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Expert Q&A


Here at ProSource, we realize the value of proper diet, training and supplementation. Making the right decisions are crucial to your efforts, thus our research and development team is available to enlighten you and dispel any confusion you may have in this ever-changing world of knowledge. Our team consists of handpicked experts who have spent years in the fitness industry studying the effects of supplementation with diet and exercise. They are continually gathering the latest information, based on independent lab testing, field-testing, customer surveys, manufacturing procedures, technical and scientific reviews and clinical studies.

While the ProSource Staff answers many questions, we've also asked leading researcher, strength coach, and dietician Jeff Volek along with members of the ProSource Research and Development Team to answer some of your questions.

E-mail us with any questions you might have on diet, exercise or supplementation and watch for your answer on our web site.


PLEASE CLICK ON A QUESTION TO VIEW THE ANSWER.


Why do I need to worry about slow, medium or fast-acting proteins?


I read your catalogs all the time. Lately, I'm seeing that you guys are really emphasizing ultra-fast-acting proteins like these new hydrolyzed whey products. So here's my question: If I'm consuming protein all day, both from food sources and from protein shakes, don't I always have aminos cruising my bloodstream? If I'm perpetually maxed on bioavailable aminos, why do I need to worry about slow-, medium- or fast-acting proteins? Thanks and keep up the good work!

Even if you have ingested a fair dose of protein before exercise, you will stay in the protein catabolic state after rigourous exercise until you have taken in enough amino acids. You obviously want to switch from the catabolic state to the anabolic state as soon as possible, right? To do so, you need to rapidly elevate blood amino acid and insulin levels (Insulin is an anabolic hormone that helps transport amino acids into hungry muscle cells).

The best way to accomplish this goal is to ingest a serving of BioQuest MyoZene immediately after exercise. This high-tech post-exercise supplement provides an elite form of protein that can be absorbed almost instantly upon ingestion, without going through the normal digestive processes.

Consequently, a massive surge of anabolic nutrients are rapidly transported to muscle tissue, where they help trigger new muscle synthesis at a greatly accelerated rate. In addition to the highest quality whey protein hydrolysate, MyoZene also contains a large dose of added leucine. This branched-chain amino acid is the key regulator of muscle protein anabolism. Finally, MyoZene provides a host of other beneficial ingredients such as glutamine, antioxidants, KIC, etc.

Use of a specialized post-workout supplement such as this is proving to be the edge many bodybuilders need to achieve dramatic muscle gains.
-- answer by: Anssi Manninen, M.H.S.

Anssi Manninen, M.H.S., Ph.D., is a well-published research scientist in the sports nutrition field. He holds an M.H.S. in sports medicine from the University of Kuopio Medical School. Anssi is currently a Ph.D. candidate in the Department of Physiology at the University of Oulu Medical School, studying effects of post-exercise nutritional supplementation on hormonal responses and blood amino acid levels. Anssi is also an Associate Editor for Nutrition & Metabolism, a leading scientific journal in the area of nutritional biochemistry

NOTE: Page 16 of the ProSource Product Guide Vol.7 states that Anssi Manninen has earned his Ph.D. This is a typo. Anssi Manninen is in the process of attaining his Ph.D.

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What is so special about BCAA


The guys in the gym tell me I should be supplementing with BCAA, especially leucine. What is so special about this supplement?

Researchers have known about leucine for decades, but exciting new research has shed a new and broader light on this important health-promoting amino acid. Leucine is one of the essential amino acids, which simply means our bodies cannot make leucine and must get it from dietary sources. Leucine is also the most abundant of the three branched-chain amino acids (BCAA), the other two being isoleucine and valine. BCAA make up a high proportion of the amino acids in muscle. BCAA are also unique because they are the only amino acids that are burned by muscle as fuel and thus both blood and muscle levels decrease after exercise. Leucine in particular is the only amino acid that increases in direct proportion to dietary intake. Historically, amino acids were simply viewed as substrates for making muscle and other body proteins - sort of like the bricks needed to build a house. In the case of leucine, recent investigations have shown multiple roles of this amino acid that go well beyond simply providing material to build muscle.

Leucine and Protein Synthesis

Whether you are interested in building muscle or preventing muscle loss that normally occurs during aging and weight loss, stimulating protein synthesis is absolutely key. It is probably not news that simply consuming protein induces an increase in muscle protein synthesis, which is why protein supplements are popular to consume after exercise. Researchers have begun to refine their knowledge on what it is about protein that stimulates anabolism in muscle. For example, scientists have shown that it is the level of amino acids in the blood that directly boosts protein synthesis in muscles. Specifically it is the amino acid leucine that is most highly related to protein synthesis. In a series of elegant experiments, researchers directly examined muscle protein synthesis after feeding animals various formulations of amino acids and compared them to glucose ingestion. When a complete protein was consumed (one that contains all the amino acids), protein synthesis was increased. When just essential amino acids were provided and the nonessential ones left out, the same increase was noted indicating nonessential amino acids are not required to stimulate protein synthesis. When just the BCAA were given, again there was the same increase in protein synthesis. Finally when just leucine was consumed, yet again protein synthesis increased to the same magnitude. These findings provided strong evidence that leucine was the driving force behind the ability of dietary protein to stimulate protein synthesis.


A series of cellular studies has now clearly shown that leucine directly activates a critical compound in muscle called the mammalian target of rapamycin (mTOR). It turns out mTOR is like a molecular switch that turns on the protein synthetic machinery in muscle and leucine is one of the major activators of mTOR. Thus, leucine not only provides the building blocks for protein synthesis, it also has a critical role in up-regulating the process. For example, even when an overabundance of amino acids are available to provide the building materials for new muscle, adding extra leucine augments protein synthetic rates further. The application of all this work is that adding additional leucine to typical protein beverages is an effective strategy to maximize muscle anabolism after resistance exercise.


Leucine and Body Fat

A large number of studies have shown that high protein diets help spare muscle loss during weight loss. Researchers at the University of Illinois have conducted studies that examined weight loss diets that contained 10 g/day of leucine and 125 g total protein per day with a minimum of 2.5 g leucine at each meal. In two separate studies, this group demonstrated that the high leucine diets resulted in greater weight loss, greater fat loss, and better preservation of lean body mass. In these studies, the high leucine diets also resulted in better glucose control. Finally, a recent animal study showed that doubling leucine intake prevented diet-induced obesity and improved a host of metabolic disturbances.


Practically Speaking

The ideal amount of leucine to take is a matter of debate among nutritionists and scientists. In acute studies, oral intake of as little as 2.5 g of leucine stimulates protein synthesis. For chronic studies, leucine intakes equivalent to 8 or more grams per day are recommended divided so that at least 2.5 g of leucine are consumed at each meal. The best food sources of leucine include any proteins from animals that naturally contain all the essential amino acids. The protein source with the highest leucine content is whey which contains about 10 g per 100 g of protein. Other protein supplements like casein and soy contain less leucine. Leucine can be purchased as a single amino acid and added to other protein sources like whey or casein. One cautionary note: supplementing with just leucine alone will not result in optimal effects if the background diet is low in protein. This is because the other BCAA (isoleucine and valine) will be preferentially oxidized and lead to a BCAA imbalance that compromises anabolism. Thus it is important to consume sufficient protein or at least supplement with all three BCAA if total protein intake is low.

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Are amphetamines in plants?


I heard about a plant that was a natural source of amphetamines - any truth to this?

I’m guessing you are talking about Acacia rigidula (also called blackbrush), a shrub found in southern Texas. Acacia rigidula has been known for some time to contain toxic alkaloids. Sheep and goats that graze on the shrub have developed uncoordinated muscle movements referred to as locomotor ataxia. In an effort to identify potential compounds of the plant that might cause this condition, researchers performed a detailed chemical analysis of leaves and stems from Acacia rigidula. The report published almost 10 years ago indicated more than 40 amines and alkaloids were detectable using highly sensitive gas chromatography mass spectrometer (GCMS). The level of amphetamine was extremely low (11.8 parts per million). The most abundant compound was N-methylphenethylamine (5265), followed by tyramine (1699 ppm), and N-methyltyramine (1238 ppm), and phenethylamine(1136 ppm). With the exception of amphetamines, these compounds are naturally found in foods and extracts. At higher levels they could possess psychoactive effects, but at these very low levels any biologic effects would likely be minimal. There could be side effects with higher intakes of tyramine compounds especially in individuals taking monoamine oxidase inhibitors (MAOIs). The plant does have an interesting mixture of chemicals, but considering the low concentrations and adverse effects seen in animals foraging on the shrub, I don’t think there is any good reason to supplement with Acacia rigidula

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