Tag Archives: Nutrition Science

Why Most Diets Fail

7212-eat1It’s a common observation that most diets fail, but the reason they fail isn’t about the weight loss. In fact, most diets are successful in that regard if the dieter has any degree of discipline and motivation. The reason most diets fail is that the dieter fails to keep the weight off. You can easily observe the phenomenon in the dieting efforts of celebrities who have weight problems.

Oprah Winfrey is a notable example. Years ago Oprah went on a special liquid-protein diet that resulted in her losing 67 pounds of fat, which she proudly wheeled out in a wheelbarrow on her TV show (not her real fat, just 67 pounds of animal fat). Alas, her svelte figure turned out to be painfully ephemeral, as Oprah soon gained all the weight back and then some.

More recent examples include most participants in the popular TV show “The Biggest Loser”—although the high recidivism rate there isn’t surprising, as the program involves a crash diet with a lot of exercise. That’s a stress on the body’s reserves that cannot be sustained, and as a result, the weight soon returns.

In fact, only one out of every six dieters is able to maintain a 10 percent weight loss after a year, and studies suggest that as many as 97 percent of those who lose bodyfat from dieting alone will gain it all back, often within a year. Why is that figure so high?

When you lose weight, your body adapts to the reduced calories through a process called adaptive thermogenesis, which is a fancy way of saying that, because of the reduced mass, it burns fewer calories than it did prior to the weight loss. Unless you can continue to eat fewer calories, your weight-loss efforts are doomed.

What’s more, other studies show that your body works against you. Research done years ago suggests that there’s an “appestat” in the brain, likely in the appetite center of the hypothalamus, that must be reset to adjust to a new calorie level. The problem is that it takes years to occur—some have suggested up to five years for the brain to adjust to a chronic lower caloric intake. In the meantime you will be extremely hungry most of the time, which doesn’t bode well for long-term weight loss.

Does the type of diet you eat make a difference? Indeed, some hormonal factors are affected by diet type, which could play a major role in your weight-loss success. Leptin, a protein released from fat cells that signals to the brain that the cells are full, is one, as are insulin and thyroid hormones.

More recent research shows that the key diet factors that determine appetite control—and weight-loss success—are carbohydrate and to a lesser extent protein. Specifically, eating greater amounts of unprocessed and low-glycemic-index carbs helps control appetite and prevent fat gain by modulating the activity of insulin.

Protein is important because the body burns more calories to process it and also because it directly affects appetite. For example, several studies have clearly shown that concentrated protein supplements, such as whey, provide a satiating effect on appetite—which, of course, makes dieting a bit easier and aids your efforts.

Recently, French researchers delineated precisely how that works. After you take in a high-protein food source, small protein residues called oligo-peptides interact with certain opiate receptors in the gut, sending a message to the brain. The brain responds with a message back to the gut via the nervous system. That triggers the release of glucose in the intestine, which sends another signal to the brain that results in appetite suppression.

A major reason that the weight returns after a diet is energy expenditure. The body has two types of energy expenditure: resting, which is the energy expended to keep the body alive—heart function, brain function and so on—and total energy expenditure, which includes both resting energy and that burned in activity. You don’t have to be a scientist to realize that lowered energy expenditure after a diet is over would tend to favor a return of lost weight, especially if you also can’t maintain the calorie reduction. So what types of diets favor greater resting and total energy use?

That was the focus of a widely reported study published in the prestigious Journal of the American Medical Association.1 Twenty-one overweight men and women, aged 18 to 40, followed one of three diets, all of which contained the same number of total calories but different macronutrient contents. This was a crossover-designed study, in which the subjects followed all three diets at different times.

Before they started, however, they went on another diet and achieved a 10 to 15 percent weight loss. So the study focused on maintenance diets, designed to keep the lost weight off:

1) Lowfat diet: 60 percent carb, 20 percent fat, 20 percent protein—the diet most commonly recommended for weight loss and health.

2) Low-glycemic-index diet: 40 percent carb, 40 percent fat, 20 percent protein.

3) Very low-carb diet: 10 percent carb, 60 percent fat, 30 percent protein—similar to the popular Atkins low-carb plan. It’s also similar to the way many bodybuilders eat when trying to lose excess bodyfat, although bodybuilders would have less fat and more protein.

The subjects stayed on each diet for four weeks. Those on the low-carb diet also got a fiber supplement that supplied three grams with each meal. That’s important, as constipation is a frequent side effect of low-carb diets that eliminate dietary fiber sources, such as fruits and vegetables.

The low-glycemic diet focused on carb sources that wouldn’t produce a rapid release of glucose in the body, such as vegetables, fruits and legumes. It minimized grains, which do trigger a higher glucose release.

The results showed that the lowfat diet, the most frequently recommended diet for weight loss, produced the lowest energy expenditure of the three. The low-glycemic diet produced greater rates of both resting and total energy expenditure; however, the low-carb plan produced the highest rates of both types. Specifically, the low-carb diet burned 67 more calories a day at rest than the lowfat plan, but the difference in total energy was a whopping 300 calories a day between the two diets. That wasn’t a thyroid effect, either, since the subjects showed slightly depressed thyroid output when on the low-carb plan compared to the other two diets. Thyroid, of course, controls the resting metabolic rate. Various other studies have shown that thyroid output is lower when subjects are on a very low-carb diet, but it obviously didn’t affect the energy expenditure in this study.

The subjects showed the greatest leptin sensitivity when they were on the low-carb diet, and that may have affected the energy expenditure. The low-carb diet also produced the greatest effect on high-density lipoprotein, which is considered highly beneficial for the prevention of cardiovascular disease. Another cardiac risk factor lowered during the low-carb diet was blood triglycerides.

On the negative side, the 24-hour urinary cortisol measure was highest on the low-carb diet. That’s indicative of stress. Previous studies have also shown higher cortisol for subjects who were on a very low-carb diet but not a moderate-carb diet. While higher cortisol is associated with increased fat deposition in the trunk of the body, insulin resistance and cardiovascular disease, I suggest that the cortisol was elevated because one of its the lesser known functions is to mobilize fat for energy. I believe that the low-carb diet triggered a much greater use of fat for energy, which may explain the higher cortisol. Cortisol is also the body’s major catabolic hormone, but its activity in that regard is offset by the greater protein intake, which is a feature of low-carb diets.

The low-carb diet also produced more C-reactive protein, a nonspecific measure of inflammation. Here, too, I think the reason is that the subjects were not engaged in intense exercise, and the high fat content of the low-carb diet (60 percent) likely produced the higher C-reactive protein. Had the subjects engaged in exercise, the CRP would not be an issue, I believe, but the major explanation for the higher CRP seen with the low-carb plan was lack of fiber. While the subjects did take a supplemental three grams of fiber per meal, their total daily intake was only 11.2 grams. Compare that to the average intake of 30.3 grams on the lowfat diet and 32.8 grams on the low-glycemic diet. The suggested daily intake for fiber is 30 to 50 grams, and lack of fiber is known to boost C-reactive protein and inflammation in the body.

The authors suggest that based on their initial findings, the often suggested lowfat, high-carb diet is the most likely to result in a rapid regain of weight due to changes in energy expenditure and a negative effect on leptin activity. Although the low-carb diet produced the best effects in terms of healthful changes in the body as well as energy use, they think it may be problematic because of the adverse effects on cortisol metabolism and CRP. They suggest that the best way to go for maintaining lost weight is the low-glycemic-index diet.

For bodybuilding purposes it would need to be modified, since it contains only 20 percent protein. A better plan might be to lower the fat from 40 to 30 percent with an emphasis on “good fats,” such as omega-3 and monounsaturated sources, and an increase in protein from 20 to 30 percent to foster lean-mass maintenance and counter any cortisol effects. —Jerry Brainum

 

Editor’s note: Have you been ripped off by supplement makers whose products don’t work as advertised? Want to know the truth about them? Check out Natural Anabolics, available at JerryBrainum.com.

 

1 Ebbeling, CB, et al. (2012). Effects of dietary composition on energy expenditure during weight-loss maintenance. JAMA. 307:2627-2634.

Pine Bark Extract

7209-prime4Study results have shown that taking a daily dose of the pine bark extract pycnogenol may help to treat or prevent metabolic syndrome, a condition that is linked to type 2 diabetes and cardiovascular disease. Researchers administered 150 milligrams per day of the extract to 64 subjects, aged 45 to 55  years, who had exhibited all five risk factors for metabolic syndrome for six months. Another group of 66 matched participants served as controls.

The researchers found that supplementation with the pine bark extract was correlated with reductions in waist circumference, triglycerides, fasting blood glucose and blood pressure and an increase in HDL cholesterol, a.k.a. the good cholesterol. They concluded that the extract may help improve health-risk factors in people with metabolic syndrome.

Belcaro, G., et al. (2013). Pycnogenol® supplementation improves health risk factors in subjects with metabolic syndrome. Phytother Res. Published online January 28.

Sleep Problems Linked to Prostate Cancer

A study of 2,102 men suggests that those who suffer from sleep problems have a significantly increased risk of developing prostate cancer. Lara G. Sigurdardóttir, M.D., of the University of Iceland in Reykjavik, and colleagues questioned participants regarding whether they took medications to help sleep, had trouble falling asleep, woke up during the night and had difficulty going back to sleep or woke up early in the morning and had difficulty going back to sleep. At the start of the study 8.7 percent of the participants reported severe sleep problems and 5.7 percent reported very severe problems. None of the participants had prostate cancer. The researchers followed the participants for five years, during which time 6.4 percent of the subjects were diagnosed with prostate cancer. Analysis revealed that the risk for prostate cancer increased proportionately with the severity of reported problems falling and staying asleep. The men with the most severe sleep problems were more than twice as likely to have developed prostate cancer as the men who reported no sleep problems. Furthermore, the association between advanced prostate cancer and sleep problems was even stronger, with men who reported “very severe” sleep problems having more than a threefold increased risk of advanced prostate cancer.

“Sleep problems are very common in modern society and can have adverse health consequences,” said Dr Sigurdardóttir. “If our results are confirmed with further studies, sleep may become a potential target for intervention to reduce the risk for prostate cancer.”

Sigurdardòttir, L.G., et al. (2013). Sleep disruption among older men and risk of prostate cancer. Cancer Epidemiol Biomarkers Prev. 22(5):872-879.

—Dr. Bob Goldman
www.WorldHealth.net

 

Editor’s note: For the latest information and research on health and aging, subscribe to the American Academy of Anti-Aging Medicine e-zine free at WorldHealth.net.

 

Dr. Robert M. Goldman MD, PhD, DO, FAASP has spearheaded the development of numerous international medical organizations and corporations. Dr. Goldman has served as a Senior Fellow at the Lincoln Filene Center, Tufts University; as an Affiliate at the Philosophy of Education Research Center, Graduate School of Education, Harvard University, He is Clinical Consultant, Department of Obstetrics and Gynecology, Korea Medical University; and Professor, Department of Internal Medicine at the University of Central America Health Sciences, Department of Internal Medicine. Dr. Goldman holds the positions of Visiting Professor, Udayana University School of Medicine, Indonesia; Visiting Professor, Huazhong University of Science & Technology Tong Ji Medical School, China; Visiting Professor, The Wuhan Institute of Science & Technology, China; Visiting Professor at Hainan Medical College, China; and Visiting Professor, School of Anti-Aging, Aesthetics and Regenerative Medicine, UCSI University, Malaysia. Dr. Goldman is a Fellow of the American Academy of Sports Physicians and a Board Diplomat in Sports Medicine and Board Certified in Anti-Aging Medicine. Dr. Goldman is a Fellow of the American Academy of Sports Physicians and a Board Diplomat in Sports Medicine and Board Certified in Anti-Aging Medicine. He has overseen cooperative research agreement development programs in conjunction with such prominent institutions as the American National Red Cross, the US National Aeronautics and Space Administration (NASA), the Department of Defense, and the FDA’s Center for Devices & Radiological Health.

Dr Goldman was awarded the 2012 LifeTime Achievement Award in Medicine &Science. Dr. Goldman is the recipient of the ‘Gold Medal for Science, the Grand Prize for Medicine, the Humanitarian Award, and the Business Development Award. He received honors from Minister of Sports and government Health officials of numerous nations. In 2001, Excellency Juan Antonio Samaranch awarded Dr. Goldman the International Olympic Committee Tribute Diploma for contributions to the development of sport & Olympism.

In addition, Dr. Goldman is a black belt in karate, Chinese weapons expert, and world champion athlete with over 20 world strength records, he has been listed in the Guinness Book of World Records. Some of his past performance records include 13,500 consecutive situps and 321 consecutive handstand pushups. Dr. Goldman was an All-College athlete in four sports, a three time winner of the John F. Kennedy (JFK) Physical Fitness Award, was voted Athlete of the Year, was the recipient of the Champions Award, and was inducted into the World Hall of Fame of Physical Fitness. Dr. Goldman was awarded the Healthy American Fitness Leader Award from the President’s Council on Physical Fitness & Sports and U.S. Chamber of Commerce. Dr. Goldman is Chairman of the International Medical Commission overseeing sports medicine committees in over 184 nations. He has served as a Special Advisor to the President’s Council on Physical Fitness & Sports. He is founder and international President Emeritis of the National Academy of Sports Medicine and the cofounder and Chairman of the American Academy of Anti-Aging Medicine (A4M). Dr. Goldman visits an average of 20 countries annually to promote brain research and sports medicine programs.
 

Boosting Muscle Recovery With Nutrition

7210-eat1When you train intensely with weights, you’re incurring injury to your muscles. It sounds bad, but the body compensates by adding an extra layer of protection to muscles to minimize or prevent further injury—muscular hypertrophy, or growth.

Through a complex interplay involving increased muscle protein synthesis and a short-term immune response, individual muscle fibers thicken, which we recognize as growth. Even so, there is a specific process that occurs in muscle following training, and timing is an important part of it.

For example, while protein synthesis is increased up to 48 hours after intense training, the major impetus for that occurs within two hours after a workout due to heightened enzymatic and hormonal activity. Hence, the “anabolic window,” in which it’s suggested that you take in essential amino acids as soon as possible after training to fuel protein synthesis.

Before the protein-production process can go into full gear, however, the immune system must intercede. It does that via cells such as macrophages, which clear out debris left over in muscle by the imposed injury of exercise. In addition, the macrophages and other immune cells secrete cytokines, which are signaling factors that, among other functions, stimulate the activity of muscle-stem cells called satellite cells that are directly involved in the repair-and-growth process.

The immune infiltration of muscle after training produces an inflammatory effect that triggers a muscular response. A problem occurs if trainees take anti-inflammatory drugs, such as ibuprofen, too soon after training because it blocks the usual postworkout inflammation along with the growth response. In short, a temporary level of muscle inflammation following training is vital for muscle growth to occur. The key word here is temporary, since, if extended, the inflammation phase of muscle repair can, paradoxically, impede full recovery. The ideal scenario is a short period of muscle inflammation after training followed by an accelerated recovery and repair process.

Some interesting recent research shows that you can optimize the muscle-recovery process through nutrition. One way is to take in essential amino acids as soon as possible after training. Another is to eat certain foods and supplements. One study compared two sources of protein, peanuts and cod, for their ability to promote more efficient muscle repair after injury.1 Although the subjects were rats, the effects are applicable to humans.

The researchers noted that previous studies have found that the amino acid arginine seems to help heal injuries and accelerate muscle repair. The likely mechanism relates to the fact that arginine is the immediate precursor of nitric oxide synthesis in the body, and NO is an established stimulant of healing and tissue repair.

The rats were placed in groups, with one group eating the milk protein casein and peanut protein. Other rats got protein derived from cod fish. After 21 days the rats’ legs were injected with either a substance that causes muscle injury or a salt solution. The peanut protein was slightly more efficient at maintaining muscle mass than the casein, but it did not trigger any additional gains.

In contrast, the cod protein proved superior to casein in promoting muscle mass gains and healing injured muscle quickly. More important, the cod protein proved most efficient in curtailing excessive inflammation in the muscle by modifying the immune cells’ activity. That helped significantly boost muscle recovery in the rats better than the combined peanut and casein proteins.

The peanut protein didn’t trigger muscle growth because of its relative lack of essential amino acids, especially when compared to cod. Excess inflammation delays muscle healing because the immune cells release large amounts of free radicals. While that is normally efficient for killing invading bacteria, when excessively released in damaged muscle, free radicals increase the damage by attacking muscle cell membranes, leading to the death of the muscle cell. Cod intercedes by speeding the clearing out of immune cells, which lowers inflammation and allows full muscle recovery to proceed.

The cod also proved superior to casein by 11 percent in promoting muscle fiber size. That was thought to be due to the reduction of inflammatory cytokines discussed above. While recent studies show that fish oil can both reduce excess muscle breakdown and help promote muscle protein synthesis, fish oil didn’t play a role in this study, as the oil had all been removed from the cod used. So what does explain the beneficial effects of cod that it shows?

The authors suggest two possible mechanisms. The first involves an upgrade in the activity of insulinlike growth factor 1 in the rats’ muscle triggered by their eating cod. IGF-1 in muscle is a major factor in muscle repair and growth after injury and exercise. Other studies have shown that when rats are fed casein or soy but also allowed to eat high-fat diets, the IGF-1 repair system is impaired. The lack of fat in the cod may have served to maximize the IGF-1 activity.

The other mechanism suggested by the researchers was that cod is rich in the amino acids arginine, glycine and taurine, all of which are potent natural anti-inflammatory compounds. Arginine, by enhancing nitric oxide release, would speed healing of wounds and reduce inflammatory cell accumulation. Glycine also provides anti-inflammatory activity in muscle by reducing the inflammatory cytokines released by immune cells. Taurine helps by acting as an antioxidant in muscle, which reduces free radical–induced damage to muscle cells and prevents their premature destruction. Cod’s high content of essential amino acids also encourages more muscle protein synthesis along with less muscle breakdown.

Another study, also involving rats, tested the effects of grape-seed extract on muscle recovery.2 The rats’ gastrocnemius muscles were purposely injured, with only some of the rats getting grape-seed extract two weeks prior to being injured.

The results showed that rats given the grape-seed extract had less immune cell infiltration in the injured muscle plus a shorter release time of inflammatory cytokines. Muscle fiber regeneration began earlier in the grape-seed-extract rats and was completed more rapidly. The injured muscles healed more rapidly because the grape-seen extract, by decreasing the excess inflammation, boosted the activity of muscle satellite repair cells.

Finally, those who want to recover more rapidly from intense training should take the advice of their mothers: Eat more greens. The wisdom of those words was shown in a recent study in which 10 healthy men, average age 23, ate 85 grams of watercress, a leafy green vegetable, for eight weeks prior to engaging in intense treadmill exercise.3 As a control, the men also didn’t eat the watercress during a different eight-week period.

The results showed that the subjects who exercised intensely but didn’t eat the watercress had more DNA cell damage than those who got the watercress. Some of the men didn’t eat watercress for eight weeks but ate it only two hours prior to the exercise—and they showed the same level of protection against DNA damage. So the protective effect of eating watercress, which is likely the result of natural antioxidants found in it, isn’t accumulative but works immediately. —Jerry Brainum

 

Editor’s note: Have you been ripped off by supplement makers whose products don’t work as advertised? Want to know the truth about them? Check out Natural Anabolics, available at JerryBrainum.com.

 

1 Dort, J., et al. (2012). Beneficial effects of cod protein on skeletal muscle repair following injury. Appl Physiol Nutr. 37:489-98.

2 Myburgh, K.H., et al. (2012). Accelerated skeletal muscle recovery after in vivo polyphenol administration. Nutr Biochem. 23(9):1072–1079.

3 Fogarty, M.C., et al. (2013). Acute and chronic watercress supplementation attenuates exercise-induced peripheral mononuclear cell DNA damage and lipid peroxidation. Br J Nut. 9(2):293-301.

Muscle Growth and Estrogen

7208-anabolicEstrogen is often called a “female hormone,” which is a misnomer, as this steroid hormone is also produced in the male body. It’s also true that women produce far greater amounts of estrogen than men, just as men produce about 10 times more testosterone than women.

Men’s greater testosterone levels are often cited as the reason that they are able to build more muscle than women. Recent studies, however, show that despite the negligible amounts of testosterone they produce while weight training, women are able to make similar muscle gains to men’s. That relates more to the fact that anabolic hormones produced during exercise don’t have as great an effect on muscle growth as was previously realized. Think about that the next time you read an article about the best ways to boost anabolic hormones during training.

If men’s bodies produce estrogen, what is the purpose? After all, nature is not known to be profligate in its actions; everything it does, it does for a reason. Although the precise functions of estrogen in men aren’t entirely clear, it appears to play a role in the maturation and development of sperm, which means that estrogen may effect male fertility.

Estrogen is vital to bone development in women, and a lack of it in older women often results in osteoporosis, a bone-thinning disease. Some scientists suggest that estrogen may play a similar role in men. Men deficient in testosterone are also subject to osteoporosis, although it’s not as common in men as in women, and when it does occur, it usually strikes in the spine.

Men are often advised not to take supplements or drugs that lower estrogen for extended times because of possible adverse affects on the cardiovascular system. That’s based on the established cardiovascular protection offered by estrogen to women. Younger women rarely suffer from heart attacks or strokes, and the reason is attributed to their higher estrogen levels. Estrogen offers cardiovascular protection in several ways. For one thing, it aides the synthesis and release of nitric oxide.

NO maintains vascular flexibility, which is important because stiff blood vessels are linked to atherosclerosis and high blood pressure. Estrogen also acts as a potent antioxidant, preventing the oxidation of low-density-lipoprotein cholesterol, which is the cornerstone of cardiovascular disease. At the same time, estrogen boosts levels of protective high-density-lipoprotein cholesterol. It is no coincidence that cardiovascular disease is higher in older women, who produce less estrogen.

On the other hand, according to a preliminary study released at the annual meeting of the Heart Rhythm Society in May 2013, having elevated blood estrogen is related to sudden cardiac death in both men and women. Sudden cardiac death occurs when the heart suddenly stops beating, known as cardiac arrest. Each year, more than 350,000 people in the United States die this way.

The study looked at people in Portland, Oregon, who either had died from sudden cardiac death or had suffered coronary artery disease. Tests done of the subject’s blood plasma at the time of death showed a similar proportion of the usual cardiovascular risk factors, such as high blood pressure, elevated cholesterol, obesity and diabetes, but the men had lowered testosterone along with elevated estrogen. In women, both testosterone and estrogen were elevated.

Those who died from sudden cardiac death showed higher estrogen levels than those who didn’t die but had coronary artery disease. Both the man and women who died showed elevated estrogen. Although this research doesn’t prove a cause-and-effect association between sudden cardiac death and elevated estrogen, it does suggest that estrogen, when elevated, produces a paradoxical reverse effect—a negative effect on heart function.

Estrogen is a dirty word to bodybuilders. The hormone is associated with greater amounts of muscle-definition-obscuring subcutaneous bodyfat and water retention. Male bodybuilders who use certain anabolic steroids that convert into estrogen can acquire a female-type breast development called gynecomastia. To prevent that and other estrogen-related effects, they often resort to using drugs that either interfere with estrogen, locking onto cellular receptors, like Nolvadex, or drugs that inhibit the enzymes that convert androgens into estrogen, known as aromatase blockers. Some bodybuilders are so fearful of estrogen that they stay on these anti-estrogen drugs year-round, believing that they are benign.

Many bodybuilders aren’t aware of the important role that estrogen plays in training and muscle growth. Women show less muscle damage when they exercise, an effect attributed to estrogen, which acts as an anti-inflammatory during exercise. Women also burn greater amounts of fat when they exercise than men, although it isn’t as apparent simply because most women have higher bodyfat levels than men. The reason is that women secrete greater amounts of growth hormone, which mobilizes fat. On the other hand, women also don’t respond to techniques such as carbohydrate loading, also thought to be due to their higher estrogen.

For years bodybuilders have been told that you need a certain amount of estrogen to maintain androgen cell receptors, which interact with testosterone to produce anabolic effects in muscle. Recent studies, however, show that estrogens may play an even more direct role in muscle hypertrophy, or growth. A 2012 study with rats explains why.1

There are two types of estrogen cell receptors (some suggest there are three), estrogen receptor-A and estrogen receptor-B. ER-A is predominant in reproductive organs, such as the uterus and breasts, but is also found in the heart, liver and kidneys, as well as the prostate gland. ER-B is found in the vascular lining, where it boosts NO, and gastrointestinal tract. Both receptors exist in the skeletal muscle of both sexes, but they have differing effects. For example, stimulation of ER-A by estrogen promotes changes in the prostate gland that are linked to prostate cancer (ironically, it is more potent than testosterone in that effect), but activation of ER-B in the prostate blocks the negative effects of ER-A, thereby helping prevent prostate cancer. Natural substances that activate ER-B, but not ER-A, such as genistein from soy, can offer some protection against it as well.

In the recent study, rats whose ovaries had been removed (so no estrogen is produced) were paired with other rats that were selectively bred not to have either ER-B or ER-A estrogen receptors. All the rats were then purposely injured with a substance that attacks muscle. Some of the rats without ovaries were also given genistein from soy and synthetic chemicals that selectively interact with either ER-B or ER-A receptors. Other of the rats without ovaries didn’t get those substances but did receive the muscle toxin. As expected, the latter rats showed greater amounts of substances linked to muscle injury, but those given the estrogen-stimulating compounds got some protection, including lesser amounts of muscle damage enzymes and reduced levels of inflammatory chemicals linked to muscle injury.

One such particular chemical, called tissue necrosis-factor-A is associated with catabolic effects in muscle and rises with age in humans. Some suggest that TNF-A is the primary arbiter of muscle loss with age, known as sarcopenia. Treatments with estrogen itself and the substance that specifically interacts with ER-B led to increases in myogenic substances aid the activity of satellite cells, the muscle stem cells that are involved in muscle repair and growth. As such, activating ER-B selectively appears to encourage muscle growth.

The researchers also tested the effects of estrogen on muscle growth in male rats. Once again, specific stimulation of ER-B, but not ER-A, triggered muscle growth in the males. It was traced to a strong induction of intramuscular IGF-1, long known to promote satellite cell activity in muscle and considered the primary anabolic hormone produced during exercise that stimulates muscle growth. The authors noted that this estrogen-related effect worked in tandem with testosterone, acting as an additive to testosterone in stimulating muscle growth. That confirms previous findings that estrogen is involved in promoting the activity of intramuscular IGF-1, and it may explain why women show less damage after exercise to men.

This animal-based study shows that selective activation of ER-B is involved in muscle growth—promoting less inflammation while boosting anti-inflammatory mechanisms that speed muscle recuperation after injury, including the injury associated with intense exercise. Activation of ER-B also boosts satellite cell activation and increases the effect of testosterone in that area as well. The question is how to use this information in your workouts and diet.

First, understand that this is an animal study, so it may not be completely replicable in humans. Even so, all the aspects studied do also occur in human muscle, so it is likely that the effects do apply to human physiology. Second, the fact that estrogen appears to be vital for muscle repair and regeneration calls into question overenthusiastic efforts to lower perceived high estrogen levels in men. Taking estrogen too low—as would occur with estrogen-lowering drugs or chronic use of supplements touted to lower estrogen—would be working against yourself in terms of muscle gains.

The best natural way to control elevated estrogen is to keep your bodyfat low. Higher bodyfat means greater activity of aromatase, the enzyme that converts androgens into estrogen. Another way to control estrogen safely is to eat generous amounts of cruciferous vegetables, such as broccoli, brussels sprouts, cabbage and kale, among others. Eating those foods converts the dangerous form of estrogen to a form that is benign, but you still get the benefits of estrogen for health and muscle growth. Consuming soy is a bit of a slippery slope, since it involves a U-shaped curve. Too much can interfere with testosterone and produce an estrogenic effect in men, but small-to-moderate amounts do no harm, and as noted, genistein, an isoflavone found in soy, is a specific activator of the ER-B receptors associated with promoting muscle growth and repair. About 25 grams a day of soy protein would be sufficient.

Editor’s note: Jerry Brainum has been an exercise and nutrition researcher and journalist for more than 25 years. He’s worked with pro bodybuilders as well as many Olympic and professional athletes. To get his new e-book, Natural Anabolics—Nutrients, Compounds and Supplements That Can Accelerate Muscle Growth Without Drugs, visit www.JerryBrainum.com.   IM

 

1 Velders, M., et al. (2012). Selective estrogen receptor-B activation stimulates skeletal muscle growth and regeneration. FASEB J. 26;1909-1920.

Inject to Grow?

7209-injectgrowThe primary purpose of using anabolic drugs, such as testosterone, steroids and growth hormone, is to trigger added muscle beyond what is attainable naturally with training and diet. Of course, athletes who use anabolic drugs also train intensely and go on diets to change body composition, frequently to lose fat. Using anabolic drugs under dieting conditions, where calories are often cut back severely, can spare muscle that might otherwise be broken down; however, the drugs also promote muscularity that is beyond genetic limits. The situation is clearly apparent when athletes get off the drugs. Their newly acquired muscle bulk often seems to melt away with each passing week.

For some athletes the added size they get with drug use isn’t enough. Because of fierce competition, they want to dwarf their competitors, literally, so they resort to techniques that temporarily—or not so temporarily—boost muscle size beyond even what can be produced with any drug. The genesis of  “local site enhancement,” as it’s known, probably began in the early 1980s, when some bodybuilders began injecting themselves with a mediocre anabolic steroid drug called Esiclene, generic name formebolone. Compared to other anabolic steroids, Esiclene didn’t produce the often dramatic size effects, but it did have one property that made it attractive to competitors. It tended to produce a localized inflammation of muscle that lasted about a week.

Experience soon showed that Esiclene use was best for smaller muscle groups, such as the biceps, deltoids and particularly the calves. The localized inflammation induced by Esiclene often boosted muscle size by one to 1 1/2 inches after a few days. In larger muscle areas, such as the chest, back, and legs, however, it tended to produce a lumpy effect that looked like tumors. It was also said to make the muscle look harder. Likely many contests have been won by competitors who gained a last-minute edge by using Esiclene.

Esiclene became increasingly hard to get over the years, however, and is no longer made or sold at all, even on the black market. The notion of producing overnight gains in mass was for many too attractive to pass up, and so, in the early ’90s German bodybuilder Chris Clark devised a concoction that he called “Pump & Pose.” It was often advertised as a “posing oil,” but its real purpose was to act just like Esiclene, boosting muscle mass quickly. The more common name was synthol, and it consisted of 85 percent oil, usually medium-chain triglycerides; 7.5 percent lidocaine, a local anesthetic, to blunt the pain of injection (Escilene also contained lidocaine for the same reason); and 7.5 percent alcohol to keep the solution sterile. The notion of injecting oil into the body for cosmetic purposes wasn’t new. Back in 1899 some folks were injecting paraffin, a type of oil, into bodyparts that appeared deformed. Oddly enough, it soon became apparent that many of those who used synthol produced deformities.

Since the development of Pump & Pose, a number of other brands have been introduced, including Syntherol, Esik Clean, Nuclear Nutrition Site Enhancement Oil, Cosmostan and Liquid Muscle. They all are expensive, so many resort to using sterilized sesame or walnut oil injected directly into muscle. In reality, many injectable anabolic steroid drugs contain sesame oil as an injection vehicle.

The idea behind these “site enhancers” involves stretching the connective-tissue sheath that surrounds muscle tissue. This fascia, as it is called, is thought to be a major impediment to maximum muscle growth, so stretching by regular injections of oil would “make room” for additional muscle growth. The typical application protocols involve frequent injections of one to two milliliters daily in various locations within the target muscles for either several weeks or up to six months or more. Injecting into distinct areas of muscle and then massaging the areas afterward are thought to produce a more natural look and prevent the development of scar tissue. The body tends to produce scar tissue around anything that is put into it that it views as foreign. That includes breast implants. Popular areas for injection include triceps, biceps, delts and calves.

In truth, it’s often painfully obvious when athletes have used synthol or other oil injections in a bodybuilding contest because they have unnatural-appearing lumps on their muscles. When the calves are involved, it’s comically obvious. More insidious is the possible damage to long-term health that can come from oil-based site injections. While 30 percent of the oil is immediately metabolized, most of it forms cysts in muscle that can last three to five years or longer. That makes the oil injections far different from Escilene, which produced a local inflammation that lasted only a few days.

Injecting oil directly into muscle can produce some serious side effects, which include a pulmonary embolism if the fat injection is wrongly injected directly into a blood vessel. The fat becomes an embolism and travels in the blood to the lungs. One elite pro bodybuilder nearly died a few years ago after his girlfriend injected him with synthol and mistakenly shot it directly into a blood vessel. Luckily, he survived. Other possible side effects of synthol include nerve damage if it’s injected into a nerve, infections and strokes. A few published case studies of bodybuilders who have used synthol have documented oil-filled granulomas, or nodules, in their muscles. Others have shown ulcers and cysts. Some who may be allergic to sesame oil get an allergic reaction involving an inflammation of blood vessels. Overenthusiastic use frequently results in a muscle appearing droopy or deformed.

Not many cases of problems involving site-enhancement injections have been published in the medical literature. Those that have often involve injection of straight oil, such as sesame or walnut oil, and subsequent infection and formation of oil and fat cysts. By far the most serious case of problems experienced after an oil injection was published recently.1

A 40-year-old man described as a “semiprofessional bodybuilder” showed up at a hospital complaining of multiple painful swellings, redness and elevated temperature in his right upper arm that had begun two months earlier. The swelling had increased over time. He felt so sick that he hadn’t trained in more than two months. A previous medical exam had left him with the incorrect diagnosis of “ruptured muscle fibers.” The doctors told him to rest and take anti-inflammatory drugs, which didn’t help. The man had injected himself with sesame oil  for eight years, until four months before his trip to the hospital. He’d injected two milliliters of sesame oil at 20 intramuscular locations, which resulted in an upper arm measuring 27 1/2 inches!

An MRI revealed more than 100 intramuscular and subcutaneous cysts of up to seven millimeters each, with no sign of obvious infection, in his left-upper arm, both shoulders, both legs and chest. Those happened to be the most frequently used areas of his site injections over the years. His right brachialis showed that the muscle mass was completely obliterated, replaced by oil cysts. The entire right biceps and the long and lateral heads of his triceps had been replaced by scar tissue, and the tissue was vastly swollen. The only muscle left in his arm was the medial head of the triceps, and that also contained oil cysts and scar tissue. Since he appeared to have an infection in his arm, he underwent surgery to remove the infected tissue. Sure enough, his muscle was infiltrated with pockets of pus and abscesses. When the oil he used was analyzed, it showed no traces of bacteria or fungi. His muscle loss was so extensive that it was considered irreversible.

A year later the bodybuilder was still suffering pain great enough to prevent him from training. Interestingly, the loss of muscle was most extensive in the areas he had either not injected or had injected lightly. Still, he had lost no size on his arms since the surgery. After three years he continued to suffer from pain and weakness but did some training. More than 90 percent of his upper-arm muscle had been replaced by oil cysts and scar tissue. The ongoing inflammation in his arm may have set him up for future cancer, as cancer is associated with chronic inflammation.

In his effort to attain superhuman muscle size, this bodybuilder literally destroyed his muscles, and the effect was not reversible. It’s obvious that the notion of injecting oil into muscle is just idiotic, and those who do so may pay dearly for it.

Editor’s note: Jerry Brainum has been an exercise and nutrition researcher and journalist for more than 25 years. He’s worked with pro bodybuilders as well as many Olympic and professional athletes. To get his new e-book, Natural Anabolics—Nutrients, Compounds and Supplements That Can Accelerate Muscle Growth Without Drugs, visit www.JerryBrainum.com.   IM

 

1 Banke, I.J., et al. (2012). Irreversible muscle damage in bodybuilding due to long-term intramuscular oil injection.Int J Sports Med. In press.

Meat, Carnitine and Heart Disease

7208-eat1A study released in April 2013 implicated beef as a primary cause of cardiovascular disease.1 What was surprising about the study, which was published in the journal Nature Medicine, was that the alleged reason for this risk factor wasn’t the fat or cholesterol content of the meat but rather its carnitine content.

Carnitine is an amino acid product familiar to most bodybuilders for its use in supplements, where it’s often touted as a fat burner. That’s based on the primary function of carnitine, which is to shuttle fatty acids into the mitochondrial portion of cells, where the fat is oxidized. Carnitine is essential for this process and is made in the liver and kidneys from the amino acids lysine and methionine, with the assistance of vitamins C, B6 and niacin and the mineral iron. How can an essential nutrient such as carnitine cause cardiovascular disease?

In fact, it isn’t carnitine itself that is the alleged culprit but a breakdown product of carnitine called trimethylamine-oxide. TMAO is produced from trimethylamine, which is degraded into TMAO through the actions of specific intestinal bacteria. According to the new study, that increase in TMAO leads to increased cholesterol being deposited in arterial linings, which can lead to cardiovascular disease, including heart attacks and strokes.

The biochemical basis of those findings regarding TMAO conversion was that it occurred in lab mice and did accelerate the progression of cardiovascular disease in the animals. The problem, however, is that the type of bacteria that converted TMA into TMAO in the mice doesn’t exist in humans. The authors conjecture that eating beef habitually does boost the intestinal content of this type of bacteria, but they offer only indirect proof. The bacteria doesn’t exist in vegetarians, so they directed one vegetarian to eat a 12-ounce serving of beef and also take a carnitine supplement. Even so, the vegetarian showed no increased production of TMAO, and that was the primary basis of their assertion that beef causes changes in intestinal bacteria that favor the buildup of the type of bacteria that readily converts TMA into TMAO. Even in the mice that did have the dangerous bacteria, the production of TMAO from carnitine was completely suppressed when the rodents were given an antibiotic before eating beef.

Initially, this study appears alarming for those who eat beef—until you consider a few other facts. For one thing, numerous studies have shown that carnitine exerts a beneficial effect on cardiovascular disease, which isn’t hard to understand when you consider that the heart’s preferred fuel is fat, not sugar, and carnitine allows the heart to use fat more effectively. For that reason, carnitine is suggested as an effective treatment for various heart ailments, including congestive heart failure, characterized by a failing heart muscle unable to produce sufficient adenosine triphosphate, or ATP, the body’s primary elemental energy source.

Indeed, less than two weeks after the Nature Medicine study was released, another study appeared in the Mayo Clinic Proceedings which found that carnitine significantly improves patient outcomes following a heart attack.2 The review looked at 13 controlled studies involving 3,629 patients who took L-carnitine and found the following:

1) A 27 percent reduction in all-cause mortality

2) A 65 percent reduction in heart rhythm disturbances, a common cause of heart attacks

3) A 40 percent reduction in the development of angina, or “heart pain.”

4) A significant reduction in the size of infarcted tissue in the heart, meaning heart tissue that has been destroyed during heart attacks. Carnitine helps the heart because it not only aides the use of fat more efficiently but also boosts mitochondrial function, which boosts the output of ATP, and that protects heart cells from dying.

From a bodybuilding standpoint, carnitine provides many benefits. Although its fat oxidation effect is questionable (because supplemental carnitine tends to increase carnitine mainly in the blood rather than in muscle, where fat is oxidized), with some studies showing definite effects and other none, other benefits are more apparent. That includes an upgrade in cell androgen receptors, which boosts testosterone availability to cells.

A recent study showed that carnitine (although in massive amounts) also blunts catabolic effects in muscle through blocking catabolic pathways and increasing the anabolic hormone IGF-13.

Other studies show that carnitine increases work efficiency by an average of 11 percent, accomplishing that through lowered glycogen use and decreased lactate production in muscle during exercise. Carnitine also boosts nitric oxide by an average of 18 percent, far more than any “NO-boosting” supplement on the market. That, however, involves a specific form of carnitine, propionyl-L-carnitine, which has been used in Europe for years as a heart medication.

Thus, the theory that carnitine—and by extension, red meat—are dangerous seems to be based on flimsy evidence, and the evidence to the contrary is quite robust. So eat your meat, put on muscle, and relax! —Jerry Brainum

 

Editor’s note: Have you been ripped off by supplement makers whose products don’t work as advertised? Want to know the truth about them? Check out Natural Anabolics, available at JerryBrainum.com.

1 Koeth, R.A., et al. (2013). Intestinal microbiota metabolism of L-carnitine, a nutrient in red meat, promotes atherosclerosis. Nature Medicine. 19(5):576-85.

2 Dinicolantonio, J.J., et al. (2013). L-carnitine in the prevention of cardiovascular disease: Systemic review and metanalysis. Mayo Clinic Proceedings. 88.

3 Keller, J., et al. (2013). Supplementation of carnitine leads to an activation of the IGF-1/P13K/Akt signalling pathway and downregulates the E3 MuRF1 in skeletal muscle of rats. Nut Metabol. 10:28.

 

Commentary by Dr. Steven Zeisel

Dr. Hazen and colleagues have published a series of three papers suggesting that choline and carnitine are precursors of trimethylamine oxide formation. In a special mouse model, where the animals have been genetically modified to have very high cholesterol and develop atherosclerosis, Hazen finds that administration of TMAO is sufficient to increase heart disease in the mice. That’s the most interesting piece of data and indicates that additional research should be conducted on TMAO.

The other data presented in the three papers is more problematic. All of the human population data presented by Hazen shows that people with heart disease have a slightly higher blood concentrations of TMAO than people who don’t have heart disease. That’s an association and is not evidence of causality. If you examine the data carefully, you can see that people with heart disease have bad kidney function. Atherosclerosis is also damaging to the kidneys, which excrete TMAO. Thus, TMAO could be higher just because kidney function is lower. That would make it a marker of kidney function and not the cause of heart disease.

In the mouse studies giving the animals choline, in the presence of gut microbes, forms TMA, which in the liver is converted to TMAO. That has been known for decades. The bacteria colonize all the way up to the stomach in the mice, but in humans there are very few bacteria above the large intestine. Choline is absorbed in the small intestine—so in humans only large doses actually reach the bacteria in the small intestine. We knew that because patients treated with very large doses of choline smell fishy, which is the odor of TMA. In the mice bacteria easily get to choline; in humans choline should be absorbed before bacteria can get to it.

Regarding carnitine, the Hazen paper researchers had to give a large amount of meat to humans to see TMAO formed. Likely that amount was large enough that the meat was not fully digested before reaching the bacteria in the large intestine. Note that carnitine treatment generated much less TMAO. In the study where eggs were administered, there was no statistically significant bump in TMAO after two eggs. When labelled phosphatidylcholine was administered, there was an increase in labeled TMAO at six hours after the meal. That is likely the small portion of label that got to the large intestine, and the amount of TMAO formed was tiny.

So, while it is an intriguing theory, the supporting data are very preliminary and confounded. People should not overdose on choline or carnitine, but they should realize that these are needed nutrients, and that deficiency in them has serious consequences. Eat a diet of normal foods, and don’t worry.

 

Steven Zeisel M.D., Ph.D.
Professor of Nutrition
Nutrition Research Institute
University of North Carolina at Chapel Hill

How Much Protein Do You Need Per Meal?

7207-eat7What’s the magic number? Twenty grams? Forty grams? How much protein should you get per meal? The dirty little answer to that is, we honestly don’t know. Not yet anyway.

Clearly, your bodyweight and training goals will affect what your feeding strategy should be. A 400-pound sumo wrestler obviously has greater macronutrient needs than a 100-pound ballet dancer.

A group of scientists recently examined the effect of one of my favorite protein foods—beef. We’ve seen the data on whey, casein, soy and even egg protein. It’s about time we got to the meat of the matter, no pun intended. The researchers examined the dose-response of muscle protein synthesis, with and without weight-training exercises, to graded servings of beef. Thirty-five middle-aged men, average age 59, ate either 0 grams, 57 grams (two ounces, 12 grams of protein), 113 grams (four ounces, 24 grams of protein), or 170 grams (six ounces, 36 grams protein) of ground beef—15 percent fat. They then performed a bout of unilateral resistance exercise to allow measurement of the fed state and the fed-plus-resistance-exercise state for each serving.

Without getting into the complex biochemistry involved, the researchers determined how each amount of beef protein affected muscle protein synthesis. They discovered that protein synthesis was increased with the 170-gram serving of beef—six ounces—to a greater extent than all other doses at rest and after resistance exercise. Furthermore, an isolated bout of weight-training exercise was potent in stimulating muscle protein synthesis and acted additively with feeding.1

So what does the study tell us? First of all, it confirms other studies showing that getting a protein meal after training is good for encouraging muscle protein gains. Second, it tells us that at least in middle-aged men, muscle protein synthesis keeps rising even at the 36-gram dose.

Many have theorized that all we need is a mere 20 grams of protein per meal to maximize protein synthesis. Clearly, that isn’t the case. Though it would be interesting to see what happens in the younger generation, the 18-to-40-year-olds.

On the flip side, it would be intriguing to see if beef protein supplementation had a different effect from, say, whey and casein supplementation postworkout. Once you reach a certain protein consumption level—for example,  40 grams per meal—does it matter if the protein comes from whey, casein, egg or beef? Or even soy?

I would surmise that at lower protein-consumption levels, like a protein-bar snack of 20 grams, the quality of the protein may be more critical. But at higher levels, like 40 grams, it may not matter all that much—assuming your primary goal is triggering muscle protein gain.

The bottom line: I’d suggest getting 40 grams of protein postworkout if your goal is to maximize muscle protein synthesis.

—Jose Antonio, Ph.D.

 

Editor’s note: Jose Antonio, Ph.D., is an assistant professor at Nova Southeastern University in sunny South Florida.

 

1 Robinson, M.J. et al. (2013). Dose-dependent responses of myofibrillar protein synthesis with beef ingestion are enhanced with resistance exercise in middle-aged men. Applied Physiology, Nutrition, and Metabolism (Physiologie Appliquee, Nutrition et Metabolisme). 38:120-125. doi:10.1139/apnm-2012-0092.

 

Nutrients That Can Increase GH

7206-anabolicHuman growth hormone is considered one of the three major anabolic hormones in the body, with the other two being testosterone and insulin. GH is of special interest to bodybuilders and athletes for several reasons.

The first is its reputed anabolic property. GH aids in nitrogen retention and also helps to transport animo acids into muscle for use in muscle protein synthesis.GH has also engendered a reputation for speeding bodyfat loss, since it promotes the sparing of carbohydrates, while at the same time fostering the use of stored fat as an energy source.

Over the years it has become apparent that GH is not as anabolic in actual practice as it appears to be on paper. In fact, most studies suggest that GH doesn’t offer any anabolic benefits to healthy young athletes who are still able to secrete GH at a normal rate. Conversely, GH production drops by 15 percent for each decade of life past age 30, and many older people show unmistakable GH deficiencies. When they’re given supplemental GH injections, they respond by making definite gains in muscle mass, along with a significant reduction in bodyfat stores.

The fact that GH may not be as anabolic in younger people as was originally thought hasn’t lowered its popularity among athletes and bodybuilders, many of whom have added insulin to their anabolic regimens. While the primary purpose of insulin is to treat diabetes, it also has some anabolic effects. In relation to muscle, it exerts mainly a permissive effect in that it prevents excessive muscle breakdown while promoting amino acid uptake into muscle. Some studies show that insulin can convert from being mainly anticatabolic in muscle to anabolic if a large amount of amino acids are also present.

Bodybuilders use insulin because it appears to be synergistic when combined with anabolic steroids and GH. A major side effect of GH is hyperglycemia, or elevated blood glucose. It’s tempered by simultaneous use of insulin, which also adds to the GH’s anticatabolic effect.

Let’s face it: Using drug forms of insulin and GH, as well as anabolic steroids, is not without risk. One obvious effect of this drug triumvirate is an enlarged, or bloated, abdomen. In recent years the odd appearance of some professional bodybuilders, who display both deep abdominal muscle definition and, when they’re not flexed, bloated abdomens, has been blamed on the combination of insulin and GH. Many other side effects are possible, depending how much and how long the drugs are used.

Natural bodybuilders, in their efforts to add muscle and lose bodyfat, look for ways to boost their various anabolic hormones without taking drugs. The most potent nutrients known to boost GH are amino acids, with arginine and ornithine leading the way, although several others can also do it to a lesser degree. Testing of the branched-chain amino acids showed that leucine and valine boosted GH by 10 percent, but the third BCAA, isoleucine, had no effect.

The idea of using arginine as a GH-booster is controversial, since most studies show that the usual oral dose for that purpose is not effective. Arginine is effective when administered intravenously—at doses of 30 grams. In fact, that route is so effective, it’s often used as a test to determine whether patients are deficient in GH. Giving intravenous arginine leads to an average 800 to 2,200 percent increase in GH above baseline, or resting, levels.

The I.V. route works because of not only the greater arginine uptake but also the insulin that’s secreted due to the presence of that much arginine. The lowered blood glucose that results leads to the GH release, as GH opposes low blood glucose. Attempting to take 30 grams of arginine orally would lead to rapid nausea and likely vomiting. Arginase enzymes located in the liver and intestine would degrade most of the ingested high-dose arginine, so you would be left nauseated but without a significant GH release.

Ornithine is a metabolite of arginine that plays a major role in helping the body produce urea, the major nitrogen waste product of protein metabolism. That’s an important function, since without significant urea production, ammonia would build up in the body, leading to toxic consequences. Ornithine is said to be about twice as effective as arginine in stimulating a GH release, although that isn’t saying much when you consider that oral arginine is not too effective for that purpose. As with arginine, the studies that have examined ornithine’s GH-releasing effects have shown mixed results. One study did turn up a significant GH effect from ornithine with an oral dose of 170 milligrams per kilogram of bodyweight, but the dose led to gastrointestinal distress in more than half of the subjects. Both arginine and ornithine taste awful, so that may have played a role.

Some have suggested that experienced bodybuilders who train intensely have already reached their maximum GH release, so using a supplement purported to boost it would be like trying to add more water to a glass filled with water. A recent study seemed to confirm that.1 Ten young men, average age 22, who had never lifted weights got either 0.1 grams of ornithine per kilogram of bodyweight or a placebo. Their blood was drawn and tested for GH both before and after they performed biceps curls using a weight equal to 60 percent of maximum, which is fairly light.

Although ornithine is said to peak in the blood within an hour, the subjects in this study had high blood levels—500 percent above baseline-—two hours after they took it. Those using the ornithine also had GH levels that were 200 percent higher than the placebo group 30 minutes after exercise. Again, however, most published studies of experienced trainees show little or no response from oral supplementation with amino acids, unless they’re taking large doses, which often leads to extreme nausea. It may be similar to what occurs with other supplements, such as HMB, amino acids like ornithine and arginine—it may work more effectively for beginners than advanced trainees.

Another recent study examined whether other nutrients besides aminos can affect GH release.2 It featured a two-part design. The first involved 108 men and women, while the second used 12 men. Both groups initially were tested to determine basal, or resting, GH, as well as body responses. The ages of the subjects in the first part ranged from 18 to 55, while those in the second part ranged from 18 to 60.

Part one found several nutrient associations with GH release, including vitamin C, dietary fiber and two saturated fatty acids. All appeared to promote GH release. Substances that blocked GH included dietary cholesterol and trans fats. Vitamins D and E and omega-3 fatty acids were not associated with peak GH release. All other carbs, amino acids and fatty acids were also not linked to GH release. Low levels of insulinlike growth factor 1, which is a product of GH, were linked to age and bodyfat but higher levels were associated with dietary fiber intake. No other nutrients were shown to affect IGF-1, although higher levels are associated with protein intake.

In the second part of the study that featured 12 men, one type of saturated fatty acid decreased the amount of time GH existed in the blood while another seemed to interfere with nighttime release of GH, which normally peaks at night. The one nutrient that showed the greatest relationship to GH release was vitamin C. The question is why.

Vitamin C is well-known as an antioxidant, but it also works with various enzymes in the body. One example is that vitamin C is required as a co-factor for enzymes that synthesize L-carnitine from amino acids in the body. Vitamin C also plays an important role in the production of collagen, a primary protein in connective tissue. In relation to GH, vitamin C acts as a co-factor in the activity of an enzyme called peptidylglycine alpha-amidating monooxygenase, or PAM, which activates various neuropeptides, or brain proteins.

It  turns out that PAM exists in great amounts in both the hypothalamus of the brain, where growth-hormone-releasing hormone is produced, and the pituitary gland, where GH is produced. The thought is that vitamin C, through its actions on PAM, activates growth-hormone-releasing hormone from the hypothalamus, which then triggers the release of GH from the pituitary gland.

So should you take in massive doses of vitamin C to promote GH release? That would not be feasible, since blood levels of C peak after an oral dose of only 200 milligrams. Although the Recommended Dietary Allowance of vitamin C is 75 milligrams a day for women and 90 milligrams for men, in this study 44 percent of the 108 part-one subjects did not meet even those levels. The thing to keep in mind about these findings regarding vitamin C and GH release is that it optimizes normal release of GH.

Editor’s note: Jerry Brainum has been an exercise and nutrition researcher and journalist for more than 25 years. He’s worked with pro bodybuilders as well as many Olympic and professional athletes. To get his new e-book, Natural Anabolics—Nutrients, Compounds and Supplements That Can Accelerate Muscle Growth Without Drugs, visit www.JerryBrainum.com.   IM

  1 Demura, S., et al. (2010). The effect of L-ornithine hydrochloride ingestion on human growth hormone secretion after strength training. Adv Biosci Biotechno.1:7-11.

2 Denny-Brown, S., et al. (2012). The association of macro and micronutrient intake with growth hormone secretion.Growth Hormone and IGF Res. 22(3-4):102-7.

DHEA Fights Painful Muscle Soreness

7205-eat6Yeah, DHEA, a.k.a. dehydroepiandrosterone, is the most abundant steroid hormone in the body. Most would say that it’s good just for old people. Well, think again.

A recent study looked at the role of DHEA in aerobic and weight training.1 In a double-blind, placebo-controlled experiment, 16 young men, 19 years old, received either a flour-capsule placebo or 100 milligrams per day of DHEA during five days of successive exercise. Oral DHEA supplementation significantly increased circulating DHEA-S by 2.5-fold, but a 35 percent drop was observed from day 3 during training.

If you’re wondering what the difference is between DHEA and DHEA-S, the S stands for an extra sulfate molecule attached. Most of the DHEA in your body occurs in the DHEA-S form. The researchers observed only a minimal DHEA-S reduction of 17 percent in the placebo group, but what was most interesting was the effect on muscle soreness.

Soreness was elevated significantly on day 2 for both groups, but on days 3 and 6 there was less in the DHEA-supplemented group. Creatine kinase, a blood marker of muscle damage, was much higher in the placebo group as well. Thus, DHEA-S protects skeletal muscle from training-induced damage in young exercising men.

In another very intriguing study, scientists compared alternate-day fasting with a lowfat diet and a high-fat diet in terms of weight loss and cardio protection.2 Thirty-two obese subjects were randomly assigned to a high-fat (45 percent) or lowfat (25 percent) alternate-day-fasting diet that consisted of two phases: 1) a two-week baseline weight-maintenance period and 2) an eight-week alternate-day-fasting weight-loss period. All food was provided, but either way, fasting sounds about as much fun as running with scissors. What the researchers found was interesting, however.

Both groups lost a lot of fat, but the high-fat group actually lost more than the lowfat group (11.9 pounds vs. 9.2 pounds). Low-density-lipoprotein cholesterol and triglycerides decreased in both equally well. High-density lipoprotein, blood pressure and heart rate remained unchanged. There were basically no group differences for any parameter. These findings prove that a high-fat alternate-day-fasting diet is equally as effective as a lowfat alternating-day-fasting diet in helping obese subjects lose weight and improve cardiovascular risk factors.More important, it shows that eating a lot of fat, when calories are restricted, is not a bad thing.

One last note: Keep in mind that eating a lot of fat as part of a high-carb diet is not the same as doing it when you’re not eating all those carbs.

Here’s one last science pearl for you. We at the International Society of Sports Nutrition just published a position paper on energy drinks.3 In summary, they work and, when used as directed, are quite safe. Don’t believe the goofy spin on the paper put out by the mainstream press. Once again, they just don’t seem to get it.

—Jose Antonio, Ph.D.

 

Editor’s note: Jose Antonio, Ph.D., is an assistant professor at Nova Southeastern University in sunny South Florida.

 

1 Liao, Y.H., et al. (2013). Effect of dehydroepiandrosterone administration on recovery from mix-type exercise training-induced muscle damage. Eur J Appl Physiol. 113(1):99-107.

2Klempel, M.C., et al. (2013). Alternate day fasting (ADF) with a high-fat diet produces similar weight loss and cardio-protection as ADF with a low-fat diet. Metabolism. 62(1):137-43.

3Campbell, B., et al. (2013). International Society of Sports Nutrition position stand: energy drinks. J Int Soc Sports Nutr. 10(1):1.

Does Protein Make You Fat?

7205-eat1Self-styled experts often attribute various side effects to long-term high-protein diets—dehydration, calcium and bone loss, kidney disease and even increased bodyfat. The latter is based on the fact that protein contains calories, and taking in too many calories inevitably leads to gaining bodyfat.

A gram of protein contains four calories, the same as a gram of carbohydrate. Fat is the most concentrated source of calories at 9 1/2 per gram, but according to many nutrition pundits, that doesn’t matter. It makes no difference if you focus on a particular macronutrient—protein, fat or carb; if you consume more calories than you burn as energy, the excess will be stored as bodyfat.

Low-carb-diet proponents vigorously object to what they consider to be an oversimplification. It’s more than just a case of excess calories causing excess bodyfat, they say. There is also a hormonal interaction, namely insulin.

Insulin is indeed the most fattening hormone in the body. Whenever it is secreted, fat is either being maintained or synthesized. Among other functions, insulin blocks the activity of various enzymes that are involved in fat mobilization from fat cells as well as the actual oxidation, or burning, of fat.

Because of that, having a simple carbohydrate—a high-glycemic-index carb—prior to training will block the use of fat as fuel due to the higher insulin release that results. That effect lasts for an average of four hours after the high-carb meal is eaten. The general recommendation is that if you consume any carb prior to training, it should be from a low-glycemic-index source, which will cause less of an insulin release and promote more fat burning.

Even so, the low-carb devotees go further, claiming that calories are less important than carb intake for losing bodyfat. As evidence, they point to published studies that found more fat loss in people who ate low-carb diets than those who ate more carbs, even when the diets contained the identical number of calories. Low-carb diets not only control the harmful effects of insulin but also produce a higher thermic effect after meals. “Thermic,” or “thermogenic,” effect refers to the dissipation of consumed calories into heat. It’s also known as futile energy cycles, since no work is done to dissipate the calories.

Critics of low-carb regimens call this “metabolic magic”—meaning nonsense. A calorie is a calorie is a calorie, they say, and when it comes to ultimate fat loss, how many calories you take in compared to how many you burn is the ultimate arbiter. As evidence, they produce studies showing that while low-carb diets do tend to bring more rapid and greater rates of fat loss initially, as time goes on, it evens out. At the end of a year the fat-loss rate for low-carb diets and other diets is about the same, assuming that they contained the same number of total calories. The naysayers hold that insulin alone cannot make you fat unless you take in an overabundance of calories.

Then there is the protein issue. One of the established tenets of low-carbohydrate regimens is that you must increase your protein. It’s based on a number of established roles of protein in the body. For one thing, a higher protein intake is known to help maintain lean mass, mainly muscle.

Critics of low-carb diets like to point out that the body requires a certain amount of carbohydrate to function properly, an assertion that is not based in science. In fact, there is no established carbohydrate requirement. One reason is that other substances can be converted in the body to the main carbohydrate it uses—glucose. As such, lactate, glycerol from fat and amino acids from protein can all be converted into glucose in the liver. Consequently, carbs are not essential.

All that said, you don’t want to avoid carbs all the time. In some cases they offer definite advantages, such as for those engaged in endurance sports or training. A minimal amount of carb also plays a role in anabolic recovery processes following training, a key reason that you should never consider a zero-carb diet.

The low-carb diet features a higher protein intake because the excess protein helps to spare muscle that might otherwise be degraded for energy. The branched-chain amino acids are particularly effective in that regard. Other reasons for taking in more protein as your calories or carbs drop is to help control appetite, since protein helps you feel full when you’re dieting. Eating more protein also appears to maintain the resting metabolic rate, which ensures optimal fat loss.

What about the notion that taking in too much protein can make you fat? The pragmatic experience of generations of bodybuilders disputes it. While the suggested optimal intake of protein for bodybuilders is 1.7 grams per kilogram—2.2 pounds—of bodyweight, in actual practice most bodybuilders get far more than that. Considering the ubiquitous presence of protein in meat, chicken, turkey, eggs, milk and so on, along with the generous intake of protein supplements and meal-replacement powders, it’s not that difficult for many bodybuilders to take in two to three times more than the recommended dose of protein.

If, in fact, protein was as fattening as some people assert, bodybuilders who eat that much would look like walking versions of the Goodyear blimp. Clearly, they do not. Plus, bodybuilders are nutritionally savvy enough to boost their protein during dieting conditions—which also should be hindering their fat loss but clearly does not. Even people who don’t engage in weight training often eat more protein than they need, yet they rarely, if ever, get fat—unless they eat too many carbs and calories along with the protein.

How can that be? For one thing, the usual fate of ingested protein differs between inactive and active people. In active people excess protein undergoes metabolic changes in which the nitrogen portion is removed and excreted as urea. What about the calories? In active people the excess calories in protein are oxidized in the liver and not stored as fat.

While there is an outside chance that excess protein can wind up as fat in sedentary folks, in reality, they also have to be overeating carbs and calories in relationship to their activity levels. That was shown in a recent highly publicized study published in the prestigious Journal of the American Medical Association.1

Twenty-five healthy men and women, aged 18 to 35, all of whom were overweight to varying degrees, stayed in a metabolic unit in a research lab for 10 to 12 weeks. First, they ate a “weight-stabilizing” diet—15 percent protein, 25 percent fat and 60 percent carbs— for 13 to 25 days, and during the last eight weeks they were randomly divided into three diet groups:

 

• 5 percent protein (low protein)

• 15 percent protein (normal protein)

• 25 percent protein (high protein)

It wasn’t just the protein intake that the researchers were looking at, however. All three groups were purposely overfed during the last two months of the study—specifically, they got 40 percent more calories than what they ate on the baseline, or maintenance, diet. The results showed that those in the low-protein group gained less weight than the others, but they also stored 90 percent of their excess calories as fat. The 6.6 percent increase in resting metabolism in the low-protein group was attributed to the metabolic cost of converting the excess calories into bodyfat. In contrast, in the normal and higher protein groups 50 percent of the excess calories were stored as fat. The rest were burned up in a thermogenic reaction.

Another difference was that neither resting energy expenditure or lean body mass increased in the low-protein group, but they did in the normal- and high-protein groups. The excess calories eaten by all three groups were in the form of fat, which contains the greatest concentration of calories. Despite that, the high-protein group had the least amount of excess calories stored as fat, which underscores the effects of that strategy, as discussed above—that is, more calories are dissipated during a higher protein intake.

Based on the results of this study, the authors say that overall calorie intake, not how much protein you eat, is what makes you fat. In addition, it should be noted that the subjects did not exercise but rather remained sedentary in a metabolic lab. Without question, vigorous exercise changes the way nutrients are used in the body. Not only does exercise burn off excess calories, but the muscle gains accrued during weight training will prevent any possibility of excess protein being converted into bodyfat.

—Jerry Brainum

 

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1 Bray, G., et al. (2012). Effect of dietary protein content on weight gain, energy expenditure, and body composition during overeating. JAMA. 307;47-55.