BCAA's, Necessary? Or Waste? I agree with these guys....BUT, Continue Reading After Their Quotes.
M. Berkhan: No, you get plenty off BCAAs from food protein sources, especially whey protein. There’s nothing showing any benefit of excessive dosing. Because BCAAs are very glucogenic, they will most likely end up in your bloodstream as glucose. Bodybuilders who eat piles of protein and consume BCAAs on the side are throwing money down the drain.
A. Aragon: No, supplemental BCAA is not necessary unless you’re not consuming enough high quality protein. Bodybuilders get marketed to death about the benefits of free-form BCAA when there’s no objective evidence of their benefit over the pre-existing BCAA within the matrix of real food. People forget that BCAA is abundant in many foods in nature, especially animal proteins. I base all of my beliefs and recommendations on scientific evidence, not subjective placebo and marketing driven testimony. You can be sure that if someone believes (by whatever means it took to convince him) that extra BCAA will work, it will. However, it’s the belief that’s the active agent, not the BCAA.
You can create the same effect by convincing someone that a lucky rabbit’s foot in his right pocket will increase his lifting strength. If the person is truly convinced or even if the person has deeply vested hopes in the product or protocol, it indeed will work. The mind has powerful effects on the body. It always has and always will.
Until I see solid replicated scientific evidence of the benefits of stacking supplemental BCAA on top of a pre-existing high protein intake (as compared to simply increasing total protein), I’m not going to buy into the hype. I’ve even experimented with my athletic clientele and had them ditch supplemental BCAA in favor of an increased protein intake. Not only did I save them a lot of money, but their performance and body composition continues to improve. I know that it’s not a tightly controlled experiment, but it definitely puts me at ease that I’m not missing out on any “magic.”
What about for fat loss?
But BCAAs reduce AMPK activity in muscle early, and actually activate it later. BCAAs stimulate mTOR & MPS so powerfully that they actually cause a depletion of ATP in muscle, which activates AMPK about 1-2 hours post ingestion. And if you'd like I'd be happy to send you a full text. The overall outcome of this is that BCAAs increase thermogenesis and long term fat burning. You cannot pick out an isolated timepoint, take a snapshot of it, and then extrapolate that as what is happening ALL the time in response to BCAA ingestion
If you were correct and BCAAs impeded fat burning, how do you explain data from Lynch at Penn State demonstrating that animals with BCAT (the enzyme responsible for transmitting BCAAs, the first step of their metabolism) knocked out are resistant to fat gain & have lower bodyfat levels than normal animals? Because these animals have no BCAT enzyme, they have chronically elevated levels of BCAAs in their blood. The study shows increased fat loss in animals eating higher protein/BCAA due to increased protein turnover activating thermogenesis. Again, BCAAs activate protein synthesis, protein synthesis is thermogenic because it requires ATP, and thus depletes ATP over time, leading to an INCREASED activity of AMPK later in the time course of post meal/supplement consumption. By your theory, this would inhibit AMPK and shut down fat loss. This is obviously not the case.
Don't always assume one kinase/enzyme controls everything. The body is very redundant and metabolism is extremely complex.
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.