BCAA's Info and Studies

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BCAA's Info and Studies
BCAA's
*Compiled from multiply web sites and sources


BCAAs prevent protein breakdown, but do not increase protein synthesis.

-Since 1978 a variety of studies have been performed in humans where BCAAs or leucine alone was administrated in varying amounts and durations. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day (B1).

-BCAA infusion in 10 postabsorptive normal subjects causes a 4-fold rise in arterial BCAA levels. Plasma insulin levels were unchanged from basal levels. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by BCAA infusion. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids (B2).

-Short-term (3 to 4 hours) infusion of branched-chain amino acids (BCAA) has been shown to suppress muscle protein breakdown.
An overnight (16-hour) systemic BCAA infusion in 8 subjects increases plasma BCAA concentrations by fivefold to eightfold, and this was associated with a 20% to 60% decline in arterial concentrations of other amino acids.
In the forearm, overnight BCAA infusion resulted in a diminished net release of Phe (-3 +/- 2 v -18 +/- 4 [saline] nmol/min/100 mL, P < .02), and BCAA balance became markedly positive (751 +/- 93 v -75 +/- 30, P < .001) (B4).

-BCAA infusion in 10 postabsorptive normal subjects does not change plasma insulin levels. Skeletal muscle proteolysis was suppressed in the absense of any apparent increase in muscle protein synthesis (B5).

-In humans, infusion of BCAA alone slows skeletal muscle protein degradation, but does not increase protein synthesis. This is perhaps not surprising, as the BCAA also inhibit whole body protein degradation and thereby decrease the arterial concentrations of other essential and nonessential amino acids. This decline may blunt any effect of infused BCAA on protein synthesis by limiting substrate availability and/or interfering with nutrient signaling by other amino acids.
BCAA stimulate the phosphorylation of eIF4E-BP1 and p70S6K involved in activating the mRNA translation apparatus. These results demonstrate that the cellular pathways that regulate translation initiation are, in fact, stimulated by BCAA in humans and suggest a potentially significant anabolic signaling role for BCAA in increasing mRNA translation and protein synthesis. This occurs with increments of circulating BCAA like those seen postprandially, suggesting that this is a normal physiological response.
After a 12 h overnight fast 7 healthy volunteers were adminitered a BCAA infusion for 6 h. Insulin concentrations did not significantly change. BCAA infusion significantly improved forearm phenylalanine balance in control subjects at 6 h (Fig. 4A), although, as we previously reported, it did not increase phenylalanine Rd (B6).

-BCAAs during 1h cycle exercise and a 2h recovery period does not influence the rate of exchange of the aromatic AAs during exercise. In the recovery period, a faster decrease in the muscle concentration of aromatic AAs was found (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise (E5)

-7.5-12 g BCAAs during intense exercise (a 30 km cross-country race and a full marathon) increases BCAA plasma and muscle concentration. In the placebo group plasma BCAA decreased and left muscle levels unchanged. The placebo group showed a 20-40% increase in the muscle concentration of aromatic AAs. BCAA supplementation prevented this increase in aromatic AAs in both muscle and plasma. These results suggest that an intake of BCAAs during exercise can prevent or decrease the net rate of protein degradation caused by heavy exercise (E8).

-Consumption of BCAA (30 to 35% leucine) before or during endurance exercise may prevent or decrease the net rate of protein degradation, may improve both mental and physical performance and may have a sparing effect on muscle glycogen degradation and depletion of muscle glycogen stores (E14).

-77 mg BCAAs/kg supplementation before exercise resulted in a doubling (P < 0.05) of the arterial BCAA levels before exercise (339 +/- 15 vs. 822 +/- 86 microM). During the 60 min of exercise, the total release of BCAA was 68 +/- 93 vs. 816 +/- 198 mumol/kg (P < 0.05) for the BCAA and control trials, respectively. Furthermore, the increased intramuscular and arterial BCAA levels before and during exercise result in a suppression of endogenous muscle protein breakdown during exercise.(E105).

-BCAA activate mRNA translation initiation, but without the anticipated increase in protein synthesis. One possible explanation for this apparent discrepancy is that BCAA inhibit proteolysis and thereby decrease the arterial concentrations of other AA (P4).


Helps in fat loss while cutting

-BCAA supplementation (76% leucine) in combination with moderate energy restriction has been shown to induce significant and preferential losses of visceral adipose tissue and to allow maintenance of a high level of performance (E14).
-In adipocytes from fed rats, the rate of fatty acid synthesis in the presence of glucose and insulin was inhibited 40% by valine (5 mm) (E4).

-Twenty-five competitive wrestlers restricted their caloric intake (28 kcal.kg-1.day-1) for 19 days. A high-BCAA diet provided 4 kg of weight loss, and 17,3% decrease in fat loss. There was no change in aerobic (VO2max) (p > 0.75) and anaerobic capacities (Wingate test) (p > 0.81), and in muscular strength (p > 0.82). (E7).


Nutraceutical Effects of Branched-Chain Amino Acids on Skeletal Muscle1,2,3

Yoshiharu Shimomura*,4, Yuko Yamamoto*, Gustavo Bajotto*, Juichi Sato, Taro Murakami**, Noriko Shimomura, Hisamine Kobayashi and Kazunori Mawatari ...

BCAA catabolism in skeletal muscle is regulated by the branched-chain -keto acid dehydrogenase (BCKDH) complex, located at the second step in the BCAA catabolic pathway. The activity of the BCKDH complex is regulated by a phosphorylation/dephosphorylation cycle. Almost all of BCKDH complex in skeletal muscle under normal and resting conditions is in an inactive/phosphorylated state, which may contribute to muscle protein synthesis and muscle growth. Exercise activates the muscle BCKDH complex, resulting in enhanced BCAA catabolism. Therefore, exercise may increase the BCAA requirement. It has been reported that BCAA supplementation before exercise attenuates the breakdown of muscle proteins during exercise in humans and that leucine strongly promotes protein synthesis in skeletal muscle in humans and rats, suggesting that a BCAA supplement may attenuate muscle damage induced by exercise and promote recovery from the damage. We have examined the effects of BCAA supplementation on delayed-onset muscle soreness (DOMS) and muscle fatigue induced by squat exercise in humans. The results obtained showed that BCAA supplementation prior to squat exercise decreased DOMS and muscle fatigue occurring for a few days after exercise. These findings suggest that BCAAs may be useful for muscle recovery following exercise.

 

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The Bigger Picture. Indeed, you may be as surprised as i was on first learning a more accurate answer to "what is protein for" is really "everything." - Just consider this list of what requires protein or just IS protein.

collagen, hair, skin, bone middles - all big huge protein components
every cell in the body EVERY cell requires protein to be replenished or replaced
muscles for sure, but organs too: protein protein protein.
the instructions for our dna, which inhabit cells, are proteins. The genetic code in the the ribosome (beside-ish the cell nucleus) for which all the recent research about "gene expression" comes, is protein.
hormones like insulin - the messengers of what to do in terms of chemical processes to stop and start - are proteins
enzymes that are essential to metabolism and respond to hormone messages, yes, protein. Indeed there are 6 types of enzymatic reactions for moving, rearranging, breaking for reforming, joining, oxidizing. All proteins. Some are also faster others slower for limiting the rate of change. Amazing proteins.
antibodies for defending our cells against infection- more proteins.
energy - yes, sometimes we need/use proteins to produce the ATP we need (usually refered to as "energy" ) to be able to move our muscles.
Isn't that amazing? Are you amazed? I'm so amazed. But wait! There's more if we want to look at protein as macronutrient and how we get it out of food sources to join this functional dance - of which muscle building seems to be quite a ways down the stack of protein's things to do.

The Primacy of Protein
Like fat and carbs, protein has carbon and hydrogen. Unlike fats and carbs, protein has Nitrogen (part of their amino group). And here we get to the interesting bits. Just a reminder, nitrogen is fundamental to life (overview of nitrogen's role). This without nitrogen no life, and protein being in everything kinda hints at the reason perhaps for protein being called PROTEIN. As per this definition:


1844, from Fr. protéine, coined 1838 by Du. chemist Gerhard Johan Mulder (1802-1880), perhaps on suggestion of Berzelius, from Gk. proteios "the first quality," from protos "first." Originally a theoretical substance thought to be essential to life, the modern use is from Ger. Protein, borrowed in Eng. 1907.

Proteins are constructed things:
The smallest protein is an Amino Acid. When little groups get together to make bigger groups we get Peptides, which form up as peptide chains these in turn are bended and folded and twisted into various shapes that make it usable for whatever role these proteins have before they begin their new life as food.


What Happens to Protein in Digestion and Beyond?
What happens when we eat protein? First, most of the time we eat food that has protein in it, right as opposed to just "protein"? So, chew chew chew, masticate, get food into bits with saliva; then food into stomach.

Stomach As food hits the stomach, hydrocholoric acid gets dumped on it, which does interesting things to all food, but to protein it has the special process of denaturing the folded bendy structures of the proteins. While these structures are important for proteins to do what they do when in living cells, for use as food, these structures need to be, well, unpacked.

So, for the purposes of getting at the amino acids, denaturing starts hiving off the other bits of the protein structures that can be used for other things. (By the way, cooking and salting can also denature parts of proteins' stuctures in food).

So acid in the stomach is one part of the stomach process. But in the amazing life of proteins as doers of everything, other proteins-as-enzymes (pepsinogen into pepsin) get happening in the stomach to break the chains of amino acids that have been unpacked from the folds and bends. The remaining "polypeptides" and single amino acids head to the small intestine.


Small Intestine I dunno about you, but the way i've imagined the small intestine is just food getting pushed through a pipe. The stomach's a tank and the intestine's a pipe. Well, no. It turns out the small intestine is more like a conveyor belt where mechanisms operate at each stage on food that keeps processing and changing (metabolizing) the stuff that's in it.

If we're taking stuff apart, we're using enzymes (more proteins), and the small intestine is, in part, doing more disassembling. The pancreas kicks proenzymes into the small intestine, these get going with other enzymes that together act as the un-superglue of peptides. Now we get smallers peptides and free amino acids heading for absorption.

Absorption and Over Crowding at the Border
Ok, i admit it, this next bit seems extremely cool to me and may even have practical implications for those of us who like to experiment with supplements. The small intestine has linings and stuff has to move through the linings to get to the blood stream. Before the proteins get into the next phase of processing (into the blood stream and most thence to the liver), they need to be transported. We won't go into it, but there are four types of transport processes, and each require energy - ATP (the stuff also used for things like muscle contraction) to do the job. So right there is an example of why just staying alive burns calories: moving amino acids out of the gut takes energy.

And by now, you guessed it, those transporters are also proteins. So here's the situation: there's proteins in the gut waiting to get moved to the blood supply. Peptides, branch chain amino acids, individual free form amino acids. They need transporters to take them there. There's a limited number of transporters at any one time and of any one type. We literally can get into a state of cuing up and overcrowding. Which peptides/amino acids go first? It ain't free form amino acids. Nope. It's the branch chain amino acids - these bigger groups take different transporters which seem to head out first. Which is better than being caught in traffic. So next time someone talks about using bcaa's to get to their muscles fast after a hard workout, you know they're not kidding: bcaas it seem can get on the bus out of the gut quite effectively. The ones that get out, that is.

The Liver A lot of the absorbed amino acids (like glutamine) get used right there for energy and intestinal cell growth. If an amino acid makes it past being used for energy or local (non skeletal muscle ) cell building (and only about a fifth of proteins ingested do), it heads into the blood stream into the amino acid pool.

The amino acid pool has about 100g of proteins ready and wating to be called into service at any time. That's not a lot but it's not a little. It's just getting turned over frequently as proteins are constantly being used and rebuilt.

Proteins are so important, and so versatile. Many can be constructed on the fly from available protein resources in the bloodstream, or the "amino acid pool." Part of the process of metabolism (changing stuff) is to take the proteins we ingest and convert them as needed by the demands of our bodies into the proteins we need. They can be converted into non-protein compounds (to be used in lieu of carbs in glyconeogenisis) and catabolized for ATP/energy conversion. Indeed, here's a shocker (to me): about 5% of the energy from longer duration activities comes from BCAAs.

This processing is where essential and non-essential proteins come into play. The essentials are the ones we need to ingest because we can't synthesize them.

It's a Wading Poo: No Deep End
That said, our bloodstream it seems is already pretty full with other stuff besides proteins cuing up for use. So we don't store a lot. Therefore, we need to ingest protein regularly. This need doesn't mean go nuts on protein. More doesn't always mean better, right? But it does mean that our bodies need a pretty consistent flow of them. And if it doesn't get those proteins from our diet? Our bodies will start taking proteins from other sources. Like muscle. And repurpose them. We're wired for survival not performance or prettiness.


Amino Acids: eat your veggies
This is just an aside to remind us that we can get the amino acids we need from plant based diets. And likewise if we rely on veggies, we will also be getting more than just protein. One of the advantages of a more plant based (i didn't say vegetarian) diet is that well, you get a lot of protein from eating a range of veggies, we also get lots of other nutrients not found just in meats/dairy, and they are less energy and calorically dense. So we can eat rather a lot, volume wise. If we get a good mix of veggies and legumes, we don't need to worry too much either about whether or not we're getting whole proteins and all the essential amino acids we need.


Protein turnover, though, means that likely the worst thing to compromise in one's diet IS protein
a) because we're mainly organisms made up of protein and water.
b) because we don't store a lot of protein for re-use in the amino acid pools and
c) because the proteins in all parts of us are constantly being replenished

Muscle is still Protein, right?
Muscle is just one of the tissues in our body that requires and turns over protein regularly. If all tissue cells have protein as a part of them, then presumably sufficient protein needs to be available for all the metabolic signalling (hormones and enzymes) and new tissue building (more amino acids), and sufficient energy stores need to be available to support the building process (ATP).

Protein synthesis is, as best i understand, cells' DNA signalling to say there's a need to create more protein of some kind for a particular requirement - whether that's a requirement to generate more hormones or muscle tissue or antibodies. Muscle use - when pushed to adapt to new stresses causes existing protein to breakdown in normal turn over and to be rebuilt, and rebuild more tissue as needed. The tissue is largely protein based. But so are the cells in our body.

Protein turnover (catabolism and anabolism) is happening all the time in all parts of the body, not just muscle, as cells die, get flushed and replaced. In muscle building we usually focus on protein synthesis - the generation of new protein - and crave anabolism and fear catabolism. We want MORE not less. But protein turnover, it seems from all the above, is important, and part of staying healthy, and effects more or less everything in our bodies.


How much protein to eat?
I'm not going to get into how much protein do we need. The 1g to 1lb of body weight is a pretty grounded heuristic for two reasons:

it's very difficult to go toxic on protein (discussed here), so potentially overeating protein in the mix of other nutrients is likely ok if one's going to err on a given macronutrient.
but, lets remember that overeating ANY food pushing into caloric surplus means what's not needed goes to fat.
For more, also checking out Brad Pilon of Eat Stop Eat on protein research (for muscle building) is a very interesting read.

 

[ketsugo]

Good to know as I got this grape flavored BCAA powder damn I mix with diet 7up lol incredible during workout or later watching tv over ice


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