MEGADOSING LEUCINE

[Smack]

Posted by brad yesterday on a study released a few days ago

Who takes BCAA's or leucine and then doesnt eat? Study isnt really relevant

 

[Mr_President]

I used to eat 300g of protein from wholefoods and whey. I now get 150g from wholefoods combined with leucine at each meal. In addition, I have ~40g EAA per day. Results: about 10lbs heavier and bodyfat is certainly lower, with no more gastric stress issues. Strength is considerably higher, too.

I used to be a slave to studies, especially during my early dietetic years. Give things a fair trial for yourself, and if it doesn't work, evaluate your protocol and adapt it, or change it entirely...

 

[mujeriego]

I used to eat 300g of protein from wholefoods and whey. I now get 150g from wholefoods combined with leucine at each meal. In addition, I have ~40g EAA per day. Results: about 10lbs heavier and bodyfat is certainly lower, with no more gastric stress issues. Strength is considerably higher, too.

I used to be a slave to studies, especially during my early dietetic years. Give things a fair trial for yourself, and if it doesn't work, evaluate your protocol and adapt it, or change it entirely...

That's interesting so your total protein consumption is 190 g a day? how much do you weigh?

 

[dougisbig]

Based on what I'm reading here, Brad is saying is that the co-consumption of all 3 BCAA's is disadvantageous compared to leucine alone, due to competition for absorption, but we've known this for many years now...and I've been saying it for years (which is why I normally advise leucine over all 3 BCAAs).

No evidence is presented here which shows that leucine supplementation does not help drive muscle growth. Brad says it, but there is no evidence. In fact, the copy & paste directly above Brad's appears to directly contradict what he is saying, as clearly says that leucine is the driver of MPS and recovery.

Yes, but that is not an equal (and therefore unfair) comparison, as the whey only group is consuming WAY more whey protein than the whey + leucine group. Furthermore, as shown in the previous study you posted, consuming leucine without additional EAA's does not increase protein synthesis to the same degree as leucine + EAAs. So, this study doesn't really apply it to the question at hand, which is "does whole food + leucine increase protein synthesis to a greater degree than equal amounts of whole food alone.

This study would be like comparing the protein synthesis rates of someone who takes 500 mg of testosterone to someone who takes only 50 mg of testosterone + 50 mg of trenbolone...and then concluding that adding trenbolone to testosterone does not result in additional increases in protein synthesis. In order for the comparison to be valid, the testosterone dose would need to be the same for both groups.

In the same way, you can't have one group consume only 6 grams of whey protein and another group consume 40 grams of whey, and then conclude that leucine supplies no additional benefit when added to whey protein. In order for a study to be relevant, we have to compare EQUAL amounts of whey, with only one of those groups supplementing with additional leucine.

There are also other studies which use equal, larger amounts of whey protein (20-40 grams, I believe) and adding leucine resulted in a greater increase in protein synthesis compared to consuming whey alone.

There are also studies comparing the protein synthesis rates of equal amounts of whey protein and whey protein hydrolysate...and the hydrolyzed whey protein group demonstrated greater increases in protein synthesis. Why? Because the leucine from the hydrolyzed whey was liberated and delivered into the bloodstream more quickly than the regular whey group. This is why adding leucine to food (or whey protein) results in a greater rate of protein synthesis--because it results in a higher concentration of leucine in the bloodstream (a critical factor in determining protein synthesis rates).

This is also why an equal amount of whey protein ALWAYS results in greater increase in protein synthesis compared to casein--because casein is digested so much more slowly (on a side note, casein is far superior at inhibiting protein breakdown, which is why every study comparing whey + casein to whey alone also showed a greater net protein gain in the whey + casein group; mother nature usually does it best).

...and don't forget, bodybuilders use a lot of other, much more slowly digesting protein sources, such as meat. The amino acids from these protein sources are liberated and delivered into the bloodstream much more slowly than free-form/peptide-bonded leucine, which is why adding leucine to whole food (especially meat) results in substantially greater increases in protein synthesis.


My main point is that adding leucine to whole food protein sources leads to a greater increase in protein synthesis...and until someone can explain to me why this additional increase in protein synthesis is irrelevant from a muscle building standpoint, I will continue to believe that supplemental leucine is beneficial.

I would like to see a study comparing larger amounts of whole food protein to an equal amount of whole food protein with additional leucine, such as 80-100 grams of meat protein. I am willing to bet that even when consuming that much meat protein, that supplementing with additional leucine will still result in greater increases in protein synthesis. Since few bodybuilders regularly consume more meat protein than that in a single sitting (most don't even eat that much per meal), it really doesn't matter if we could achieve comparable increases in protein synthesis (which I doubt) with that quantity of meat...and if it took even larger amounts of meat to achieve comparable results, it would be even more irrelevant, as no one is going to regularly consume that much meat protein in a single siting on a regular basis...and neither should they from a health standpoint (not to mention the misery associated with that type of diet).

So, even if it is just from a health and enjoyment standpoint alone, I will stick with my leucine.



As far as fat loss is concerned, yes, leucine is certainly a valuable aide for muscle maintenance when calories are low.

Mike,

Help me out with the above in bold. I (think) I understand the competition between leucine and the other BCAA's, however, how is this not an issue with a complete protein source such as hydro whey? If we did use hydro whey as our source of bolus leucine, do we need to up the dose of leucine to offset the competition?
Not sure if you were ever on Dat's board, but he had a very specific amino drink that he promoted that I believe was leucine, alanine, glycine, and glutamine. How is there not 'competition' in a mix like that?

Thx.
D

 

[TheOtherOne55]

I used to eat 300g of protein from wholefoods and whey. I now get 150g from wholefoods combined with leucine at each meal. In addition, I have ~40g EAA per day. Results: about 10lbs heavier and bodyfat is certainly lower, with no more gastric stress issues. Strength is considerably higher, too.

I used to be a slave to studies, especially during my early dietetic years. Give things a fair trial for yourself, and if it doesn't work, evaluate your protocol and adapt it, or change it entirely...

Interested in exactly HOW you are doing thing.
Are you having say 30g of whole food protein per meal or what?
Or are you doing 50+g of whole food protein in certain meals and EAA at other meals?
Would love to hear what you do.

 

[Mr_President]

Interested in exactly HOW you are doing thing.
Are you having say 30g of whole food protein per meal or what?
Or are you doing 50+g of whole food protein in certain meals and EAA at other meals?
Would love to hear what you do.

I don't stress about meal patterns. For example, one day it's 3 x 50g protein from wholefood meals, another day it's 5 x 30g. It depends very much on my circumstances for the day or how I'm feeling. Working in a hospital I'll sometimes go 12-hours during the day without a meal and only end up consuming 2 x 75g protein meals and will mostly rely on EAAs. The unchanging variable here is that I consume ~10g leucine (tablets) with each meal.

The EAAs are consumed either 10g/500ml water or 20g/500ml for 40-50g/d; 5g lecuine per 15g. These concoctions are consumed bolus style. That's it.

I understand that studies indicate periods of 3-4 hrs between meals to maximise MPS by leucine but, for me, I've noticed absolutely zero difference by not doing that, or indeed by doing it. The take-away factor for me is that since doing this gains have been consistent: bodyfat has crept down, strength is consistently up, and I'm no longer feeling like a bloated mess who is also a slave to diet.

I'm maintain 225lbs at 6'0 and according to calipers ~10% bodyfat; 200mg test E per week. So nope, I'm not a mass monster, but I'm very healthy and I actually look like I lift heavy iron.

 

[DOGGCRAPP]

I got in an argument about this very subject today online. Im the worst guy to comment on this because its one of the raw ingredients we sell and just like i knew it would....the guy goes to "yea you are arguing this because you stand to lose money if....."
thats why I stay out of these things...I dont care if someone uses them or doesnt use them to be honest.

I will just say this. There is so much data saying YES NO MAYBE about this subject its nauseating.

Noone is putting a gun to your head. Decide if its for you and go with it and then use deductive reasoning on whether it was viable and keep doing your thing or chuck it.....thats how I feel about it.


https://www.ncbi.nlm.nih.gov/pubmed/23551944

https://www.ncbi.nlm.nih.gov/m/pubmed/16365096/

https://www.ncbi.nlm.nih.gov/m/pubmed/16365095/

https://www.ncbi.nlm.nih.gov/m/pubmed/11344218/

https://www.ncbi.nlm.nih.gov/m/pubmed/2174312/

https://www.ncbi.nlm.nih.gov/m/pubmed/16365096/

https://www.ncbi.nlm.nih.gov/pubmed/24284442

https://www.ncbi.nlm.nih.gov/m/pubmed/27053525/

https://jissn.biomedcentral.com/articles/10.1186/1550-2783-9-20

I believe in leucine...I dont know if you can do it alone with leucine (due to some studies) so Ive always taken at least 4 times the leucine as the other aminos.
I use EAA's/BCAA's with a much larger dose of leucine in place of whey protein...when trying to cut back calories....until thats proven to be catabolic....thats the way im going to go.

3 protein drinks a day are roughly 750 calories...so if im trying to lean out i drop 500 calories and replace protein drinks with EAA/BCAA with a large amount of leucine.

 

[OutToLunch]

Replacing/supplanting with leucine to maintain or diet down sounds more reasonable than saying 10lbs of muscle was put on provided all else remained constant.

 

[Mike Arnold]

Replacing/supplanting with leucine to maintain or diet down sounds more reasonable than saying 10lbs of muscle was put on provided all else remained constant.

I don't think anyone here claimed that leucine added 10 pounds of muscle, but then again, can we accurately measure the amount of muscle gained with anything? Since bodybuilders typically use multiple anabolic/anti-catabolic substances at once, including food and food-based substances, attributing a particular amount of muscle gain (especially when so many thing are interconnected) to a single substance is difficult to impossible.

Once thing is certain. Leucine is the primary activator of mTOR, without which we aren't gaining any muscle.

 

[MKSuccess500]

I don't think anyone here claimed that leucine added 10 pounds of muscle, but then again, can we accurately measure the amount of muscle gained with anything? Since bodybuilders typically use multiple anabolic/anti-catabolic substances at once, including food and food-based substances, attributing a particular amount of muscle gain (especially when so many thing are interconnected) to a single substance is difficult to impossible.

Once thing is certain. Leucine is the primary activator of mTOR, without which we aren't gaining any muscle.

When you say "Results: about 10lbs heavier and bodyfat is certainly lower" you are basically claiming what you changed added 10lb of muscle.

But I agree, anyone thinking leucine supplementation is going to add 10 POUNDS OF MUSCLE is off their rocker. Not to mention how much time was between that interval? I switched to 3 meals a day five years ago instead of 7-8 meals a day...I'm also 15lb heavier at the same body fat...that sure isn't because of my meal pattern changing. How much gear was used that that time? Etc.

Every pro-leucine study posted on this page is about protein synthesis or various enzymes. But then again I agree you can't just go by studies. Just amusing to me that anyone thinks even if it does work it will help more than a few percent.

 

[Mike Arnold]

When you say "Results: about 10lbs heavier and bodyfat is certainly lower" you are basically claiming what you changed added 10lb of muscle.

But I agree, anyone thinking leucine supplementation is going to add 10 POUNDS OF MUSCLE is off their rocker. Not to mention how much time was between that interval? I switched to 3 meals a day five years ago instead of 7-8 meals a day...I'm also 15lb heavier at the same body fat...that sure isn't because of my meal pattern changing. How much gear was used that that time? Etc.

Every pro-leucine study posted on this page is about protein synthesis or various enzymes. But then again I agree you can't just go by studies. Just amusing to me that anyone thinks even if it does work it will help more than a few percent.

I never claimed to have gained any amount of bodyweight. You must be confusing me with some else in this thread (unless when you said "you" you were referring to someone else).

 

[MKSuccess500]

I never claimed to have gained any amount of bodyweight. You must be confusing me with some else in this thread (unless when you said "you" you were referring to someone else).

Yes I meant the general "you"....I think you may have missed Mr_President's post above which clearly implies adding leucine and EAAs resulted in him being 10lb heavier while being leaner, which I think any knowledgeable person would agree is an absurd claim. I'm not saying he's lying, I'm saying if it's true it sure as hell isn't due to adding leucine and maybe he's not factoring in other aspects. Most of us kill ourselves in the gym and use (abuse) AAS to gain even 5lb of real muscle tissue once we're at an advanced stage. No single supplement in the world adds 10lb of lean body mass to someone.

 

[Mr_President]

When you say "Results: about 10lbs heavier and bodyfat is certainly lower" you are basically claiming what you changed added 10lb of muscle.

But I agree, anyone thinking leucine supplementation is going to add 10 POUNDS OF MUSCLE is off their rocker. Not to mention how much time was between that interval? I switched to 3 meals a day five years ago instead of 7-8 meals a day...I'm also 15lb heavier at the same body fat...that sure isn't because of my meal pattern changing. How much gear was used that that time? Etc.

Every pro-leucine study posted on this page is about protein synthesis or various enzymes. But then again I agree you can't just go by studies. Just amusing to me that anyone thinks even if it does work it will help more than a few percent.

No, I wasn't claiming that at all, though I see how it can be construed that way. I was merely stating that using EAA + lecuine in favour of wholefood protein hadn't stopped gains but actually made it better with the added fat loss; I didn't experience this with the former diet.

 

[Deleted member 106824]

https://www.ncbi.nlm.nih.gov/pubmed/28444456/ not stating my opinion on it, just posting due to relevance

 

[mujeriego]

https://www.ncbi.nlm.nih.gov/pubmed/28444456/ not stating my opinion on it, just posting due to relevance

It's not too relevant though, no offence bro it's good that you posted it still. But yeah the study is not a very good one. I could of predicted those results before the study was ever done. Training 2x/week and only supplementing with leucine at 3 grams post workout was never going to give any sort of indication as to leucines ability to increase mps

 

[Deleted member 106824]

It's not too relevant though, no offence bro it's good that you posted it still. But yeah the study is not a very good one. I could of predicted those results before the study was ever done. Training 2x/week and only supplementing with leucine at 3 grams post workout was never going to give any sort of indication as to leucines ability to increase mps

I agree it's too low of a dose. Good that they did it post-workout (I'm assuming they ate soon afterwards) so the timing was better than some other studies but it would have been nice to see a higher dose.

 

[DOGGCRAPP]

Interesting study posted by Stewie

Frontiers | Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans | Physiology

Discussion
The present study demonstrated that ingesting of all three BCAAs alone, without concurrent ingestion of other EAA, protein, or macronutrients, stimulated a 22% greater response of myofibrillar-MPS following resistance exercise compared with a placebo. The magnitude of this increased response of myofibrillar-MPS was ~50% less than the previously reported myofibrillar-MPS response to a dose of whey protein containing similar amounts of BCAAs (Churchward-Venne et al., 2012; Witard et al., 2014). Taken together, these results demonstrate that BCAAs exhibit the capacity to stimulate myofibrillar-MPS, however a full complement of EAA could be necessary to stimulate a maximal response of myofibrillar-MPS following resistance exercise. This information potentially has important nutritional implications for selecting amino acid supplements to facilitate skeletal muscle hypertrophy in response to resistance exercise training and the maintenance of muscle mass during aging, unloading, or disease.

The most likely physiological explanation for the apparent attenuation of the post-exercise response of myofibrillar-MPS to BCAA ingestion in comparison to an intact protein source relates to the limited availability of amino acids as substrate for MPS. It is well-established that BCAA ingestion stimulates the activation of mTORC1 signaling pathways that regulate the translational activity of MPS (Karlsson et al., 2004; Apro and Blomstrand, 2010; Moberg et al., 2016). Moreover, recent results demonstrate that the presence of the valine and isoleucine enhances the response of mTORC1 to leucine (Moberg et al., 2016). However, results from the present study suggest that ingesting BCAAs alone, without the other EAA, provides limited substrate for protein synthesis in exercised muscles. Thus, the overall response of MPS is not maximized. Instead, the limited availability of EAA likely explains the qualitative difference in magnitude of the MPS response to ingestion of BCAAs alone and ingestion of similar amounts of BCAAs as part of intact whey protein (Churchward-Venne et al., 2012, 2014; Witard et al., 2014). Moreover, in the present study, we observed a decline in arterialized phenylalanine concentrations 3 h after drink ingestion in the BCAA trial. This finding is consistent with previous research that observed decreased EAA concentrations following leucine ingestion (Hagenfeldt and Wahren, 1980; Nair et al., 1992; Tipton et al., 2009; Borgenvik et al., 2012). Taken together, these data support the notion that EAA availability is the rate-limiting factor for stimulating a maximal MPS response to resistance exercise with BCAA ingestion.

The decline in EAA availability that we observed with BCAA ingestion also provides a potential physiological explanation for the differential response of MPS to ingesting a BCAA source at rest and following resistance exercise. Previously, Wilkinson and colleagues reported an ~100% increase in myofibrillar-MPS in response to ingestion of leucine alone at rest (Wilkinson et al., 2013). Furthermore, a study from Churchward-Venne and colleagues reported that adding leucine to a “suboptimal” dose (6.25 g) of whey protein resulted in rates of myofibrillar-MPS similar to those after ingestion of 25 g of whey protein at rest. However, consistent with the results reported in the present study, the addition of leucine to 6.25 g of whey protein was not as effective as higher doses of whey protein ingested after resistance exercise (Churchward-Venne et al., 2012). Thus, exercise has been shown to alter the relationship of the MPS response to ingested leucine and intact protein. It is likely that the enhanced ability of muscle to utilize ingested protein following exercise (Pennings et al., 2011; Witard et al., 2014) leads to a greater demand for EAA, thus resulting in limited EAA availability at the greater rates of MPS. In another study, Churchward-Venne et al. (2014) also reported that BCAA added to a suboptimal dose of whey protein resulted in less stimulation of MPS than when the same amount of leucine alone was added to suboptimal whey protein. These data suggest that leucine alone may be sufficient to stimulate MPS following exercise provided a minimal amount of EAA is included. However, Churchward-Venne et al. (2014) included ingestion of leucine with 6.25 g of whey protein and a mixed macronutrient beverage making direct comparisons with our results difficult. Leucine seems to be the most important BCAA for stimulation of the translation initiation pathways (Anthony et al., 2000; Crozier et al., 2005) and leucine alone stimulates MPS at rest (Wilkinson et al., 2013). Thus, it is possible that leucine is solely responsible for the stimulation in MPS we report here. On the other hand, recent data suggest that there is a greater stimulatory effect on mTORC1 when valine and isoleucine are consumed alongside leucine (Moberg et al., 2016). Nevertheless, taken together, these past and present data suggest that the availability of EAA may be a critical factor for the optimal response of MPS following resistance exercise. Since the ingestion of BCAAs alone stimulates myofibrillar-MPS, but does not increase the supply of all EAA, the overall response of myofibrillar-MPS following resistance exercise is limited.

The influence of exogenous BCAAs on the stimulation of MPS following exercise is mediated by an increased activation of the mTORC1-S6K1 signaling pathway. In the present study, the stimulation of PRAS40Thr246, and S6K1Thr389 phosphorylation 1 h following drink ingestion was higher in BCAA than PLA. Thus, our results are consistent with earlier work demonstrating an upregulation of translational activity with BCAA ingestion (Karlsson et al., 2004; Apro and Blomstrand, 2010). The present study is the first to demonstrate the upregulation of mTORC1 signaling with BCAA ingestion translates into an increased response of myofibrillar-MPS following resistance exercise.

BCAAs has been shown to influence muscle protein metabolism through MPB as well as MPS (Buse and Reid, 1975; Louard et al., 1990; Wilkinson et al., 2013). Early studies demonstrated that BCAAs reduce whole-body protein breakdown (Ferrando et al., 1995) and MPB (Louard et al., 1990; Nair et al., 1992). Recent evidence suggests the impact of BCAAs on MPB may be mediated by the leucine metabolite, β-hydroxy-β-methylbutyrate (Wilkinson et al., 2013). However, to date no study has investigated the impact of BCAA supplementation on MPB following exercise. Unfortunately, it was not possible to directly measure MPB in the present study, however our data suggest that whole-body protein breakdown was reduced by BCAA ingestion. Whereas, urea production rates were similar between trials, phenylalanine Ra, and phenylalanine oxidation rates—both indicators of whole body protein catabolism—were lower in BCAA than PLA during the 4 h period after drink ingestion. These data are consistent with previously reported results following ingestion of intact protein with similar amounts of BCAAs (Witard et al., 2014). It has been reported that MPB is reduced by insulin following resistance exercise (Biolo et al., 1999). However, the insulin response to BCAA and PLA was similar, so it is unlikely that insulin explains the decline in whole-body protein breakdown following BCAA ingestion. Thus, it seems clear that whole-body protein breakdown is decreased, albeit minimally, with ingestion of BCAAs following resistance exercise. However, these results do not necessarily mean that MPB is decreased with BCAA ingestion.

To conclude, the ingestion of BCAAs alone, without the concurrent ingestion of other EAA, intact protein or other macronutrients, increases the stimulation of mTORC1 activity and myofibrillar-MPS following exercise in resistance-trained young men. Our data support the notion that BCAA ingestion alone does not maximally stimulate myofibrillar-MPS following exercise despite stimulation of translation initiation pathways. The lack of sufficient EAA appears to limit the response of myofibrillar-MPS following exercise. Thus, whereas our data clearly show that BCAA ingestion activates cell-signaling pathways that result in increased myofibrillar-MPS, ingestion of BCAAs alone may not be the optimal nutritional regimen to stimulate a maximal MPS response to resistance exercise training.

 

[Stewie]

Interesting study posted by Stewie

Frontiers | Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans | Physiology

Discussion
The present study demonstrated that ingesting of all three BCAAs alone, without concurrent ingestion of other EAA, protein, or macronutrients, stimulated a 22% greater response of myofibrillar-MPS following resistance exercise compared with a placebo. The magnitude of this increased response of myofibrillar-MPS was ~50% less than the previously reported myofibrillar-MPS response to a dose of whey protein containing similar amounts of BCAAs (Churchward-Venne et al., 2012; Witard et al., 2014). Taken together, these results demonstrate that BCAAs exhibit the capacity to stimulate myofibrillar-MPS, however a full complement of EAA could be necessary to stimulate a maximal response of myofibrillar-MPS following resistance exercise. This information potentially has important nutritional implications for selecting amino acid supplements to facilitate skeletal muscle hypertrophy in response to resistance exercise training and the maintenance of muscle mass during aging, unloading, or disease.

The most likely physiological explanation for the apparent attenuation of the post-exercise response of myofibrillar-MPS to BCAA ingestion in comparison to an intact protein source relates to the limited availability of amino acids as substrate for MPS. It is well-established that BCAA ingestion stimulates the activation of mTORC1 signaling pathways that regulate the translational activity of MPS (Karlsson et al., 2004; Apro and Blomstrand, 2010; Moberg et al., 2016). Moreover, recent results demonstrate that the presence of the valine and isoleucine enhances the response of mTORC1 to leucine (Moberg et al., 2016). However, results from the present study suggest that ingesting BCAAs alone, without the other EAA, provides limited substrate for protein synthesis in exercised muscles. Thus, the overall response of MPS is not maximized. Instead, the limited availability of EAA likely explains the qualitative difference in magnitude of the MPS response to ingestion of BCAAs alone and ingestion of similar amounts of BCAAs as part of intact whey protein (Churchward-Venne et al., 2012, 2014; Witard et al., 2014). Moreover, in the present study, we observed a decline in arterialized phenylalanine concentrations 3 h after drink ingestion in the BCAA trial. This finding is consistent with previous research that observed decreased EAA concentrations following leucine ingestion (Hagenfeldt and Wahren, 1980; Nair et al., 1992; Tipton et al., 2009; Borgenvik et al., 2012). Taken together, these data support the notion that EAA availability is the rate-limiting factor for stimulating a maximal MPS response to resistance exercise with BCAA ingestion.

The decline in EAA availability that we observed with BCAA ingestion also provides a potential physiological explanation for the differential response of MPS to ingesting a BCAA source at rest and following resistance exercise. Previously, Wilkinson and colleagues reported an ~100% increase in myofibrillar-MPS in response to ingestion of leucine alone at rest (Wilkinson et al., 2013). Furthermore, a study from Churchward-Venne and colleagues reported that adding leucine to a “suboptimal” dose (6.25 g) of whey protein resulted in rates of myofibrillar-MPS similar to those after ingestion of 25 g of whey protein at rest. However, consistent with the results reported in the present study, the addition of leucine to 6.25 g of whey protein was not as effective as higher doses of whey protein ingested after resistance exercise (Churchward-Venne et al., 2012). Thus, exercise has been shown to alter the relationship of the MPS response to ingested leucine and intact protein. It is likely that the enhanced ability of muscle to utilize ingested protein following exercise (Pennings et al., 2011; Witard et al., 2014) leads to a greater demand for EAA, thus resulting in limited EAA availability at the greater rates of MPS. In another study, Churchward-Venne et al. (2014) also reported that BCAA added to a suboptimal dose of whey protein resulted in less stimulation of MPS than when the same amount of leucine alone was added to suboptimal whey protein. These data suggest that leucine alone may be sufficient to stimulate MPS following exercise provided a minimal amount of EAA is included. However, Churchward-Venne et al. (2014) included ingestion of leucine with 6.25 g of whey protein and a mixed macronutrient beverage making direct comparisons with our results difficult. Leucine seems to be the most important BCAA for stimulation of the translation initiation pathways (Anthony et al., 2000; Crozier et al., 2005) and leucine alone stimulates MPS at rest (Wilkinson et al., 2013). Thus, it is possible that leucine is solely responsible for the stimulation in MPS we report here. On the other hand, recent data suggest that there is a greater stimulatory effect on mTORC1 when valine and isoleucine are consumed alongside leucine (Moberg et al., 2016). Nevertheless, taken together, these past and present data suggest that the availability of EAA may be a critical factor for the optimal response of MPS following resistance exercise. Since the ingestion of BCAAs alone stimulates myofibrillar-MPS, but does not increase the supply of all EAA, the overall response of myofibrillar-MPS following resistance exercise is limited.

The influence of exogenous BCAAs on the stimulation of MPS following exercise is mediated by an increased activation of the mTORC1-S6K1 signaling pathway. In the present study, the stimulation of PRAS40Thr246, and S6K1Thr389 phosphorylation 1 h following drink ingestion was higher in BCAA than PLA. Thus, our results are consistent with earlier work demonstrating an upregulation of translational activity with BCAA ingestion (Karlsson et al., 2004; Apro and Blomstrand, 2010). The present study is the first to demonstrate the upregulation of mTORC1 signaling with BCAA ingestion translates into an increased response of myofibrillar-MPS following resistance exercise.

BCAAs has been shown to influence muscle protein metabolism through MPB as well as MPS (Buse and Reid, 1975; Louard et al., 1990; Wilkinson et al., 2013). Early studies demonstrated that BCAAs reduce whole-body protein breakdown (Ferrando et al., 1995) and MPB (Louard et al., 1990; Nair et al., 1992). Recent evidence suggests the impact of BCAAs on MPB may be mediated by the leucine metabolite, β-hydroxy-β-methylbutyrate (Wilkinson et al., 2013). However, to date no study has investigated the impact of BCAA supplementation on MPB following exercise. Unfortunately, it was not possible to directly measure MPB in the present study, however our data suggest that whole-body protein breakdown was reduced by BCAA ingestion. Whereas, urea production rates were similar between trials, phenylalanine Ra, and phenylalanine oxidation rates—both indicators of whole body protein catabolism—were lower in BCAA than PLA during the 4 h period after drink ingestion. These data are consistent with previously reported results following ingestion of intact protein with similar amounts of BCAAs (Witard et al., 2014). It has been reported that MPB is reduced by insulin following resistance exercise (Biolo et al., 1999). However, the insulin response to BCAA and PLA was similar, so it is unlikely that insulin explains the decline in whole-body protein breakdown following BCAA ingestion. Thus, it seems clear that whole-body protein breakdown is decreased, albeit minimally, with ingestion of BCAAs following resistance exercise. However, these results do not necessarily mean that MPB is decreased with BCAA ingestion.

To conclude, the ingestion of BCAAs alone, without the concurrent ingestion of other EAA, intact protein or other macronutrients, increases the stimulation of mTORC1 activity and myofibrillar-MPS following exercise in resistance-trained young men. Our data support the notion that BCAA ingestion alone does not maximally stimulate myofibrillar-MPS following exercise despite stimulation of translation initiation pathways. The lack of sufficient EAA appears to limit the response of myofibrillar-MPS following exercise. Thus, whereas our data clearly show that BCAA ingestion activates cell-signaling pathways that result in increased myofibrillar-MPS, ingestion of BCAAs alone may not be the optimal nutritional regimen to stimulate a maximal MPS response to resistance exercise training.

And stupid me.

I recently ordered 5# combo blend (40% WPIC-F, 40% Micellar Casein, 10% Egg Pr) from TN. Intended on adding extra EAA to the mix and totally spaced out

Will on the next order.

 

[mister69]

Guess I have to order more eaa


Sent from my iPhone using Tapatalk

 

[KillerStack]

Came across this article which sounds logical. Author theorizes that taking a bolus of leucine alone, not bcaa, maybe 20 minutes before meals might be optimal based on current evidence. Sure it's micromanaging but some of us like to think about the absolute optimal way of doing things. This is in line with what Mike Arnold thought about spiking leucine.
https://www.strongerbyscience.com/athlete-protein-intake/

Stewie and anyone else, do you see any utility with HMB?
Some recent studies had some insane results with the free HMB acid and I think the studies must be faulty in some way or even fraudulent, but even if it worked 1/10th as well it would be worth it I think.