The Boirie Interview - Part 1

[admin]

The truth is out there!

Next time you’re in a restaurant and getting set to tear into that juicy New York strip, stop for a moment, -get a grip! Don’t you realize that you can’t digest more than thirty grams of protein in one sitting? Haven’t you ever heard that you need to consume protein every three hours to provide the optimal anabolic environment for muscle growth? Were you perhaps on another planet when they told the rest of us that whey is the ideal protein source for muscle growth?

If you answered yes to any of the above (except that last one), I want you to think hard about where you heard these “facts”. In truth, this information has circulated around gyms for so long now that you probably don’t remember the “where” or “when” anymore. I swear, I’ve even heard pro bodybuilders recite these statistics in seminar, only to state in their next breath that they consume at least one and a half grams of protein per pound of bodyweight a day. Trust me, when a 300 lb bodybuilder passes on such nutritional pearls of wisdom and you find the penny doesn’t drop, it can only reveal one of two things:

A. You’re desperate for knowledge but definitely not the sharpest tool in the box, or:

B. The life of a Pro bodybuilder has its drawbacks, -no sleep and a 45-hour day that revolves around cleaning a blender!

Could it be possible that these statements, the ones that you’ve always believed to be set in stone, are not facts? Well that all depends on your definition of a fact. If, like me, you believe that it’s something supported by credible scientific studies, the revelation of years of trial and error or even just an obvious conclusion, then these statements fall far short. For the most part, they are the philosophy passed down from the well-meaning gurus (Rheo Blair, Vince Gironda et al) of a bygone age, devoid of the technology and access to information that spoils us now. In order to progress faster, you need to open your mind, -take these “urban protein myths” and file them somewhere between Roswell and The Yeti.

Today, with the gigabyte-sized results of countless scientific studies swelling the world’s medical databases to bursting point, we ought to be hearing the truth, right? You’d think. Unfortunately, honest intentions have now given way to dishonest marketing hype. Your vulnerability stems from the fact that most research on protein metabolism never involved athletes, unless of course “athlete” is a pseudonym for “rat with short-bowel syndrome”. With no drug or product to be licensed from its conclusions, there’s little or no commercial application to fund such research. Most supplement companies could never support the huge costs involved with conducting a legitimate scientific study, -a figure that could probably buy-out most of their rivals! Instead, many have now opted for deception, -a tried and trusted formula. They mislead with bogus studies that produce the kind of results drug companies could only dream of. This form of unethical advertising obviously preys on the young and the naïve. However, for the more discerning athlete, the perpetrators simply desecrate the limited relevant material available by adding their own tainted interpretation. With the contortion skills of Houdini and the slipperiness of a mafia defence lawyer, they’ll present only what they want you to see, confident in the fact that most never bother to read the small print (the references). So what does all the research really tell us? Where do we look to find the truth? Whose work can we actually trust anymore? Enter Yves Boirie.

Over the last three years, there can have been no scientist whose work on dietary protein has been more referenced than that of Yves Boirie. It all started with an article that appeared in a 1998 edition of the now defunct PEAK TRAINING JOURNAL, a hardcore think-tank for some of the industry’s more “out there” authorities. The article, titled “Whey out of line”, was written by Jeff Feliciano, a straight-talking science writer/researcher who crusades directly from the trenches. In true PEAK fashion, Feliciano pulled no punches as he spilled the beans about the whole issue of protein quality and the whey/casein controversy. For my money, that article was worthy of a Nobel Prize. As supporting evidence for the case against the protein moguls, Feliciano referenced a particular study titled “Slow and fast dietary proteins differently modulate postprandial protein accretion”. This was the first place we would see the name Yves Boirie.

Further articles followed, as the unrelenting Feliciano was joined in his campaign by other boffins, including Dr. Jim Wright, the “heavyweight” Science Editor of FLEX and one of the most respected individuals in the game. Boirie’s studies soon became the common denominator in all quality protein articles (not to mention most protein quality articles!). Through the pages of FLEX, IRONMAN, PEAK and PLANET MUSCLE, we became privy to perhaps the most significant and thought-provoking discoveries about protein metabolism yet. However, magazines float on advertising bucks and within the industry these revelations were extremely unpopular (you’ll soon understand why). Often times, having the balls to tell the truth can equate to financial Russian roulette (R.I.P. Peak).

Why did the work of Monsieur Boirie and his colleagues ruffle so many feathers? Apparently, the open contempt for regulations and moral barriers displayed by the “snake oil salesmen” belies their sense of security. The problem here was that Boirie brought a different kind of science to the table, -one that came with a totally different kind of message.

In the 1997 paper referenced by Feliciano and others, we weren’t to find elderly, sick, injured or even half-starved subjects being employed, -a set of circumstances that may allow nutritive value to be derived from chewing on an old lifting belt! On the contrary, Boirie and his team would go out of their way to make sure that only young healthy and well-fed individuals were used.

Basically, what this study did was look at how the amino acid absorption rate may influence the amount of protein synthesized, broken down and actually retained from a particular meal. A comparison was made between a “fast” and a “slow” protein source, whey and casein represented examples of each. To present as accurate an assessment as possible, five separate protocols were performed. These protocols involved the use of an i.v. metabolic tracer (a stable isotope, -in this instance 13C-leucine) to observe the fate of the amino acid leucine. In two of the protocols, the tracer was also actually incorporated into the protein source. With such studies, whole body leucine balance is generally accepted as an index of protein deposition. At this point, anyone would easily be forgiven for asking how the hell you go about incorporating an isotope into a dairy protein. Unbelievably, precise quantities of labelled whey and casein were obtained by using a previously developed methodology where lactating cows were infused with the tracer. Who said protein supplementation isn’t rocket science?

[admin]

The ingenuity, expertise and integrity of those who conducted this study are beyond dispute. Yves Boirie MD is Assistant Professor at the University of Clermont-Ferrand, France. Specializing in endocrinology and nutrition, he currently works in the Protein-Energy Metabolism Unit of the prestigious Human Nutrition Research Centre, based in Clermont-Ferrand. The director of the unit is Professor Bernard Beaufrere, himself an authority who, along with several other members of the team, has conducted a mountain of research on just about every single aspect of protein metabolism. Over the years, their work has looked at the influence of such diverse factors as age, exercise, feeding pattern and the administration of GH and IGF-1. Most of the teams work is based on in vivo investigations using labelled amino acids (tracers).

OK, so now you’ve got the picture, -this study was thorough with a capital T. The messages given off by its results are just as crystal clear, but I’m going to leave the explaining to Yves Boirie. My reason for this is that even this study, which isn’t really open to interpretation, has become the victim of yet another “hatchet job”. Basically, several companies have put their own unique twist on one particular statement from the study (regarding protein synthesis) and used it as an endorsement for their whey products. After becoming aware of the situation, Monsieur Boirie was less than happy. So displeased was he, that he has since declined to be interviewed by any bodybuilding magazine or enter into any correspondence with anyone representing a sports nutrition company, -until now.

I had conversed with Yves Boirie several times over the early part of this year, during which time I expressed a sincere interest in conducting an interview with him. Like many others in the field, I realised that he had hit on something vital here, something too important to be left at the mercy of the sharks that dog our industry. Having previously familiarised myself with most of the teams’ work, I was totally aware that the 1997 paper may not be the only valuable contribution. Indeed, some of their other studies could also hold the key to solving bodybuilding’s greatest conundrums. After an assurance that my interest was academic and in no way commercially motivated, I couldn’t believe my luck when he finally agreed to an interview. As far as I was concerned, this was an opportunity not to be missed! The necessary arrangements were promptly made and, less than one month later, I travelled to Clermont-Ferrand to meet him.

On a sunny spring afternoon, the interview was commenced in an informal atmosphere over lunch. Later that same day, we took it back to the Human Nutrition Research Centre, where the real “meat and bones” of the issue would be discussed. One thing that impressed me above all else about Boirie was his commitment to his work. This wasn’t a man who cared one iota for solving the relatively petty disputes of our industry. This was a man with a far nobler objective, - improving the quality of human life through nutrition.

Before we get down to the dialogue, I would like to point out that this article isn’t about whey, casein or the superiority of either. As Boirie and his team have evidenced, both are quality proteins with individual properties, making each suitable to a different and even possibly a common set of circumstances. What this article is about is having the opportunity to let a real expert explain exactly what he means, in his own words and in a concise manner.

The Boirie Interview; part one

The following is the first part of my interview, where we discussed the studies that looked at the “fast” and “slow” protein concept.

BB: In your 1997 paper “Slow and fast dietary proteins differently modulate postprandial protein accretion”, it’s indicated that casein is superior to whey at maintaining positive nitrogen balance over longer periods. The study also indicates that casein had anti-catabolic effects, demonstrated by a 34% inhibition of whole body protein breakdown, and that whey however, did not. Do you feel that this represents an accurate conclusion from the results?

YB: Yes. This was significant, because in this paper we have shown that you could highly stimulate protein synthesis at a whole body level. You could dramatically stimulate protein synthesis with a whey protein, but if you don’t change protein breakdown, the final balance may still be even negative. It is important to not only have an impact on the protein synthesis, but also the protein breakdown. This is an exact example of the situation, because here the casein did not increase to the same extent the synthesis, but protein breakdown was decreased. Therefore, the final balance was better for the casein meal because of the inhibition of protein breakdown.

BB: So the whey protein had no effect on protein breakdown?

YB: Absolutely none. It was really intriguing because in other studies using stable isotopes, we gave small repetitive meals, mimicking a “slow” protein, and all the studies in this area have shown an inhibition effect of the meal. This is almost the only study showing that one protein meal has no effect on protein breakdown, and I think this is because of the kinetics study that we did. All the other studies just looked at the steady effect of a meal, and the effect is different when you have a big (fast) absorption, it is completely different.

Many people also argue that the insulin secretion caused by the different proteins could have an effect on the protein breakdown. However, we had very little insulin stimulation, -it was no different for the whey than the casein. Everyone will tell you that insulin is able to inhibit protein breakdown, but this small increase in insulin secretion had no effect. Although the magnitude of amino acid concentration may be important, this study demonstrated that the most important thing (to influence protein balance) is the duration of amino acid elevation.

BB: That’s very interesting. Today, many sports nutrition companies promote whey as an anticatabolic protein, yet your study clearly indicates that a single feeding of whey does nothing to prevent protein breakdown.

[admin]

YB: That is correct, from what has been demonstrated at the whole body level.

BB: Are you familiar with the term micellar casein?

YB: Yes, this is the native casein, where the alpha, beta and kappa forms are represented.

BB: In the 1997 study, is the casein that was used micellar casein, - casein in the micelle structure from bovine milk (as opposed to regular calcium caseinate)? You indicated earlier that this could have some effect on the results?

YB: Yes, -as I told you earlier, we used a native protein. The protein we used here was obtained after filtration, after membrane micro filtration for the casein and after ultra filtration for the whey. So we did not use a precipitated (acid treated) casein, as this would not have given us the correct morphological behaviour. In the stomach, where you have an important acidity, you would have a clotting of the casein. However, if you use casein that is already clotted, it could behave differently, you would not get the same coagulum.

BB: So you thought that the positive benefits from the casein may in part, have been attributable to the fact that it was a native milk protein, in its micellar form. In at least one of your studies, you mention that there are active opiod regulatory peptides contained in some of the micellar casein fractions and that these may play a role by influencing gastrointestinal motility.

YB: Its difficult to answer this question for definite, in other studies, we found that even using calcium caseinate could behave similarly. I think it is an important issue that needs to be determined by us all.

BB: Have you or your colleagues performed any other studies on protein accretion in healthy adults?

YB: Yes, we have done a study looking at the effects of insulin without any amino acid profiling. It was a study performed with young people and we showed that insulin has absolutely no effect at the whole body level on protein synthesis, -only an effect on protein breakdown. However, elderly people have less response to insulin, and this could be very important.

BB: They are more insulin resistant?

YB: Yes. This could be important to prevent sarcopenia in elderly people. We did another study where carbohydrate was added to the protein meal and it may, for example, answer some of your questions on the combination of protein and carbohydrates or protein and lipids. The question is, do we have the same sparing effect with carbohydrate or fat with protein? We are communicating with the European Society for Nutrition in Munich, we will shortly publish this.

BB: Excellent, that should be very interesting.

YB: Actually, I can give you some indication that there is a sparing effect of carbohydrate and also from fat.

BB: Exactly what kind of effect? What type of carbohydrate did you use - was it simple or complex?

YB: You will have to wait and see!

BB: In February 2001, you published a study titled “The digestion rate of protein is an independent regulating factor of postprandial protein retention”. Once again, this looked at the link between digestion rate and protein deposited. As you pointed out in the first study, amino acids are potent modulators of protein synthesis, breakdown and oxidation, so it may have been possible that different amino acid profiles could yield different results?

YB: This was an important study to us. After the publication of the 1997 paper, some people could argue that the differences between the whey and the casein were attributable to the differences in amino acid composition i.e., this could explain the difference in protein balance.

BB: So in simple terms, what you were trying to determine was whether it was the digestion rate and not the amino acid profile that accounted for the different results?

YB: Yes, the different results and responses.

BB: In this study, you employed four groups of six healthy young men, each group following a different protocol. The first group consumed 30 grams of micellar casein, a “slow” protein. The second group were given 30 grams of a free-form amino acid mixture that mimicked the casein amino acid profile; this represented a “fast” protein source. In the third group, 30 grams of whey were given, -another “fast” protein. Finally, the fourth group were given 13 small whey protein meals, 20 minutes between each, over a period of 4 hours. The thirteen meals totalled 30 grams and represented another “slow” meal. Briefly, what were the results of this study?

YB: First of all, leucine oxidation was dramatically decreased with the protocol that involved multiple small feedings of whey when compared with a single whey feeding. The same situation was found when we compared the single feeding of casein with the amino acid mixture that mimicked the casein profile. The utilisation of the protein from the meal is not really the result of the amino acid profile, but merely a case of the digestion rate.

[admin]

BB: And the postprandial leucine balance was therefore, higher for which meals, - the slower ones?

YB: Yes that is correct. Also with regards to protein breakdown, this was significantly inhibited only by the slow meals.

BB: So basically, the findings from the 2001 paper confirmed the previous findings established in the 1997 study?

YB: Yes, it was exactly consistent with the first study.

BB: In that 2001 paper, it was stated that in young adults, slow proteins fared better with respect to postprandial gain, which is exactly the same finding with the earlier paper.

YB: Correct.

BB: From a practicality point of view, if we look at your studies, and those of your colleagues what type of bovine milk protein do you think provides the best overall efficiency of utilization in the human body? Would it not appear to be the casein?

YB: Yes, from a practicality point of view. But you will not have the same amino acid concentration in the blood and stimulation of synthesis, which may be of specific benefit in some circumstances. The best protein for human use would have a balanced logical amino acid profile, with good bioavailability and inducing good amino acid synthesis at the right time and in the right tissues, because we are concerned with muscle tissue here and not splanchnic tissue. Also, it should have an impact on protein breakdown, but we also have to look at what happens in regards to protein turnover if we consume a large quantity of that particular protein (as would a bodybuilder). When you consume a large amount of protein, you increase protein turnover and this costs a lot of energy, not only for protein synthesis, but also for protein breakdown. People do not realize the energy expense of protein breakdown.

BB: In some circumstances, the rate of synthesis could be a critical factor. For example, for an athlete after he has competed or after training, am I right in making that conclusion? If we look at whey protein, being a fast protein, this may be beneficial immediately post-workout, as a fast influx of amino acids may be required.

YB: It may be.

BB: Could it perhaps be just as logical to assume that if a slow protein had been consumed at the appropriate time prior to exercise, this could have averted catabolism?

YB: As I told you earlier, muscle sensitivity is higher after a bout of exercise, so it could be important to increase the availability of amino acids to the muscle then. All I can tell you is that whey is more rapidly absorbed and that it appears to stimulate synthesis. However, your theory about taking a slow protein may well also have an impact on protein synthesis after the exercise. This is interesting, we have a similar situation where many people are looking at this protocol as a preparation for surgery. We know that after surgery there is a kind of insulin resistance, so people have shown in Sweden that if you preload with glucose prior to surgery, then you have a better insulin sensitivity after that surgery. So we could possibly have exactly the same situation with the preloading of amino acids that you mentioned (consumption of a slow protein); we could modulate the post-operative period by modulating the pre-operative period. It is very impressive the effect that can be achieved after surgery, previously I was never really convinced by this theory, but now I am totally convinced.

BB: What I am actually trying to say about these protein sources, or rather what I am trying to elucidate, is that basically neither of these proteins are inferior, -they are each suitable to different situations/conditions. Is that correct?

YB: Absolutely.

BB: So there may be a situation where the priority is to stop protein breakdown and there may be another set of circumstances where the priority is to deliver amino acids fast?

YB: Yes, absolutely.

BB: Therefore, whey and casein both have their own unique attributes that could contribute to the various situations faced by an athlete?

YB: That is correct, but it is important to remember that even if a protein is a slow protein, if muscle sensitivity is increased, the body will be able to make full use of the amino acids as and when required.

BB: If we take a look at the individual properties of each protein source, e.g. digestibility, effects on synthesis, breakdown, deposition, etc., do you feel that it would be an obvious conclusion that the situation would be improved by combining the two protein sources (whey and casein)?

YB: I think this is right. This is why native milk protein is such a very good protein, - it’s perfect. First we have the fast release of amino acids and then, when these start to disappear, those from the slower casein pick the situation up. Also, the fast protein would boost the synthesis of the flood of amino acids, while the slow protein will slow down the protein breakdown. This combination is a perfect one.

BB: What about species specifity, after all, bovine milk is vastly different to human maternal milk?

YB: Yes, that’s correct, there are only 5 grams per litre of whey and 25 grams per litre of casein in bovine milk.

BB: So do you feel that there may be a more specific ratio of whey to casein that is more suitable to use by humans? If we look at the 60:40 ratio that occurs in human maternal milk, is it not possible that this may be a more appropriate ratio for the athlete?

YB: You are absolutely right, and some companies are already looking at these ratios. There are patents being applied for in this area by some companies, not for sports nutrition products, but for products intended for clinical use. This is a very exciting area of investigation, and I think we are at the beginning of a whole new period of development.

So, there we have it for part one. In part two, we’ll stir up even more controversy when we introduce you to a concept that’s so radical it may well turn conventional protein supplementation theory totally on its head!

Until then, -open your mind!