Archive for the ‘Bodybuilding Supplements’ Category

A Temple University researcher seeking physiological evidence of chronic fatigue syndrome (CFS) has found a link between creatine and metabolic energy. The findings, which hold promise for future CFS treatments, were published in a recent issue of the Journal of Applied Physiology.

“We found that creatine affects mitochondria – the parts of the cells that produce energy for all biological functioning – in normal human subjects. Now that we have established this baseline evidence, we are looking at the link between creatine and energy production in CFS patients,” said lead author Sinclair Smith, Sc.D., assistant professor of occupational therapy in Temple’s College of Health Professions.

Creatine, thought to build muscle and improve performance, is a popular over-the-counter supplement used by athletes. Smith and his colleagues wondered if creatine could also be used to help relieve the extreme physical and mental fatigue that strikes CFS sufferers. “Many physicians still don’t believe that CFS exists, making it important to investigate possible physiologic differences and to determine if we can impact metabolic function in CFS patients,” explained Smith.

“In addition to improving muscle metabolic function, recent studies show that creatine supplementation may improve nervous system function as well. Given that cognitive fatigue is a frequent symptom of CFS, we thought that creatine may enhance both muscle and neural metabolic status in people with CFS,” said Smith.

In the study, “Use of phosphocreatine kinetics to determine the influence of creatine on muscle mitochondrial respiration: an in vivo 31P-MRS study of oral creatine ingestion,” the researchers analyzed the effect of naturally -produced and supplemental creatine on the rate of muscle metabolism using non-invasive magnetic resonance imaging (MRI) techniques during exercise and rest.

While previous studies have evaluated the link between creatine and mitochondria in animals and human muscle samples, Smith’s was the first lab to test in people.

Smith collaborated in this research with the U.S. Army Research Institute of Environmental Medicine, Brigham and Women’s Hospital and Harvard Medical School, Boston University and Sargent College of Health and Rehabilitation Sciences.

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    Article adapted by MD Sports from original press release.
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    Creatine, a popular nutritional supplement used by weightlifters and sprinters to improve athletic performance, could lend muscle strength to people with muscular dystrophies.

    Muscle strength increased by an average of 8.5 percent among patients taking creatine, compared to those who did not use the supplement, according to a recent review of studies. Creatine users also gained an average of 1.4 pounds more lean body mass than nonusers.

    The evidence from the studies “shows that short- and medium-term creatine treatment improves muscle strength in people with muscular dystrophies and is well-tolerated,” said lead reviewer Dr. Rudolf Kley of Ruhr University Bochum in Germany.

    The review appears in the latest issue of The Cochrane Library, a publication of The Cochrane Collaboration, an international organization that evaluates medical research. Systematic reviews draw evidence-based conclusions about medical practice after considering both the content and quality of existing medical trials on a topic.

    Creatine is found naturally in the body, where it helps supply energy to muscle cells. Athletes looking for short bursts of intense strength have used creatine in powders or pills for decades, but the supplement became more popular after the 1992 Barcelona Olympics, when sprinters, rowers and cyclists went public with their creatine regimens.

    Although creatine has been widely studied as a performance enhancer, it’s still not clear if the supplement makes a difference, according to Roger Fielding, Ph.D., of Tufts University, who has also recently written a review of creatine treatments for neuromuscular diseases.

    People with muscular dystrophies can have lower-than-normal levels of creatine, along with increasing muscle weakness as their disease progresses. Since some studies suggest that creatine improves muscle performance in healthy people, many researchers have reasoned that it might be helpful in treating muscle disease.

    The Cochrane researchers reviewed 12 studies that included 266 people with different types of muscular dystrophy. People in the studies who took creatine supplements used them for three weeks to six months.

    In muscular dystrophies, the proteins that make up the muscles themselves are either missing or damaged. In a related group of disorders called metabolic myopathies, the chemicals that help muscles operate go awry.

    Although creatine seemed to help many patients with muscular dystrophies, those with metabolic myopathies gained no more muscle strength or lean body mass than patients who did not use the supplement.

    The reason for the contrasting results — creatine’s “fairly consistent” effects in muscular dystrophy and lack of effectiveness in metabolic diseases — is “not entirely clear,” Kley said, calling for more research on treatment for metabolic disorders.

    The review was supported by the Neuromuscular Center Ruhrgebiet/Kliniken Bergmannsheil, at Ruhr-University Bochum and the Hamilton Health Sciences Corporation, in Canada. Kley and colleagues have each participated in trials of creatine treatment for muscle disorders, although none of the studies was sponsored by a maker of creatine.

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    Article adapted by MD Sports from original press release.
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    FOR MORE INFORMATION
    Health Behavior News Service: hbns-editor@cfah.org

    Kley RA, Vorgerd M, Tarnopolsky MA. Creatine for treating muscle disorders. Cochrane Database of Systematic Reviews 2007, Issue 1.

    The Cochrane Collaboration is an international nonprofit, independent organization that produces and disseminates systematic reviews of health care interventions and promotes the search for evidence in the form of clinical trials and other studies of interventions. Visit http://www.cochrane.org for more information.

Lower muscle mass and an increase in body fat are common consequences of growing older.

While exercise is a proven way to prevent the loss of muscle mass, a new study led by McMaster researcher Dr. Mark Tarnopolsky shows that taking a combination of creatine monohydrate (CrM) and conjugated linoleic acid (CLA) in addition to resistance exercise training provides even greater benefits.

The study to be published on Oct. 3 in PLoS One, an international, peer-reviewed online journal of the Public Library of Science, involved 19 men and 20 women who were 65 years or older and took part in a six-month program of regular resistance exercise training.

In the randomized double blind trial, some of the participants were given a daily supplement of creatine (a naturally produced compound that supplies energy to muscles) and linoleic acid (a naturally occurring fatty acid), while others were given a placebo. All participants took part in the same exercise program.

The exercise training resulted in improvements of functional ability and strength in all participants, but those taking the CrM and CLA showed even greater gains in muscle endurance, an increase in fat-free mass and a decrease in the percentage of body fat.

“This data confirms that supervised resistance exercise training is safe and effective for increasing strength and function in older adults and that a combination of CrM and CLA can enhance some of the beneficial effects of training over a six month period,” said Tarnopolsky, a professor of pediatrics and medicine.

This study provides functional outcomes that build on an earlier mechanistic study co-led by Tarnopolsky and Dr. S. Melov at the Buck Institute of Age Research, published in PLoS One this year, which provided evidence that six months of resistance exercise reversed some of the muscle gene expression abnormalities associated with the aging process.
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Article adapted by MD Sports Weblog from original press release.
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Contact: Veronica McGuire
McMaster University

By studying the genes of a German child born with unusually well developed muscles, an international research team has discovered the first evidence that the gene whose loss makes “mighty mice” also controls muscle growth in people.

Writing in the June 24 issue of the New England Journal of Medicine, German neurologist Markus Schuelke, M.D., and the team show that the child’s extra-large muscles are due to an inherited mutation that effectively silences the myostatin gene, proving that its protein normally keeps muscle development in check in people.

People with muscle-wasting conditions such as muscular dystrophy, and others just wanting to “bulk up,” have eagerly followed work on myostatin, hoping for a way to counteract the protein’s effects in order to build or rebuild muscle mass. But while research with mice has continued to reveal myostatin’s role and the effects of interfering with it, no one knew whether any of the results would be relevant to humans.

“This is the first evidence that myostatin regulates muscle mass in people as it does in other animals,” says Se-Jin Lee, M.D., Ph.D., professor of molecular biology and genetics in the Institute for Basic Biomedical Sciences at Johns Hopkins and co-author on the study. “That gives us a great deal of hope that agents already known to block myostatin activity in mice may be able to increase muscle mass in humans, too.”

Lee and his team discovered in 1997 that knocking out the myostatin gene led to mice that were twice as muscular as their normal siblings, lending them the moniker “mighty mice.” Later, others showed that naturally bulky cattle, such as Belgian Blues, got their extra muscles from lack of myostatin, too.

An unusual opportunity to examine myostatin’s role in humans arose when Schuelke examined a newborn baby boy, almost five years ago, and was struck by the visible muscles on the infant’s upper legs and upper arms. When ultrasound proved that the muscles were roughly twice as large as other infants’, but otherwise normal, Schuelke realized that a naturally occurring mutation in the child’s myostatin gene might be the cause.

Sequencing the myostatin gene from the boy and his mother, who had been a professional athlete, revealed a single change in the building blocks of the gene’s DNA. Surprisingly, the change was not in the gene regions that correspond to the resulting protein, but in the intervening regions that are used only to create protein-making instructions, thus changing the gene’s protein-building message.

“The mutation caused the gene’s message, the messenger RNA, to be wrong,” says Hopkins

neurologist Kathryn Wagner, M.D., Ph.D., who tested the genetic mutation’s effect in laboratory studies. “If the message had been used to make a protein, it would be much shorter than it should be. But we think the process doesn’t even get that far; instead the cells just destroy the message.”

Co-authors from Wyeth Research, Cambridge, Mass., analyzed samples of the child’s blood for evidence of the myostatin protein and found none. “Both copies of the child’s myostatin gene have this mutation, so little if any of the myostatin protein is made,” says Schuelke. “As a result, he has about twice the muscle mass of other children.”

Completely lacking myostatin, the boy is stronger than other children his age, and fortunately has no signs of problems with his heart so far, Schuelke says. But he adds that it’s impossible to know whether the lack of myostatin in that crucial muscle might lead to problems as the boy gets older.

While other family members — the boy’s mother and her brother, father and grandfather — were also reported to have been usually strong, only the mother’s DNA was available for analysis along with her son’s. Schuelke discovered that only one copy of the mother’s myostatin gene had the mutation found in both copies of her son’s myostatin gene. (We have two copies of each gene; one inherited from the mother and one inherited from the father.)

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Article adapted by MD Sports Weblog from original press release.
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 Contact: Joanna Downer
Johns Hopkins Medical Institutions

 

The Johns Hopkins researchers were funded by the National Institutes of Health and the Muscular Dystrophy Association. The German researchers were funded by the parents’ self-help group (Helft dem muskelkranken Kind).

Authors on the paper are Schuekle, Christoph Hubner, Thomas Riebel and Wolfgang Komen of Charite, University Medical Center Berlin, Germany; Wagner and Lee of Johns Hopkins; Leslie Stolz and James Tobin of Wyeth Research, Cambridge, Ma.; and Thomas Braun of Martin-Luther-University, Halle-Wittenberg, Germany.

*Under a licensing agreement between MetaMorphix Inc. and The Johns Hopkins University, Lee is entitled to a share of royalty received by the University on sales of products described in this article. Lee also is entitled to a share of sublicensing income from arrangements between MetaMorphix and American Home Products (Wyeth Ayerst Laboratories) and Cape Aquaculture Technologies. Lee and the University own MetaMorphix Inc. stock, which is subject to certain restrictions under University policy. Lee owns Cape Aquaculture Technologies stock, which is subject to certain restrictions under University policy. Lee has served as a paid consultant to MetaMorphix Inc. The terms of these arrangements are being managed by The Johns Hopkins University in accordance with its conflict of interest policies.

Don’t drink alcohol. Take vitamins. Avoid eating eggs. We’ve heard these pieces of nutritional advice for years – but are they accurate?

Not necessarily, say two exercise physiologists who presented at the American College of Sports Medicine (ACSM) 11th-annual Health & Fitness Summit & Exposition in Dallas, Texas. Wendy Repovich, Ph.D., FACSM, and Janet Peterson, Dr.P.H., FACSM, set out to debunk the “Top 10 Nutrition Myths.”

According to Repovich and Peterson, these nutrition myths are:

10. Eating carbohydrates makes you fat. Cutting carbs from your diet may have short-term weight loss benefits due to water loss from a decrease in carbohydrate stores, but eating carbs in moderation does not directly lead to weight gain. The body uses carbs for energy, and going too long without them can cause lethargy.

9. Drink eight, 8-oz. glasses of water per day. You should replace water lost through breathing, excrement and sweating each day – but that doesn’t necessarily total 64 ounces of water. It’s hard to measure the exact amount of water you have consumed daily in food and drink, but if your urine is pale yellow, you’re doing a good job. If it’s a darker yellow, drink more H2O.

8. Brown grain products are whole grain products. Brown dyes and additives can give foods the deceiving appearance of whole grain. Read labels to be sure a food is whole grain, and try to get three-ounce equivalents of whole grains per day to reduce the risk of heart disease, diabetes, and stroke.

7. Eating eggs will raise your cholesterol. This myth began because egg yolks have the most concentrated amount of cholesterol of any food. However, there’s not enough cholesterol there to pose health risks if eggs are eaten in moderation. Studies suggest that eating one egg per day will not raise cholesterol levels and that eggs are actually a great source of nutrients.

6. All alcohol is bad for you. Again, moderation is key. Six ounces of wine and 12 ounces of beer are considered moderate amounts, and should not pose any adverse health effects to the average healthy adult. All alcohol is an anticoagulant and red wine also contains antioxidants, so drinking a small amount daily can be beneficial.

5. Vitamin supplements are necessary for everyone. If you eat a variety of fruits, vegetables, and whole grains, along with moderate amounts of a variety of low-fat dairy and protein and the right quantity of calories, you don’t need to supplement. Most Americans do not, so a multi-vitamin might be good. Special vitamin supplements are also recommended for people who are pregnant or have nutritional disorders.

4. Consuming extra protein is necessary to build muscle mass. Contrary to claims of some protein supplement companies, consuming extra protein does nothing to bulk up muscle unless you are also doing significant weight training at the same time. Even then the increased requirement can easily come from food. A potential problem with supplements is the body has to work overtime to get rid of excess protein, and can become distressed as a result.

3. Eating fiber causes problems if you have irritable bowel syndrome (IBS). There are two kinds of fiber: soluble and insoluble. Insoluble fiber can cause problems in IBS sufferers; soluble fiber, however, is more easily absorbed by the body and helps prevent constipation for those with IBS. Soluble fiber is found in most grains.

2. Eating immediately after a workout will improve recovery. Endurance athletes need to take in carbohydrates immediately after a workout to replace glycogen stores, and a small amount of protein with the drink enhances the effect. Drinking low-fat chocolate milk or a carbohydrate drink, like Gatorade, is better for the body, as they replace glycogen stores lost during exercise. Protein is not going to help build muscle, so strength athletes do not need to eat immediately following their workout.

1. Type 2 diabetes can be prevented by eating foods low on the glycemic index. High levels of glucose are not what “cause” diabetes; the disease is caused by the body’s resistance to insulin. Foods high on the glycemic index can cause glucose levels to spike, but this is just an indicator of the presence of diabetes, not the root cause.

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Article adapted by MD Sports Weblog from original press release.
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Contact: Communications and Public Information
American College of Sports Medicine

The American College of Sports Medicine is the largest sports medicine and exercise science organization in the world. More than 20,000 International, National and Regional members are dedicated to promoting and integrating scientific research, education and practical applications of sports medicine and exercise science to maintain and enhance physical performance, fitness, health and quality of life.

Lower muscle mass and an increase in body fat are common consequences of growing older.

While exercise is a proven way to prevent the loss of muscle mass, a new study led by McMaster researcher Dr. Mark Tarnopolsky shows that taking a combination of creatine monohydrate (CrM) and conjugated linoleic acid (CLA) in addition to resistance exercise training provides even greater benefits.

The study to be published on Oct. 3 in PLoS One, an international, peer-reviewed online journal of the Public Library of Science, involved 19 men and 20 women who were 65 years or older and took part in a six-month program of regular resistance exercise training.

In the randomized double blind trial, some of the participants were given a daily supplement of creatine (a naturally produced compound that supplies energy to muscles) and linoleic acid (a naturally occurring fatty acid), while others were given a placebo. All participants took part in the same exercise program.

The exercise training resulted in improvements of functional ability and strength in all participants, but those taking the CrM and CLA showed even greater gains in muscle endurance, an increase in fat-free mass and a decrease in the percentage of body fat.

“This data confirms that supervised resistance exercise training is safe and effective for increasing strength and function in older adults and that a combination of CrM and CLA can enhance some of the beneficial effects of training over a six month period,” said Tarnopolsky, a professor of pediatrics and medicine.

This study provides functional outcomes that build on an earlier mechanistic study co-led by Tarnopolsky and Dr. S. Melov at the Buck Institute of Age Research, published in PLoS One this year, which provided evidence that six months of resistance exercise reversed some of the muscle gene expression abnormalities associated with the aging process.

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Article adapted by MD Sports Weblog from original press release.
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Contact: Veronica McGuire
McMaster University

Myostatin (MSTN) is a transforming growth factor-ß (TGF-ß) family member that plays a critical role in regulating skeletal muscle mass [1]. Mice engineered to carry a deletion of the Mstn gene have about a doubling of skeletal muscle mass throughout the body as a result of a combination of muscle fiber hyperplasia and hypertrophy [2]. Moreover, loss of myostatin activity resulting either from postnatal inactivation of the Mstn gene [3], [4] or following administration of various myostatin inhibitors to wild type adult mice [5][7] can also lead to significant muscle growth. Hence, myostatin appears to play as least two distinct roles, one to regulate the number of muscle fibers that are formed during development and a second to regulate growth of muscle fibers postnatally. The function of myostatin appears to have been conserved across species, as inactivating mutations in the myostatin gene have been demonstrated to cause increased muscling in cattle [8][11] , sheep [12], dogs [13] and humans [14]. As a result, there has been considerable effort directed at developing strategies to modulate myostatin activity in clinical settings where enhancing muscle growth may be beneficial. In this regard, loss of myostatin activity has been demonstrated to improve muscle mass and function in dystrophic mice [15][17] and to have beneficial effects on fat and glucose metabolism in mouse models of obesity and type II diabetes [18].

Myostatin is synthesized as a precursor protein that undergoes proteolytic processing to generate an N-terminal propeptide and a C-terminal dimer, which is the biologically active species. Following proteolytic processing, the propeptide remains bound to the C-terminal dimer and maintains it in an inactive, latent complex [6], [19], [20], which represents one of the major forms of myostatin that circulates in the blood [21], [22]. In addition to the propeptide, other binding proteins are capable of regulating myostatin activity in vitro, including follistatin [19], [21], FLRG [22], and Gasp-1 [23]. We previously showed that follistatin can also block myostatin activity in vivo; specifically, we showed that follistatin can ameliorate the cachexia induced by high level expression of myostatin in nude mice [21] and that transgenic mice expressing follistatin in muscle have dramatic increases in muscle mass [19]. Here, I show that overexpression of follistatin can also cause substantial muscle growth in mice lacking myostatin, demonstrating that other TGF-ß related ligands normally cooperate with myostatin to suppress muscle growth and that the capacity for enhancing muscle growth by targeting this signaling pathway is much larger than previously appreciated.

Results

Increased muscle mass in transgenic mice expressing FLRG

Previous studies have identified several proteins that are normally found in a complex with myostatin in the blood [22], [23]. One of these is the follistatin related protein, FLRG, which has been demonstrated to be capable of inhibiting myostatin activity in vitro. To determine whether FLRG can also inhibit myostatin activity in vivo, I generated a construct in which the FLRG coding sequence was placed downstream of a myosin light chain promoter/enhancer. From pronuclear injections of this construct, a total of four transgenic mouse lines (Z111A, Z111B, Z116A, and Z116B) were obtained containing independently segregating insertion sites. Each of these four transgenic lines was backcrossed at least 6 times to C57 BL/6 mice prior to analysis in order to control for genetic background effects. Northern analysis revealed that in three of these lines the transgene was expressed in skeletal muscles but not in any of the non-skeletal muscle tissues examined (Figure 1); in the fourth line, Z111B, the expression of the transgene was below the level of detection in these blots. As shown in Table 1, all four lines exhibited significant increases in muscle weights compared to wild type control mice. These increases were observed in all four muscles that were examined as well as in both sexes. Moreover, the rank order of magnitude of these increases correlated with the rank order of expression levels of the transgene; in the highest-expressing line, Z116A, muscle weights were increased by 57–81% in females and 87–116% in males compared to wild type mice. Hence, FLRG is capable of increasing muscle growth in a dose-dependent manner when expressed as a transgene in skeletal muscle.

The research was funded by grants from the NIH and the Muscular Dystrophy Association and by a gift from Merck Research Laboratories.

See http://www.jhu.edu/sejinlee/%20for%20more%20information for more information.
Citation: Lee S-J (2007) Quadrupling Muscle Mass in Mice by Targeting TGF-ß Signaling Pathways. PLoS ONE 2(8): e789. doi:10.1371/journal.pone.0000789

LINK TO THE PUBLISHED ARTICLE http://www.plosone.org/doi/pone.0000789

Source: Nick Zagorski
Johns Hopkins Medical Institutions