Friday, January 18, 2013

Branching Out for More Muscle by Jerry Brainum


       How Branched-Chain Amino Acids Can Help You Get Bigger, Stronger and Leaner

Bodybuilders do not need to eat protein. There, I’ve said it. Before I’m accused of an ephedrine overdose or outright psychosis, permit me to qualify that seeming heresy. What bodybuilders—and everyone else—need are amino acids.
     During the digestion process, whole-food proteins, such as milk, meat and eggs, are broken down into their elemental parts, which are amino acids. Twenty-two dietary amino acids have been identified. Eight are considered essential, in that they cannot be synthesized in the body but have to be supplied by food. While all essential amino acids are vital for making gains in muscular size and strength—indeed, recent studies show that only the essential aminos are required in muscle protein synthesis—some of them are more vital than others.
    Three—valine, isoleucine and leucine—are collectively known as the branched-chain amino acids, so named because of their molecular structure, which features branched chains of carbon extending from their primary carbon structure. The BCAAs are unique because they’re not metabolized in the liver but in muscle instead. That’s why they’re called muscle aminos.
     Leucine stands out as having the most anabolic properties. When you see ads for supplements that claim to “overcome genetic limitations” and that feature complicated diagrams of protein synthesis, you’re probably looking at an illustration of BCAA molecules, especially leucine.
     BCAAs make up more than a third of the minimum daily requirement for essential aminos. They account for 15 percent of the total amino acid content of food proteins. Some popular protein supplements, such as whey, are effective primarily because of their rich BCAA content, although other aminos in whey, such as cysteine, offer considerable health benefits.
     Controversy dogs the BCAAs. Many scientists suggest that endurance athletes need more protein than strength athletes because extended exercise taps into protein as an energy source. The aminos primarily used for energy purposes in muscle are the BCAAs.Ammonia is a by-product of BCAA metabolism in muscle. While a high level of ammonia production is linked to fatigue, the ammonia produced in muscle by BCAA metabolism converts into two other amino acids, glutamine and alanine, which are energy substrates. Alanine gets transported to the liver, where it’s converted into glucose.  Early studies concluded that the energy-producing effect of BCAAs was so potent that it constituted a third form of muscle energy, after carbohydrate and fat. Later studies, however, showed that the enzymes involved in BCAA oxidation are too limited to affect muscle energy. Using radioactive-tagged leucine, researchers observed that BCAA oxidation increases—at most—by a factor of three. Compare that with the 10-to-20-fold increase in carbohydrate and fat oxidation. Besides, taking in carbs before or during a workout prevents the use of BCAAs for energy, which is good, as BCAAs are more suitable for muscle-building purposes.
    BCAAs offer a definite protein-sparing action in muscle during low-carbohydrate dieting.. When glycogen stores in muscle and the liver are low as a result of limited carb intake, the body tends to tap into muscle aminos as a source of energy. That’s more likely to happen when total calories are very low in relation to exercise or when bodyfat is below a certain point. The leaner you are, the higher the risk of tapping into muscle amino acid stores, especially during aerobic exercise. Taking BCAAs before cardio spares—that is, doesn’t gobble up—muscle aminos, thus preventing excess muscle protein breakdown during training.
    Another controversy related to BCAAs is whether they improve exercise performance or efficiency. In one experiment, presented at the 2004 conference of the National Strength and Conditioning Association, six healthy men took either BCAAs or a placebo, then engaged in weight training. When they took BCAAs, their levels of the stress hormone cortisol and creatine kinase, an enzyme released during muscle breakdown, went down and their testosterone count went up. The authors noted that participants who had more bodyfat needed a bigger dose of BCAAs to experience any anabolic effect     In a study of endurance exercise that used rats as subjects, researchers found that feeding the rats BCAAs led to a threefold increase in blood BCAA after only five minutes and gave them more stamina.1 The rats also generated more ammonia in their muscles because of BCAA metabolism.
     Studies show a relationship between the oxidation, or burning, of fat in muscle and the subsequent oxidation of BCAAs in the body.2 Exercise promotes the activity of an enzyme (BCKDH) that controls BCAA oxidation. That implies that any exercise leading to fat oxidation also raises the requirement for BCAA intake, explaining why those engaged in endurance exercise, which uses fat as an energy source, need more BCAAs. The same may apply to those engaged in extensive aerobic exercise to lose bodyfat.
Too much exercise can depress immune function, exposing hard-training athletes to disease. Some studies have linked the immune suppression to both the increased presence of cortisol and the decreased presence of glutamine. Studies with endurance athletes show that when they supplement with BCAAs, their glutamine count and immune function hold steady.3  Glutamine is important because immune cells use it as a direct fuel source.
    The relationship of BCAAs to glutamine synthesis raises the obvious question of whether it’s beneficial to use glutamine supplements if you’re also getting plenty of BCAAs. As with so many health issues, the answer is, it depends. For example, if you overtrain or are under industrial-strength stress, taking extra glutamine would be a sound idea. It counteracts the catabolic properties of cortisol and myostatin, and your body would prefer to conserve BCAAs for anabolic activity.
     One great advantage of BCAAs is that they spare muscle under hard-training conditions. In an experiment that used swimmers as subjects, one group received BCAA supplements, while another group got a placebo. Those in the BCAA group experienced decreased muscle breakdown following intensive exercise.4 Elsewhere, researchers who observed the behavior of rat skeletal muscle found that BCAAs block catabolic pathways in muscle by activating ubiquitin lysosome enzymes.5
     Some have suggested taking BCAAs before training as an anabolic stimulus, but they don’t come into play as an energy source except under extended low-carb dieting or with people who are way low in bodyfat. Nor do BCAAs contribute to protein synthesis during actual training; in fact, training blunts protein synthesis.6 The main concerns during training are energy production and maintaining muscle function. Protein synthesis kicks in after exercise. On the other hand, recent studies show that taking essential amino acids, including BCAAs, before exercise kick-starts anabolic processes. That’s because the increased blood flow you get from training promotes greater amino acid entry into muscle.
    One study showed that BCAAs help diminish muscle damage during exercise and block what is called delayed-onset muscle soreness following intense training.7 Sixteen women and 14 men took five grams of BCAAs prior to doing seven sets of 20-rep squats, resting two minutes between sets. Some of the subjects got a placebo. Those who took the BCAA supplement had significantly less soreness than the placebo group, the effect being more pronounced in the male than female subjects. The authors suggest that the mechanism may be a combination BCAAs’ blunting muscle breakdown and leucine’s stimulation of muscle protein synthesis.
    We already know that overtraining releases cortisol, which helps pump your stress up and break your muscle down. Some studies show that BCAAs trigger the metabolic processes that result in muscle protein synthesis. Other studies show that abundant cortisol interferes with BCAA metabolism, which may partially explain why cortisol is linked to muscle loss.8
     Also acting against cortisol are anabolic hormones, such as testosterone, growth hormone and insulin. It turns out that BCAAs stimulate the activity of all three anabolic hormones, which may help explain why BCAAs spare muscle protein. 9 Leucine in particular potently partners with insulin, which is anticatabolic and which, along with the essentital aminos, encourages muscle protein synthesis.
     Still another controversial aspect of BCAA metabolism involves the relationship of BCAA intake to exercise fatigue. The literature lists five possible causes of exercise-related fatigue:
1) Depletion of muscle creatine
2) Increased metabolic acidosis in muscle
3) Depleted muscle glycogen
4) Lowered blood glucose
5) An increase in the ratio of the amino acid tryptophan to BCAA.
     Take another look at item 5, which is known as the central fatigue theory, formulated in 1987. It seems that fatty acids and L-tryptophan compete for places to bind with a protein in the blood called albumin. During exercise, when free fatty acids increase in the blood, tryptophan gets bumped from albumin and travels to the brain, where it rapidly converts into serotonin, the brain chemical linked to relaxation, sleep and feelings of fatigue. BCAAs are in the picture because they compete with tryptophan for uptake into the brain. Their molecular structures enable them to get to the brain more easily than tryptophan, thereby blunting the fatigue effect.10
    The problem with the central fatigue idea is that it’s unlikely to play a significant role in bodybuilding workouts the notable exception being working out in the heat. That’s why you tire more when you train in a warm environment. Taking BCAAs could possibly energize you, but you probably couldn’t tell anyway if your workout is shorter than one hour.11 The central fatigue theory seems more relevant to long-distance endurance exercise. So really, you need to take another look at items 1 through 4 above.
Recent scientific findings show that of all amino acids, leucine is the most potent by far in relation to muscle protein synthesis. Some studies even suggest that taking leucine all by itself would be sufficient. It works both with and without insulin to get the muscle protein synthesis ball rolling.12
     Several studies point to leucine as a means of maintaining muscle, while dieting to lose bodyfat. If you do aerobics while dieting, taking a BCAA supplement prior to training—a dose of about five grams ought to do it—will prevent muscle loss. To get the most out of the BCAAs, include a source of vitamin B1, or thiamine, which is required for BCAA metabolism. A B-complex vitamin would work.
    Studies with older people show that a primary cause of frailty is muscle loss, known as sarcopenia. One reason that condition is so prevalent in older people is that age has blunted muscle protein synthesis. Studies show that such people respond favorably when provided with higher doses of BCAAs, particularly leucine.13, 14
     One recent study found that depleting animals of leucine initiated a type of starvation response and led to a complete loss of bodyfat.15 After 17 days on their leucine-deficient diet, normal mice lost 48 percent of their liver fat and 97 percent of their abdominal fat. While that finding could lead to the development of new drugs in the war against obesity, don’t try it at home: Removing leucine from your diet would result in serious health problems. Yes, you would lose plenty of fat—but muscle too.
    One thing that does impair leucine’s protein-synthesis effect is alcohol, which produces leucine resistance in muscle and shuts down muscle protein synthesis.15
    While leucine is the most anabolic of the three BCAAs—indeed the most anabolic of any amino acids—your body still needs the other essential aminos. The usual suggested proportions for the BCAAs are 50 percent leucine, 25 percent isoleucine and 25 percent valine. Since the BCAAs compete with other amino acids for uptake into the brain, getting too much of one or another could lead to a drop in the synthesis of brain chemicals, such as serotonin, dopamine and norepinephrine. By and large, BCAAs are nontoxic and balanced in dietary intake. The only exception is with a genetic disorder specific to newborns, called maple syrup disease. So named because the urine smells like maple syrup (don’t add to pancakes!), it’s caused by a lack of enzymes that metabolize BCAAs, leading to an unhealthy buildup of the aminos in blood and brain. One result: mental retardation.
So do you need to take BCAAs? BCAA supplements do come in handy just prior to training, but if you’re taking a protein supplement, odds are you’re getting plenty. Consider the content of common protein sources:
 Food:/leucine/ BCAAs

Whey protein isolate: 14%, 26%
Milk protein: 10%, 21%
Muscle protein (meat): 8%, 18%
Soy protein isolate: 8%, 18%
Wheat protein: 7%, 15%
To take or not to take; the decision is up to you.
                                     
                                                     References
1 Calders, P., et al. (1997). Pre-exercise branched-chain amino acid administration increases endurance performance in rats. Med Sci Sports Exer. 29:1182-1186.
2 Shimomura, Y., et al. (2004). Exercise promotes BCAA catabolism: Effects of BCAA supplementation on skeletal muscle during exercise. J Nutr. 134:1583S-1587S.
3 Bassit, R.A., et al. (2002). Branched-chain amino acid supplementation and immune response of long-distance athletes.Nutrition. 18:376-79.
4 Tang, F. (2006). Influence of branched-chain amino acid supplementation on urinary protein metabolite concentrations after swimming. J Am Coll Nutr. 25:188-94.
5 Busquets, S., et al. (2000). Branched-chain amino acids inhibit proteolysis in rat skeletal muscle: Mechanisms involved. J Cell Physiol. 184:380-84.
6 Blomstrand, E., et al. (2001). BCAA intake affects protein metabolism after but not during exercise in humans. Am J Physiol Metab. 281:E365-E374.
7 Shimomura, Y., et al. (2006). Nutraceutical effects of branched-chain amino acids on skeletal muscle. J Nutr. 136:529S-532S.
8 Zhenqi, L., et al. (2001). Branched-chain amino acids activate messenger ribonucleic acid translation regulatory proteins in human skeletal muscle, and glucocorticoids blunt this action. J Clin Endocrin Metabol. 86:2136-2143.
9 De Palo, E., et al. (2001). Plasma lactate, GH and GH-binding protein levels in exercise following BCAA supplementation in athletes. Amino Acids. 20:1-11.
10 Blomstrand, E. (2001). Amino acids and fatigue. Amino Acids. 20:25-34.
 11 Mittleman, K.D., et al. (1998). Branched-chain amino acids prolong exercise during heat stress in men and women. Med Sci Sports Exerc. 30:83-91.
12 Anthony, J.C., et al. (2000). Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formulation. J Nutr. 130:139-45.
13 Rieu, I., et al. (2006). Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidemia. J Physiol. 575:305-315.
14 Fujita, S., et al. (2006). Amino acids and muscle loss with age. J Nutr. 136:277S-280S.
15 Guo, F., et al. (2007). The GCN2 elIF2a kinase regulates fatty acid homeostasis in the liver during deprivation of an essential amino acid. Cell Metabol. 5:103-114.

©,2013 Jerry Brainum. Any reprinting in any type of media, including electronic and foreign is expressly prohibited.

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

 
 

The Applied Ergogenics blog is a collection of articles written and published by Jerry Brainum over the past 20 years. These articles have appeared in Muscle and Fitness, Ironman, and other magazines. Many of the posts on the blog are original articles, having appeared here for the first time. For Jerry’s most recent articles, which are far more in depth than anything that appears on this blog site, please subscribe to his Applied Metabolics Newsletter, at www.appliedmetabolics.com. This newsletter, which is more correctly referred to as a monthly e-book, since its average length is 35 to 40 pages, contains the latest findings about nutrition, exercise science, fat-loss, anti-aging, ergogenic aids, food supplements, and other topics. For 33 cents a day you get the benefit of Jerry’s 53 years of writing and intense study of all matters pertaining to fitness,health, bodybuilding, and disease prevention.

 

See Jerry's book at  http://www.jerrybrainum.com

 

Want more evidence-based information on exercise science, nutrition and food supplements, ergogenic aids, and anti-aging research? Check out Applied Metabolics Newsletter at www.appliedmetabolics.com

 

Friday, January 11, 2013

Gain Preserve by Jerry Brainum

                                               Does whey help retain muscle?

When you take a layoff from training, you begin to lose muscle size. Conversely, a combination of training and a higher protein intake promotes gains in muscular size and strength. Thus, the question arises: Will consuming a high-protein whey supplement help maintain muscle during a period of no or reduced training?
    That question was investigated by researchers from the University of Nebraska, who presented their findings at the 2006 meeting of the National Strength and Conditioning Association. Sadly, the study was flawed to a certain extent because the subjects were untrained. They were randomly assigned to either a group getting whey and leucine, a branched-chain amino acid linked to increased muscle protein synthesis, or a placebo. The subjects did resistance training three times a week, using weights equal to 80 percent of one-rep maximum. For the first month they trained without using any supplements. During weeks four to eight the training was reduced to once a week, followed by no training from weeks eight to 20. They took the whey-and-leucine supplement during weeks four to 12, with no supplements during weeks 12 to 20.
     The results: There were no differences in measures of strength, muscle size and bodyfat levels between those who got the whey and leucine and those who got the placebo. Conclusion: Protein—or any supplement, for that matter—can’t preserve muscle size and strength in the absence of sufficient exercise stimulation.

©,2013 Jerry Brainum. Any reprinting in any type of media, including electronic and foreign is expressly prohibited.
 

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

 
 

The Applied Ergogenics blog is a collection of articles written and published by Jerry Brainum over the past 20 years. These articles have appeared in Muscle and Fitness, Ironman, and other magazines. Many of the posts on the blog are original articles, having appeared here for the first time. For Jerry’s most recent articles, which are far more in depth than anything that appears on this blog site, please subscribe to his Applied Metabolics Newsletter, at www.appliedmetabolics.com. This newsletter, which is more correctly referred to as a monthly e-book, since its average length is 35 to 40 pages, contains the latest findings about nutrition, exercise science, fat-loss, anti-aging, ergogenic aids, food supplements, and other topics. For 33 cents a day you get the benefit of Jerry’s 53 years of writing and intense study of all matters pertaining to fitness,health, bodybuilding, and disease prevention.

 

See Jerry's book at  http://www.jerrybrainum.com

 

Want more evidence-based information on exercise science, nutrition and food supplements, ergogenic aids, and anti-aging research? Check out Applied Metabolics Newsletter at www.appliedmetabolics.com


Saturday, January 5, 2013

Soy, Muscles and Hormones by Jerry Brainum

      The three primary supplemental proteins bodybuilders use are whey, whey-and-casein combinations and soy. Of the three, soy is by far the most controversial. Soy contains active substances called isoflavones, such as genistin and diadzin, that are also known as phytoestrogens, or plant estrogens. They are so named because of their structural resemblance to estrogen. They confer certain health benefits, such as decreased incidence of breast and prostate cancers, but some people feel that the estrogenlike components of soy can produce negative estrogenic effects, such as water retention.
     Each gram of soy protein contains three to four milligrams of isoflavones. Blood levels of isoflavones begin to peak one to two hours after you eat soy, although the major peak occurs after four to six hours. The half-life, or time it takes to eliminate half the initial dose, is four to eight hours.
     From a bodybuilding standpoint the main concern is that soy may interfere with other hormones, such as thyroid and testosterone. Testosterone is a major anabolic hormone, while thyroid hormones control the metabolic rate. Too much thyroid can lead to muscle catabolism, and too little thyroid output makes dieting difficult because it blunts the rate of fat loss.
    Animal studies show that soy interferes with enzymes involved in the synthesis of thyroid hormone. That research has been extended to human use of thyroid, but a recent review of human studies found that soy or isoflavone had no effect on thyroid function in healthy adults.1 If anything, soy appears to increase the level of T4 thyroid hormone in the body. It may, however, interfere with the absorption of thyroid drugs if taken concurrently. The simple solution is to take soy at a different time.
     Soy still may interfere with thyroid function under two conditions. The first involves an existing problem, such as hypothyroid, or low thyroid output, that’s not being treated by thyroid drugs. The second condition is a deficiency of the trace mineral iodine, which the body requires for the synthesis of thyroid hormones. The likelihood that most people in the United States have an iodine deficiency is remote. Seafood and iodized salt are common sources of iodine, and most food supplements contain it.
    The notion that soy interferes with testosterone metabolism stems from animal research, plus a few human-based studies. Studies with monkeys show that feeding infant monkeys soy lowers testosterone levels—but that doesn’t happen with adult monkeys. Some rat studies show that soy lowers testosterone, others that it increases testosterone. Studies with young men did show a minor lowering of testosterone, but the effect was transient and occurred only with a low-isoflavone soy protein, which is curious because the isoflavones are thought to be the active ingredients. Those who took a high-isoflavone soy protein experienced no change in testosterone levels.
    The latest study to examine the issue featured subjects who were given a high-isoflavone soy protein supplement, a vanilla whey protein supplement or a placebo, vanilla cake mix.2 The subjects used the substances over four weeks.
    Only the soy protein provided an antioxidant effect, while none of the proteins (or the cake mix) lowered testosterone levels in any of the subjects. The authors suggest that a particular amino acid pattern in soy was responsible for the lowered testosterone levels found in earlier studies, which would not occur if other proteins were also ingested.
                                                    A Surprising Estrogen Inhibitor

     The enzyme aromatase converts androgens, such as testosterone, into estrogen. That’s a real problem for those who use anabolic steroids known to be subject to aromatization, including any type of testosterone injection. Too much estrogen causes water retention and fat deposition just under the skin. In addition, elevated estrogen levels are more potent than androgens in providing negative feedback to the brain, which results in depressed synthesis of testosterone in the body. Recent studies have implicated elevated estrogen levels in men in the onset of prostate cancer.
    Bodybuilders and athletes on steroids counter the effects of elevated estrogen in two ways. The older solution blocks estrogen receptors with a drug such as Nolvadex. A better solution blocks or inhibits the activity of the aromatase enzyme itself. Drugs that accomplish that were developed to treat estrogen-dependent breast cancers, especially in older women. Aromatase-blocking drugs are now the most popular means of controlling estrogen.
    What’s not generally known, however, is that natural aromatase blockers exist in certain foods and supplements. Red wine, green tea and grapeseed extract all contain polyphenols that have aromatase-inhibiting properties. A new study identifies another aromatase blocker: beer.3 The particular ingredients responsible for the effect are hops and barley malt.
    Hops add bitterness to beer, while malt is a flavoring compound. So-called prenylflavonoids in hops are thought to explain the health effects associated with beer drinking, such as cardiovascular protection and protection against cancer. They don’t interfere with the synthesis of aromatase (as do the drug versions) but instead seem to throw a biochemical monkey wrench at its activity. The net effect, however, is lower estrogen synthesis.
     What isn’t clear from the study is how much beer is effective against aromatase. That’s because the study design was in vitro, involving isolated cells. Earlier research showed that a flavonoid called chrysin was just as effective as anti-estrogen drugs. Later studies, however, showed that while chrysin works great outside the body, a living human being has difficulty absorbing it.
     That doesn’t mean the active ingredients in beer suffer a similar fate. Beer’s many benefits indicate that natural substances are indeed absorbed. The information shouldn’t be construed as a license to drink vast amounts of beer. Alcohol itself can lower anabolic hormone levels and directly destroys muscle fibers. Drink beer in moderation.
                                          Good News About Omega-3 Fatty Acids


        Omega-3 fatty acids, found in fatty fish and fish oils, offer a plethora of health benefits. Omega-3 fats lower inflammation by inhibiting the conversion of arachidonic acid (AA), a ubiquitous fatty acid found in red meat and various other proteins, into inflammatory eicosanoids (the eicosanoids produced from omega-3 fats are neutral and don’t contribute to inflammation in the body).
    While that sounds good, at least one of the inflammatory eicosanoids produced from AA, known as prostaglandin F2-A, is involved in muscle growth. Various published studies show that drugs that lower inflammation, such as aspirin and Advil or Motrin (a.k.a. ibuprofen), can interfere with muscle protein synthesis following exercise, thought to be due to a blocking of the synthesis of prostaglandin F2-A. Because omega-3 fatty acids also interfere with that enzyme, it was assumed that taking a supplement such as fish oil might interfere with muscle gains as well.
     A newly published study, however, dispels that notion.4 Researchers randomly assigned 162 men and women diets that contained high proportions of saturated and monounsaturated fatty acids for three months. Participants were given either fish oil capsules (3.6 grams daily) or a placebo.
Taking fish oils produced an antioxidant effect but didn’t affect the synthesis of prostaglandin F2-A in any of the subjects. In practical terms, that means you can take omega-3 fatty acid supplements, such as fish oils, without any fear of limiting your progress in building muscle and getting stronger.
                                                
                                            Steroids and Antioxidant Protection
  

    Exercise protects against cardiovascular disease through several mechanisms. One obvious way involves a loss of bodyfat. Losing fat improves health by lowering blood pressure, workload on the heart, and body inflammation. Since exercise requires a higher oxygen intake, the body increases the production of several natural antioxidant enzymes, such as superoxide dismutase and glutathione.
     The natural, built-in antioxidants offset the greater release of noxious by-products of oxygen metabolism called free radicals, which occurs after you work out. They’re considered a primary benefit of exercise because they provide extra protection against diseases caused by excess free radicals in the body, such as cardiovascular disease and cancer.
    Anabolic steroids have been linked to cardiovascular disease. Particularly when used in large amounts, steroids have adverse effects on blood lipids, such as high-density lipoprotein (HDL). A new study, using rats as subjects, identifies another way that steroid use promotes cardiovascular disease.5
    Researchers gave the rats large doses of the injectable anabolic steroid nandrolone decanoate, trade name Deca-Durabolin. Deca is popular among athletes because of its high-anabolic, low-androgenic profile. On the other hand, it’s also easily identified in drug tests, and markers for the drug can be detected for as long as a year after its use is discontinued.
    The experiment showed that when exercised rats are given amounts of Deca comparable to levels used by athletes, the antioxidant protection exercise produces is nullified. That sets up a scenario for increased cardiovascular damage and may explain some of the cardiovascular disease effects linked to high steroid use.
Although the study involved animal subjects and awaits confirmation in human studies, the mechanism is likely to also be true of humans. It would be prudent for anyone who uses anabolic steroid drugs to increase his or her intake of various dietary antioxidants, such as vitamins C and E, and various minerals, such as selenium and zinc. Manganese is also vital because one of the antioxidant enzymes requires manganese to be activated in the body.On the other hand, it would also be prudent not to go overboard with pre-workout antioxidant supplements. Recent research shows that reactive oxygen species, or free radicals, act as signaling factors in the muscle growth and recovery process.As such, it's better to ingest your antioxidant supplements away from a workout.
                                                                 References
1 Messina, M., et al. (2006). Effects of soy protein and soybean isoflavones on thyroid function in healthy adults and hypothyroid patients: A review of the relevant literature. Thyroid. 16:249-258.
2 DiSilvestro, R.A., et al. (2006). Soy protein intake by active young adult men raises plasma antioxidant capacity without lowering plasma testosterone. Nutr. Research. 26:92-95.
3 Monteiro, R., et al. (2006). Effect of hop (Humulus lupulus) flavonoids on aromatase (estrogen synthase) activity. J Agric Food Chemist. 54:2938-2943.
4 Nalsen, C., et al. (2006). Dietary (N-3) fatty acids reduce plasma F-2 isoprostanes but not prostaglandin F2-A in healthy humans. J Nutr. 136:1222-1228.
5 Chaves, E.A., et al. (2006). Nandrolone decanoate impairs exercise-induced cardioprotection: Role of antioxidant enzymes. J Steroid Biochem Molec Biol. 99(4-5):223-230
 

©,2013 Jerry Brainum. Any reprinting in any type of media, including electronic and foreign is expressly prohibited.
 

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

 
 

The Applied Ergogenics blog is a collection of articles written and published by Jerry Brainum over the past 20 years. These articles have appeared in Muscle and Fitness, Ironman, and other magazines. Many of the posts on the blog are original articles, having appeared here for the first time. For Jerry’s most recent articles, which are far more in depth than anything that appears on this blog site, please subscribe to his Applied Metabolics Newsletter, at www.appliedmetabolics.com. This newsletter, which is more correctly referred to as a monthly e-book, since its average length is 35 to 40 pages, contains the latest findings about nutrition, exercise science, fat-loss, anti-aging, ergogenic aids, food supplements, and other topics. For 33 cents a day you get the benefit of Jerry’s 53 years of writing and intense study of all matters pertaining to fitness,health, bodybuilding, and disease prevention.

 

See Jerry's book at  http://www.jerrybrainum.com

 

Want more evidence-based information on exercise science, nutrition and food supplements, ergogenic aids, and anti-aging research? Check out Applied Metabolics Newsletter at www.appliedmetabolics.com