedule. And you can easily pre-pack whey protein in your bag or case and bring it with you anywhere you go. Life requires you to act.

The choice is now in your hands.

---

About the Author

Ori Hofmekler is the author of The Warrior Diet, The Anti-Estrogenic Diet, Maximum Muscle Minimum Fat, and the upcoming book Unlocking the Muscle Gene/North Atlantic Books.

---

References

• Layman, D.K., Baum, J.I. 2004. Dietary Protein Impact on Glycemic Control during Weight Loss. The American Society for Nutritional Sciences. J Nutr. 134:968S-973S, April 2004.
• Layman, D.K., Baum, J.I. 2004. The Emerging Role of Dairy Proteins and Bioactive Peptides in Nutrition and Health. The American Society for Nutritional Sciences. J. Nutr. 134:968S-973S, April 2004.
• Svanberg, E., Jefferson, L.S., Lundhold, K., Kimball, S.R. 1997. Postprandial stimulation of muscle protein synthesis is independent of changes in insulin. Endocrinology and Metabolism, Vol. 272, Issue 5 E841-E847.
• Hirsch, J., Hudgin, L.C., Leibel, R.L., Rosenbaum, M. 1998. Diet composition and energy balance in humans. Am. J. Clin. Nutr. 67: 551S-555S.
• Skov, A.R., Toubro, S., Ronn, B., Holm, L. & Astrup, A. 1999. Randomized trial on protein vs carbohydrate in ad libitum fat reduced diet for the treatment of obesity. lnt. J. Obes. 23:528-536.
• Layman. D.K., Boileau, R.A., Erickson. D.J., Painter, J.E., Shiue, H., Sather, C., Christou, D.D. 2003. A reduced ratio of dietary carbohydrate to protein improves body composition and blood lipid profiles during weight loss in men. J. Nutr. 133:411-417.
• Reeds., P.J., Burrin, D.G., Davis, T.A., Stoll B. l998. Amino acid metabolism and the energetic of growth. Arch. Anim. Nutr. 51:187-197.
• Gautsch, T.A., Anthony, J.C., Kimball, S.R., Paul, G.L., Layman, D.K., Jefferson, L S. 1998. Availability of cIF4E regulates skeletal muscle protein synthesis during recovery from exercise. Am. J. Physiol. Cell Physiol. 274:C406-C414.
• Layman, D.K. 2002. Role of leucine in protein metabolism during exercise and recovery. Can. J. Appl. Physiol. 27:592-608.
• Layman, D.K. 2003. The role of leucine in weight loss diets and glucose homeostasis. J. Nutr. 133:261S-267S.
• Layman. D.K., Shiue, H., Sather, C., Erickson, D.J., Baum, J. 2003. Increased dietary protein modifies glucose and insulin homeostasis in adult women during weight loss. J. Nutr. 133:405-410.
• Pacy, P.J., Price, G.M., Halliday, D., Quevedo, M.R., Millward, D.J. 1994. Nitrogen homeostasis in man: the diurnal responses of protein synthesis and degradation and amino acid oxidation to diets with increasing protein intakes. Clin. Sci. 86: 103-118.
• Fernstrom, J.D., Wurtman, R.J. 1972. Brain serotonin content: physiological regulation by plasma neutral amino acids. Science 178:414-416.
• Fornstrom, M.H., Fernstrom, J.D. 1995. Brain tryptophan concentrations and scrotonin synthesis remain responsive to food consumption after the ingestion of sequential meals. Am. J. Clin. Nutr. 61:312-319.
• Moncada, S., Higgs, E.A. 1995. Molecular mechanisms and therapeutic strategies related to nitric oxide. FASEB J. 9:1319-1330.
• Wu, G., Morris, S.M. 1998. Arginine metabolism: nitric oxide and beyond. Biochem. J. 336:1-17.
• FAO/WHO/UNU 1985. Energy and protein requirements. Report of joint FAO/WHO/UNU expert consultation. WHO Tech. Rep. Sev. 724:1-206.
• Wagenmaker, A.J.M. 1998. Muscle amino acid metabolism at rest and during exercise: role in human physiology and metabolism. Exerc. Sport Sci. Rev. 26:287-314.
• Rennie, M.J, Tipton, K. D. 2000. Protein and amino acid metabolism during and after exercise and the effects of nutrition. Annu. Rev. Nutr. 20:457-483.
• Kimball, S.R., Jefferson, L.S. 2001. Regulation of protein synthesis by branched-chain amino acids. Curr. Opin. Clin. Nutr. Metab. Care. 4:39-43.
• Ruderman, N.B. 1975. Muscle amino acid metabolism and gluconcogenesis. Ann. Rev. Med. 26:245-258.
• El-Khoury, A.E., Kukagawa, N.K., Sanchez, M., Tsay. R.H, Gleason, R.E., Chapman, T.E., Young. V.R. 1994. The 24-h pattern and rate of leucine oxidation, with particular reference to tracer estimates of leucine requirements in healthy adults. Am. J. Clin. Nutr. 59:1012-1020.
• Krebs, M., Krssak, M., Bemroider, E., Anderwald, C., Brehm, A., Meyerspeer, M., Nowotny, P., Roth, E., Waldhausl, W., Roden, M. 2002. Mechanism of amino acid-induced skeletal muscle insulin resistance in humans. Diabetes. 51:599-605.
• Floyd. J.C., Fajans, S.S., Conn, J.W., Knopl, R.F., Rull, J. 1966. Stimulation of insulin secretion by amino acids. J. Clin. Invest. 45:1487-1502.
• Reavens, G.M. 1993. Role of insulin resistance in human disease (Syndrome X): an expanded definition. Annu. Rev. Mod. 44:121-131.
• Baum, J.I., Seyler, J.E., O'Conner, J.C., Freund, G.G., Layman, D.K. 2003. The effect of leucine on glucose homeostasis and the insulin signaling pathway. FASEB J. 17:A811.
• Layman, D.K., Evans, E.M., Erickson, D., Seyler, J., Weber, J., Bagshaw, O., Griel, A., Psota, A., Kris-Etherton, P. A Moderate Protein Diet Produces Sustained Weight Loss and Long Term Changes in Body Composition and Blood Lipids in Obese Adults. J. Nutr., March 1, 2009; 139(3): 514-521.
• Paddon-Jones, D., Westman, E., Mattes, R.D., Wolfe, R.R., Astrup, A., Westerterp-Phantenga, M. Protein, weight management, and satiety. Am. J. Clinical Nutrition, May 1, 2008; 87(5): 1558S-1561S.
• Millward, D.J., Layman, D.K., Tome, D., Schaafsma, G. Protein quality assessment: impact of expanding understanding of protein and amino acid needs for optimal health. Am. J. Clinical Nutrition, May 1, 2008; 87(5); 1576S-1581S.
• Baum, J.I., Layman, D.K., Freund, G.G., Rahn, K.A., Nakamura, M.T., Yudell, B.E. A Reduced Carbohydrate, Increased Protein Diet Stabilizes Glycemic Control and Minimizes Adipose Tissue Glucose Disposal in Rats. J. Nutr., July 1, 2006; 136(7); 1855-1861.
• Norton, L.E., Layman, D.K. Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise. J. Nutr., February 1, 2006; 136(2); 533S-537S.
• Layman, D.K., Walker, D.A. Potential Importance of Leucine in Treatment of Obesity and the Metabolic Syndrome. J. Nutr., January 1, 2006; 136(1): 319S-323S.
• Garlick, P.J. The Role of Leucine in the Regulation of Protein Metabolism. J. Nutr., June 1, 2005; 135(6): 1553S-1556S.
• Koopman R, van Loon LJ. Aging, exercise, and muscle protein metabolism. J Appl Physiol. 106:2040-2048. First published January 8, 2009.
• Boirie Y, Dangin M, Gachon P, Vasson M-P, Maubois J-L, Beaufrere B. 1997. Slow and fast dietary proteins differently modulate postprandial protein accretion. Laboratorire de Nutrition Humaine, University Clermont Auvergne, Centre de Recherche en Nutrition Humaine, BP 321, 6.
• Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, Ritz P, Antoine JM, Prugnaud J, Beaufrere B, et aI. Protein pulse feeding improves protein retention in elderly women. Am. J. Clinical Nutrition 1999;69(6):1202-8.
• Boutrif, E. Recent developments in protein quality evaluation. Food, Nutrition and Agriculture. 1991;2/3:36-40.
• Doherty TJ. Invited Review: Aging and sarcopenia. J. Appl Physiol 2003;95(4):1717-27.
• Fitts RH, Widrick, JJ. Muscle mechanics: adaptations with exercise training. Exerc. Sport Sci. Rev. 1996;24:427-73.
• Hannan D. Free radical theory of aging: role of free radicals in the origination and evolution of life, aging and
• disease process. In Biology of aging, Eds. Johnson, J., Walford, R. Hannan, D., Miguel, J. New York: Liss, 1986,
• 3-50.
• Hasten, DL, Pak-Loduca J, Obert KA, Yarasheski KE. Resistance exercise acutely increases MHC and mixed muscle protein synthesis rates in 78-84 and 23-32 yr olds. Am. J. Physiol Endocrinol Metab. 2000;278(4):5620-E626.
• Hsich RH, Hou, JH, Hsu HS, Wei, YH. Age-dependent respiratory function decline and DNA deletions in human muscle mitochondria. Biochem. Mol. Biol. Int. 1994;32: 1009-22.
• Hunt JV, Dean RT, Wolff SP. Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and
• ageing. Biochem. J. 1988;256:205-12.
• Jostarndt-Fogen K, Puntschart A, Hoppeler H, Billeter R. Fibre-type specific expression of fast and slow essential myosin light chain mRNAs in trained human skeletal muscles. Acta. Physiol. Scand. 1998;164:299-308 .
• Jubrias SA, Esselman PC, Price LB, Cress ME, Conley, KE. Large energetic adaptations of elderly muscle to resistance and endurance training. J. Appl Physiol. 2001;90(5):1663-70.
• Karlsson J. Exercise, muscle metabolism and the antioxidant defense. World Rev. Nutr. Diet. 1997;82:81-100.
• Larsson L, Grimby G, Karlsson J. Muscle strength and speed a movement in relation to age and muscle morphology. J. Appl. Physiol 1979;46:451-6.
• Lee CK, Klopp RC, Weindruch R, Prolla TA. Gene expression profile of aging and its retardation by calorie restriction. Science 1999;285: 1390-3.
• Leewenburgh C, Fiebig R, Chandwancy R Ji. Aging and exercise training in skeletal muscle: responses of glutathione and antioxidant enzyme systems. Am.]. Physiol 1994;267:R439-45 .
• Lemon PWR. Beyond the Zone: Protein Needs of Active Individuals. J. Am. Coll. Nutr. 2000;19:5135-S21.
• Lexell J. Human aging, muscle mass, and fiber type composition. J. Gerontol A. Biol Sci. Med. Sci. 1995;50A:11-6.
• Lexell J, Downham D. What is the effect of ageing on type 2 muscle fibres? J. Neurol Sci. 1992;107: 250-1.
• Makrdies L, Heigenhauser JG, McCartney N, Jones NL. Maximal short term exercise capacity in healthy subjects aged 13-70 years. Clin. Sci. Lond. 1996;69:197-205.
• Marx JO, Kraemer WJ, Nindl BC, Larsson L. Effects of Aging on Human Skeletal Muscle Myosin Heavy-Chain mRNA Content and Protein Isoform Expression. J Gerontol A. Biol. Sci. Med. Sci. 2002;57 (6):B232-8.
• Mattson M. The need for controlled studies of the effects of meal frequency on health. Lancer. 2005;365:1978-80.
• Miguel J, Fleming J; Theoretical and experimental support for an "oxygen radical mitochondrial injury" hypothesis of cell aging. In: Biology of aging. Eds. Johnson, J., Walford, R., Harman, D., Miquel, J. New York: Liss, 1993, 51-76.
• Paddon-Jones D, Sheffield-Moore M, Zhang XJ, Volpi E, Wolf SE, Aarsland A, Ferrando AA, Wolfe RR. Amino acid ingestion improves muscle protein synthesis in the young and elderly. Am. J. Physiol Endrincrinol Metab. 2004;286(3) :E321-8.
• Putman CT, Jones NL, Lands LC, BLagg TM, Hollidge-Horvat MG, Heigenhauser CJ. Skeletal muscle pyruvate dehydrogenase activity during maximal exercise in humans. Am J. Physiol. 1995;269(Endomnol. Metab. 32):E458-68.
• Roubenoff R. Sarcopenia: Effects on Body Composition and Function. J. Gerontol. A. Biol. Sci. Med. Sci. 2003;58(11):M1012-7.
• Short KR, Vittone JL, Bigelow ML, Proctor DN, Nair KS. Age and aerobic exercise training effects on whole body and muscle protein metabolism. Am. J. Physiol. Endocrinol. Metab. 2004;286(1):E92-2101.
• Staron RS, Malicky ES, Leonardi MJ, et al. Muscle hypertrophy and fast fiber type conversions in heavy resistance-trained women. Eur. J. Appl. Physiol. Occup. Physiol. 1990;60:71-9.
• Tiidus PM. Radical species in inflammation and overtraining. Can. J. Physiol. Pharmacol. 1998;76(5):533-8.
•  
• fitness.mercola.com/sites/fitness/archive/2011/01/05/best-way-to-prevent-inevitable-muscle-wasting-as-you-age.aspx

 

• Physical Fitness
• Sleep
• Go Back

Related in this Category