Is it necessary to supplement BCAA's
- 01-22-2006, 03:09 AM
- 01-22-2006, 08:31 AM
I actually thought about megadosing up to 50 grams a day for a couple of months just to see where it would take me. I enjoy taking my EAA's during my workouts, but damn if it doesn't get expensive, especially if I wanted to take them everyday.
01-22-2006, 01:29 PM
Your daily protein intake is fine. BCAA likely aren't going to be doing anything normal protein wouldn't. You guys mega dosing all day need to research something called the muscle full effect...basically flooding the system causes decreased effect on signalling and protein synthesis. If you're going to use BCAA (which I wouldn't because I don't think its any better than just using whey) you should use them only at meals, as bolus doses seem to have the most impact on protein synthesis and make sure you take some carbs. The signalling will be greatly enhance by high physiologic levels of insulin (though interestingly will not increase protein synth any more).
The ironic part is many (some) of the authors sited in these pro BCAA articles don't think supplementing is a good idea. People that say athletes need more protein cause they are active blah blah need to keep a few things in mind: 1) protein metabolism for energy makes up less than 20% of energy used by athletes. 2) training increases the efficiency with which protein is used. Bottom line is if you're eating enough calories your probably eating enough protein and your probably getting ample BCAA anyway. You could say probably is too risky for you, but I would say thats just the OCD bodybuilder in you coming out
FYI in some research as little as 10g had an impact on post workout muscle protein synthesis. This was usually in the postworkout window where protein synth was already very low. It generally doubled protein synth...but something recently pointed out to me that makes great sense: 2x not much is still not much.
I think the intellectual chest thumping related to mTOR/eIF2 and p70S6k and BCAA are fun and neato from a molecular mechanistic standpoint but I think their application to real world things is null in the face of proper nutrition.
01-22-2006, 01:36 PM
oh and during workout...high intracellular Ca/calmodulin inactivate the eEF2's directly...translation, no protein synthesis during your workout. This is exciting new research as previously people thought this was an AMPk effect which might lend itself to being overcome by stiff mTOR stim. The Ca pathway subverts even mTOR stimulated prot synth (since mTOR works mainly activate eIF2B and decrease the activity of GSK inactivation of EIF2B's but the inhibition of EEF2's is downstream of this step ...inhibiting a ribosomal/mRNA interaction vs the construction of an mRNA c mTOR)
One flip side is that you could say well, you ahve more mRNA floating around so that its immediately available post exercise after contraction/inhibition stop.
The real question is still...will it make a difference....
01-22-2006, 02:28 PM
I'm not so sure on the benefits during a cutting cycle. Specifially UD2 style.
In the writeups for BCAA its states that the body will use the BCAA to form glucose, and activate MTOR(which inhibits AMPK). A cutting cycle that relies on low carbs and muscle glycogen depletion is going to work best when no glucose formation is happening, is it not?
I read a recent study that shows ampk activation causes apoptosis, and fat cells dying off during a cutting cycle sounds like a pretty good deal. Isnt BCAA supplementation going to inhibit this process via the pathways stated above?
On a side note creatine also inhibits ampk acitivation, so I would say thats a no-no as well.
As far as muscle protein sparing, wouldnt 15-20 grams of whey preworkout supplly enough amino acids to limit muscle protein breakdown during the glycogen depletion workout? I would think instead, adding ephedrine is going to help with muscle protein sparing as well by causing the muscles to preferencially use free fatty acids, and this would be more ideal in a cutting environment.
I guess in the end it depends on what kind of genetics you have to work with
01-22-2006, 08:02 PM
Nate,Originally Posted by natedogg
How are you measuring your BCAAs? You have a lil' scale, or are you doing it by teaspoons? Again, if anyone knows how many grams are in your average BCAA powder teaspoon I'd love to hear it. I was originally thinking a teaspoon = 5grams, but I just want to be sure. Even with Crystal light they are pretty foul tasting.
01-22-2006, 11:13 PM
Right now I'm using EAA's. I use a TBSP which equals about 6.25 grams, since 2 TBSP's is supposed to equal 12.5 grams according to the label. I do have a scale so I guess I could always double check, but Matt at CNW said it was correct so I haven't bothered. I usually use about 20 grams during workouts mixed in with some Gatorade and a packet of Emergen-C. Don't even taste it.
01-23-2006, 12:02 AM
I think EAA supplements have other advantages over whole protein (at least on paper). One reason is that they are a more concentrated form of complete protein (if they have tryptophan in them) and thus decrease the acid load your body would normally see from a high protein intake. Actually that is why I think they are responsible for decreased protein breakdown more than anything else. As far as synthesis goes they appear to be not as good as a whole protein (with the non) only because some conversion of essential to non essential needs to take place. Still the "Net" gain in protein accretion with EAA vs whole protein appears to be better for the EAAs only because the decreased breakdown far outweighs the slight decreased synthesis.
I have no idea how much you'd need to take to show improvements in body composition though.
Whoever was talking about intracellular calcium. Yes I agree that it will antagonize acute synthesis, but may " " the muscle later on for activation of the sodium potassium pump and thus uptake of amino acids etc.
P.S. Most EAA supplements are predominately BCAAs just in case anybody didn't know.
01-23-2006, 01:26 AM
a lot of that decreased breakdown is a fxn of mTOR overcoming inhibition by atrophy factors (mainly eIF2 inhibitors). So you could argue even if EAA (specifically BCAA (leucine)) had little effect on increasing protein synth it might have benefit in preventing protein breakdown, which I think was your contention. Keep in mind the nature of the research on these subjects (mostly in vitro or in pathologically derranged metabolic states in murine models), the duration of the effect (transient, 3-4 hours tops and capable of reaching saturation), and the implications for a well nourished healthy individual (slim to none)Originally Posted by Phosphate bond
Most of the research we are reading was written by people interested in preventing cachexia/wasting in cancer, immuno comp'd peoples. We are just greedy bastards and try and twist it to our perverse desires to get hyooge
I think 15-25% of calories on a hypercaloric diet are all the protein most people need. Some of these 300g protein diets are a bit out there.
On a diet (cut) I think its a lost cause. You are never going to be anabolic, thats why youre on a diet.
01-23-2006, 01:35 AM
Why do you say on a cut it is a lost cause?Originally Posted by Jay Mc
The whole idea in my opinion to use a EAA mix for cutting is reduce the acidosis you'll likely have...but still get adequate essential aminos.
I look at things differently because at this point I'm mainly interested in body recomposition.
P.S. There is cutting and then there is cutting....Yes any caloric deficit that is too severe will always be muscle wasting.
01-23-2006, 01:45 AM
True....just like all the research you read on EPA (omega 3) and it's effects on cachexia.Originally Posted by Jay Mc
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