High protein diets and BCAA supplementation: overdoing it

[NumberTwentyTwo]

I know that Tans_Isomer is big on the no protein before or during exercise because of it increasing cortisol levels. Well Im wondering if we are overdoing the protein and if it actually becomes more catabolic than anabolic. Sounds like a really stupid question, I know.

Also BCAAs during exercise. Dont BCAAs just turn into glucose via glycolosis? If so what would be the point to use them during exercise (especially in a cutting phase).

From what Im seeing Im thinking moderate protein intake and increased Leucine intake is the way to go....


Before you all call me a NEWB....something from Nandi that I found on another board

"So lots of peopel our builiding up ICE and rightfully so, it is a very good product. The thing is though...it seems that loading up on BCAA's would be awesome for dieting, their anti-catabloic /anabolic actions would make it great to take in between meals and keep muscle wasting at an absolute minimum. However with BCAA's increasing Insulin release, wouldn't they be counter productive to fat loss goals...just looking for others thoughts.."

Quite possibly. Amino acid infusions produce insulin resistance:

" A approximately 2.1-fold elevation of plasma anabolic steroids [amino acids] reduced whole-body glucose disposal by 25% (P < 0.01). Rates of muscle glycogen synthesis decreased by 64% (180--315 min, 24 plus minus 3; control, 67 plus minus 10 micromol center dot l(-1) center dot min(-1); P < 0.01), which was accompanied by a reduction in G6P starting at 130 min (DeltaG6P(260--300 min), 18 plus minus 19; control, 103 plus minus 33 micromol/l; P < 0.05). In conclusion, plasma amino acid elevation induces skeletal muscle insulin resistance in humans by inhibition of glucose transport/phosphorylation, resulting in marked reduction of glycogen synthesis. (1)

The resulting insulin resistance would be expected to lead to hyperinsulinemia and impaired lipolysis.

An even more interesting question ( in my mind ) is to what extent the resulting insulin resistance affects protein metabolism. If a person is insulin resistant with respect to glucose, are they also insulin resistant with respect to the anabolic effects of insulin? The answer may be yes, at least somewhat.

Resistance to glucose uptake evidently does not affect amino acid uptake; the transport systems are different (2). So amino acid transport seems to be the same in normal and insulin resistant people, and the stimulatory effect of hyperaminoacidemia on protein synthesis is the same as well. However, what appears to be different is that in insulin resistance, the antiproteolytic effect of insulin is lost, at least in the research presented here:

"In conclusion, insulin resistance is a common feature of both glucose and protein metabolism in obesity. The defect in protein metabolism is characterized by an impairment of the ability of insulin to inhibit proteolysis; the stimulatory effect of hyperaminoacidemia on protein synthesis is intact in obesity." (3)

So it seems, ironically, that a high protein diet could actually lead to a catabolic state. This is especially true in light of the fact that a high protein diet induces subclinical metabolic acidosis, which raises cortisol levels."

(1) Diabetes 2002 Mar;51(3):599-605

Mechanism of amino acid-induced skeletal muscle insulin resistance in humans.

Krebs M, Krssak M, Bernroider E, Anderwald C, Brehm A, Meyerspeer M, Nowotny P, Roth E, Waldhausl W, Roden


(2) Diabetes 1993 Dec;42(12):1868-77

Different sensitivity of glucose and amino acid metabolism to insulin in NIDDM.

Luzi L, Petrides AS, De Fronzo RA


(3) Am J Physiol 1996 Feb;270(2 Pt 1):E273-81

Insulin and hyperaminoacidemia regulate by a different mechanism leucine turnover and oxidation in obesity.

Luzi L, Castellino P, DeFronzo RA




"Most athletes take in more protein than they need. Especially without a buffering protocol, the resulting acidosis is quite catabolic. The insulin resistance only adds insult to injury. This is especially true in anabolic steroids using athletes who are already experiencing some degree of AAS induced insulin resistance. Moreover, there is evidence that AAS users require LESS protein than non users becuase the cells become much more efficient at recycling amino acids.

BCAA supplementation is a waste of money, IMHO, and probably detrimental as well."

[dan7681]

I know that Tans_Isomer is big on the no protein before or during exercise because of it increasing cortisol levels. Well Im wondering if we are overdoing the protein and if it actually becomes more catabolic than anabolic. Sounds like a really stupid question, I know.

Also BCAAs during exercise. Dont BCAAs just turn into glucose via glycolosis? If so what would be the point to use them during exercise (especially in a cutting phase).

From what Im seeing Im thinking moderate protein intake and increased Leucine intake is the way to go....


Before you all call me a NEWB....something from Nandi that I found on another board

You NEWB

Can't really answer your question. But I do know leucine and protein is def a good way to go.

I usually just like taking (when I do) BCAAs pre and post workout but am interested to hear what the opinions of others.

[pu12en12g]

I think Beast has a good way of breaking it down with the big picture in mind:

http://forum.bodybuilding.com/showpo...&postcount=190

Note the nutrient timing logic towards the bottom.

The thing about Derek / Beast is that he has the knowledge AND the physique, yet he doesn't claim to know it all or overanalyze like some.. he's the real deal.

[JRRBadBoy4Life]

increased Leucine intake is the way to go....

Exactly. Very cheap, certainly worth a shot.

[NumberTwentyTwo]

I think Beast has a good way of breaking it down with the big picture in mind:

http://forum.bodybuilding.com/showpo...&postcount=190

Note the nutrient timing logic towards the bottom.

The thing about Derek / Beast is that he has the knowledge AND the physique, yet he doesn't claim to know it all or overanalyze like some.. he's the real deal.

what is keeping the bcaa from turing into glucose via glycolosis?

especially while megadosing

[pu12en12g]

what is keeping the bcaa from turing into glucose via glycolosis?

especially while megadosing

Because we're specifically using FREE FORM aminos... this is exactly where most people get sidetracked or confused a bit. It's the FREE FORM aminos and the timing here that are important.

Unlike whey, the FREE FORM aminos basically bypass digestion

When whole protein is eaten, it must be broken down into individual amino acids before they can pass into the blood and into the circulation to be used as needed. Free-form amino acids are in their individual amino acid form and do not require digestion before transportation into the blood. Once amino acids are in the blood and extracellular fluids, they make up a large group called the amino acid pool or free pool. This pool also contained amino acids that were catabolized from other tissues and those created in the liver. Amino acids are constantly entering and leaving this pool.

The largest amount of protein in the body is in the form of muscle. When amino acid requirements are not met, muscle is broken down into amino acids, which are then sent to the amino acid pool to be used accordingly.

Here is how MCT's can come into play:

During resting periods when other fuel sources, such as carbohydrates and fats, are available they spare the BCAA's from oxidation, leaving them available for use in protein synthesis which is what you want them to do - serve you by building muscle. The important thing is that although BCAA's account for only about 20% of the total amino acids in a protein meal they account for 50-90% of the total amino acids released into general circulation to be taken up by the muscles. BCAA's are the most abundant amino acids incorporated into muscle protein and make up 1/3 of this muscle.

They are also heavily catabolized (broken down and used for energy) during exercise. These 2 reasons plus the fact that the body can't make it's own BCAA's increases the need for BCAA's for athletes.

Why all FREE FORM EAA's and not just Leucine ?

The role of leucine in the regulation of protein metabolism.

Nutr. 2005 Jun;135(6 Suppl):1553S-6S.

Garlick PJ.

Department of Animal Sciences, University of Illinois, Urbana, 61801, USA. pgarlick@uiuc.edu

Studies both in vivo and in vitro have shown that leucine at a very high dose can stimulate muscle protein synthesis, an effect that is enhanced in vivo by insulin secreted in response to the leucine dose. High leucine can also inhibit protein degradation in skeletal muscle, as well as in liver. In contrast, at normal physiological levels, increasing leucine concentration by infusion stimulates muscle protein synthesis by enhancing its sensitivity to insulin. It is concluded that the role of leucine in vivo is to provide a signal that amino acids are available, which in combination with the signal of energy availability from insulin, stimulates muscle protein synthesis.

[pu12en12g]

http://forum.bodybuilding.com/showpo...83&postcount=5

http://forum.bodybuilding.com/showpo...6&postcount=28

[pu12en12g]

Amino acids regulate skeletal muscle PHAS-I and p70 S6-kinase phosphorylation independently of insulin.
Long, W., L. Saffer, L. Wei, and E. J. Barrett. Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908

Refeeding reverses the muscle protein loss seen with fasting. The physiological regulators and cellular control sites responsible for this reversal are incompletely defined. Phosphorylation of phosphorylated heat-acid stabled protein (PHAS-I) frees eukaryotic initiation factor 4E (eIF4E) and stimulates protein synthesis by accelerating translation initiation. Phosphorylation of p70 S6-kinase (p70S6k) is thought to be involved in the regulation of the synthesis of some ribosomsal proteins and other selected proteins with polypyrimidine clusters near the transcription start site. We examined whether phosphorylation of PHAS-I and p70S6k was increased by feeding and determined the separate effects of insulin and amino acids on PHAS-I and p70S6k phosphorylation in rat skeletal muscle in vivo. Muscle was obtained from rats fed ad libitum or fasted overnight (n = 5 each). Other fasted rats were infused with insulin (3 muU×min«minus»1×kg«minus»1, euglycemic clamp), amino acids, or the two combined. Gastrocnemius was freeze-clamped, and PHAS-I and p70S6k phosphorylation was measured by quantifying the several phosphorylated forms of these proteins seen on Western blots. We observed that feeding increased phosphorylation of both PHAS-I and p70S6k (P < 0.05). Infusion of amino acids alone reproduced the effect of feeding. Physiological hyperinsulinemia increased p70S6K (P < 0.05) but not PHAS-I phosphorylation (P = 0.98). Addition of insulin to amino acid infusion was no more effective than amino acids alone in promoting PHAS-I and p70S6k phosphorylation. We conclude that amino acid infusion alone enhances the activation of the protein synthetic pathways in vivo in rat skeletal muscle. This effect is not dependent on increases in plasma insulin and simulates the activation of protein synthesis that accompanies normal feeding.

Interesting one

[NumberTwentyTwo]

I still think that megadosing is a waist. Im gonna look into some studies and get back at this.....

[deserusan]

I still think that megadosing is a waist. Im gonna look into some studies and get back at this.....

I agree with you completely and if you want the full studies just ask. I've dropped my BCAA intake a lot and still noticing the same effects. While I don't agree with Tranny's position with regards to GH release I do feel megadosing is a waste.

Also, to everyone posting, please don't post abstracts to studies that you haven't read. It's an insult to people who can actually comprehend the difference between a single sentence conclusion and the methods, materials, and full discussion which lead to abstract conclusions. They are usually a poor indicator of how the hypothesis was proven or not. It looks like we need the science police here to call bull**** once again.

[pu12en12g]

I still think that megadosing is a waist. Im gonna look into some studies and get back at this.....

Yep, I wouldn't megadose above 20g EAA at one time... and that time obviously needs to be pre-workout or pre-cardio.

[JRRBadBoy4Life]

Also, to everyone posting, please don't post abstracts to studies that you haven't read.

I'm finding that most studies are bull****. Many contradict one another and are pretty worthless to read. I'd rather trust my own body and see what works for me than spend hours doing research on garbage studies.

[deserusan]

I'm finding that most studies are bull****. Many contradict one another and are pretty worthless to read. I'd rather trust my own body and see what works for me than spend hours doing research on garbage studies.

I read the studies and pay attention to my body. It's hard to discern the bodybuilding applications from the raw science because 99.999999% of them do not involve the physiological state most bodybuilders are in. Even trying to seperate studies on athletes and applying it to a physique athlete is hard.

I do see your point though because what is sad is that a lot of studies are misquoted which misguides the consumer. That's why I will only quote something I have read in it's entirety. I actually have quite the library of studies now.

[JRRBadBoy4Life]

Also, if there is a study done for a particular product which involves 100 athletes of varying sports, how closely were those athletes followed? Were they taking any other performance enhancing products? Were they tested for performance enhancing drugs? Just some things to consider when reading studies, not to mention many of the logs kept on here.

[GeneGnomeX]

Yep, I wouldn't megadose above 20g EAA at one time... and that time obviously needs to be pre-workout or pre-cardio.

Sure...if you put all your faith into the Tipton study.

[NumberTwentyTwo]

...

Genernally the oxidation of BCAA's usually correlates to increased gluconeogensis (leucine will be oxidized as a fuel source to spare glucose for use elsewhere). This condition is usually only relevant when dieting. You can eliminate this simply by adding a carb.

As for megadosing, I just don't feel the body can utilize large amounts effectively. A small amount of carbs couple wiht a small amount of BCAA's make the most sense IMO.

[deserusan]

Sure...if you put all your faith into the Tipton study.

I should post up all the Tipton full conclusions. It's quite the laugh when you compare them to the abstract conclusions.

[pu12en12g]

Sure...if you put all your faith into the Tipton study.

Not at all

[bodybuilder45]

well since high protein diets can ultimately lead to higher cortisol levels due to metabolic acidosis, couldnt glutamine be beneficial here for PH balance to reduce acidity? this is what i understand to be the main problem from the starting post. what do you all think?

[hotasice2003]

I read the studies and pay attention to my body. It's hard to discern the bodybuilding applications from the raw science because 99.999999% of them do not involve the physiological state most bodybuilders are in. Even trying to seperate studies on athletes and applying it to a physique athlete is hard.

I do see your point though because what is sad is that a lot of studies are misquoted which misguides the consumer. That's why I will only quote something I have read in it's entirety. I actually have quite the library of studies now.

That's quite a precise number! lol........ if I am not mistaken, most all studies done showing the effects of EAA's on preotein synthesis, only used around 6g EAA's........ do you think this is a sufficient amount? I have been using WPI+ added BCAA's, but am thinking on just doing EAA's, with still a little more added BCAA's....... I sip my cocktail 15min pre-wo, during, and then finish immediately post. I also have 30-35g sugars during, which decreases BCAA oxidation. I guess I am just asking your stance on the whole pre/during/pwo cocktails......

[40-Yard Dash_2]

what is keeping the bcaa from turing into glucose via glycolosis?

especially while megadosing

The fed and fasted states. An adequate amount of stored glycogen and the AA pool determine it. If not enough glycogen in peripheral tissue, then your AA's carbon skeleton will be converted into an intermediate of the krebs cycle. B/c of its cyclic character, once these intermediates enter the krebs cycle they are easily converted to oxaloacetate. Of course we know that OAA is a critical intermidiate in the krebs cycle and that the first step in the cycle involves the combination of OAA and Acetyl-CoA to form Citrate. The production of OAA from AA's means that the cell no longer needs to use as much glucose to maintain adequate leves of OAA in the krebs cycle. This, in turn, means that blood glucose is used more sparingly.

AA breakdown and glc production in the liver: In the fasting state mentioned above, a significant portion of the AA produced by the breakdown of protein in peripheral tissues, such as muscle, is released to the blood. B/c of its very rich blood supply, the liver has excellent access to these circulating AA's. Glc can be synthesized from several key intermediates in metabolism. One of these is from the components of krebs cycle, malate. Just as for OAA, all of the krebs cycle intermediates can be converted to malate. Since the carbon skeletons of many of the AA's are converted into krebs cycle intermediates, they also serve as starting material for the synthesis of glucose. With this in mind, it is easy to now see that AA released from peripheral tissues can be converted to glc in the liver. AA's are released, taken up by the liver, converted into krebs cycle intermediates that are converted to malate, with malate then being used for the synthesis of glc. Well, you get the general idea.

[tweaked17]

I think Beast has a good way of breaking it down with the big picture in mind:

http://forum.bodybuilding.com/showpo...&postcount=190

Note the nutrient timing logic towards the bottom.

The thing about Derek / Beast is that he has the knowledge AND the physique, yet he doesn't claim to know it all or overanalyze like some.. he's the real deal.

good info, that's pretty interesting.

twentytwo, how exactly does a high protein diet increase cortisol production? this is the first i've heard of this

and, as stated, the body will turn to energy from protein (via gluconeogenesis not glycolysis) when glycogen depleted.

[jmaths117@comcast.net_old]

If you are going to use BCAA, use them after you workout, then your body will use them to repair the muscles.

[Guardian]

The problem I think in terms of this entire supplement industry and nutrtion and everything lol is the body is a homeostatic organism. If you eat before bed you will have less growth hormone release. But if you dont eat before bed you have greater chance of catabolism.

If you take cortisol blockers (as I have see my retain log) there is a good chance that test will inevitably fall or lose effect over time if you keep taking the cortisol blocker.

High protein diets have good and bad effects and I wouldnt be surprised if they do raise cortisol.

Through my 4 or 5 years of training experience and experience with diff diets and supplements and so forth take it from me the most important part of bbing is genetics and training protocol. Everything else is considerably less important and often contradicting.