Talk about coming back with a vengence... this brings a tear to my eye... Good to see you Spook.

Jake why do I get the feeling you've been lurking here for years?

Interesting excerpts from the article:







One theory:



And shouldn't PWO carbs still be utilized to take advantage of increased insulin sensitivity and replenish glycogen stores ASAP? Increased cell volume -> anabolism, right?

They did a lot of the data with phenylalanine -- wouldn't data on the BCAAs be more applicable?

this doesnt mean they are a waste.

Aren't there like a ton of other studies that support carbohydrates increasing protein synthesis? So was is it that this one study should be telling me?

I think his point may have been that carbs aren't increasing PRO synthesis much beyond what 20-25 g/hr (for my bw) of hydrolyzed casein already do -- that sufficient PWO PRO will probably stimulate enough insulin to make adding carbs superfluous.

The researchers were looking at protein synthesis. Muscle protein balance is what ultimately matters. It's the net effect between protein synthesis and protein breakdown. Study after study after study shows that after training, aminos increase protein synthesis and carbs/insulin decrease protein breakdown. This study was looking at protein synthesis so, no surprise, it didn't find an additive effect from the carbs.

But how could the addition of carbs in a PWO shake be "useful"?

1. Net protein balance. In this study, they looked at the fractional synthetic rate in muscle, but they "did not assess skeletal muscle protein breakdown rates". For example, there was no 3-methylhistidine data looking at myofibrillar degradation. This was an acute study looking at the effects for 6 hours after one training bout. This raises questions, since studies like this have found that supplementing with CHO+EAA after training, for 12 weeks, leads to a reduction in protein degradation and an increase in cross sectional muscle area when compared to EAA alone. Yet EAA alone in this study raised insulin to 12.7 - 19.4 μU/ml-1. If it's true that "an increase in insulin levels above 10-15 μU/ml-1 does not further enhance muscle protein synthesis and/or reduce protein degradation" then why did adding carbs to the drink make such a difference? Well, perhaps by increasing glycogen levels or decreasing muscle damage...

You have to keep in mind that with FSR they're looking at extremely small numbers that are hard to detect. The margin of error on the readings is relatively high (around 10% of the value). You've got to have some power to detect statistically significant differences here. For example, the FSR readings for the PRO and PRO+HCHO groups were 0.10+/-0.01 and 0.11+/-0.01 %?h-1. Now with 10 subjects, there was no statistical difference here. With more, things might be different. It's quite possible that the actual means in this study were 0.09 and 0.12. That would be a 33% increase from the PRO group to the PRO+HCHO group, yet that still might not have had statistical significance with the small group size.

What I think this study does is call into question the importance of CHO intake PWO as it relates to muscle protein balance. The results were unexpected since carbs are known to reduce protein breakdown. Surely more research will be done on this. The take home message is that protein is the primary factor when it comes to protein synthesis. I think it's premature to say that this disproves the usefullness of taking carbs PWO, though. As I pointed out, this study has questionable scope when you look at the protocol and amount of protein ingested. 6 hours of frequent dosing with an assload of casein hydrolysate is far different than a single PWO bolus of complete whey protein. The sipping makes this fast protein hydrolysate mimic the digestion of a slow protein (like unfractionated casein). This sustained release might inhibit degradation to such an extent that insulin hardly reduces it any more. Also, with so much research in other circumstances showing a benefit from the addition of carbs, I think it's safe to say that this study has NOT disproved the usefulness of adding carbs.

2. Repleting glycogen. The addition of carbs in a PWO shake is especially "useful" from the standpoint of glycogen replacement. Immediately PWO is optimal for both the rate and amount of replenishment. This is probably a primary reason that many people include them, at a time when muscle insulin sensitivity is high and partitioning is most favorable. You can't replenish glycogen nearly as quickly at other times as you can PWO.

3. Reducing muscle damage. Protein is most important for this, but carbs also play a role. Reducing muscle damage accelerates recovery and restores performance more quickly.

The usefulness of adding carbs to a PWO shake IS backed by science and though this study raises some very good questions, it doesn't "apparently disprove" the usefulness of carbs in your typical PWO whey shake.

sigh...oh bother....

1. Folks. Don't forget about the use of prework out carbs. No point in duscussing post workout ingestion in isolation.



One can make a sound argument both ways. On one hand you have increased glycogen superacompensation and cell swelling. On the other hand you have the fact that damaged muscle is insulin resistant, excesively high insulin seems to offer little benefit, glycogen supra-compensation is just going to atenuate exercise response like the increase in GLUT translocation, increase in glycogen synthetic cellular machinery, localized gowth factor production (think MGF), satallite cell proliferation and myoblast fusion, etc....



Of course not. I allways write inflamatory post titles in an atempt to entice people to read the post and spark conversation. There are limitations to this study. The ones people in this thread have brought up are frankly kind of silly and petty. If you want to find fault with it, the real fault is how long they tracked protein synthesis post exercise, and the effect each treatment type had on nitrogen balance over a longer period. To get a really clear picture one needs to track it over the 36-48 hour peroid of increased ribosome activity for turely meaningful data.



1. Post workout carb ingestion as it relates to muscular hypertrophy is backed by science, huh? prove it. Nothing proves a point quite like unsubstantiated and unqualified conclusions... (sigh)
2. If you are going to take a scientific aproach to analysis and criticism how about using precise terms in your argument. IOW what the hell are you defining "muscle damange" to be.
3. If you are making the argument I think you are making then all you have done is shift the burden of proof. You now need to explain why imediate glycogen repetion, a post workout insulin spike, and decrease "muscle damage" are optimal for muscular hypertrophy and/or body composition.

I've seen research that shows that insulin resistance increases when there's an emphasis on the eccentric component during a workout.

I still haven't seen anything to suggest that faster glycogen replenishment = faster recovery/more hypertrophy.

Because your a smart man, and I like your style.

I've seen it quiped that concentration on the eccentric motion also spikes GH response to weight training as well... but try to implement the theories... With this type of thinking powerlifters every where would be going super slow mo for hours on end... which isn't the case.

Christian Thibadeau talks about this a lot in his Black Book of Training Secrets and his other book (I can't remember the name).

On another note, I thought the whole PWO carb not increasing protein synthesis rates argument was already hashed out in the High/Low GI carb PWO thread that we had going a while back? Maybe I'm wrong, but weren't some of these studies brought to the limelight then....

Yeah, you seem to have read a good deal of this forum and been around.

I thought so, too. Although, Spook's study is a new one it seems.

As long as you have a good pre-workout meal, I don't see why you would have to have carbs post-workout. With that said, currently I am using carbs in a peri/post workout shake, but if I was focused on cutting I'd drop the carbs and only have them pre-workout.

this has been my protocol as well.... So.. insulin has no muscle building tendancies at all?

Well, with extreme doses...

Don't forget powerlifters don't give a crap about spiked GH, hypertrophy, or pretty much damn well anything... UNLESS it makes them stronger.. They're going for neural adaptation rather than muscle building which are 2 very different things.

Shoulda stopped yourself RIGHT there.

Well...I don´t use carbs to get my protein synthesis up via insulin...i use carbs to get my protein synthesis up by eating tons of them and getting my caloric intake up.

carbs post workout are aswome they add a good 300 calories in my regimen.

I don't know why people here aren't sucking down 50 grams of leucine post workout.. I see leucine a major playor more than anything.

LOL....are you serius??

People have mentioned 10g of leucine around workouts. Has anyone or study looked into diminishing returns? Like what amount of leucine is optimal, and dosages over do negligible amounts? Layne, anyone?

Or maybe someone knows what amount layne uses based on his hunches?

Method is this what you were looking for?

Supplement: Branched-Chain Amino Acids in Exercise
Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise1,2
Layne E. Norton and Donald K. Layman3

Division of Nutritional Sciences, Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801

3 To whom corresponding should be addressed. E-mail: dlayman@uiuc.edu.

High-performance physical activity and postexercise recovery lead to significant changes in amino acid and protein metabolism in skeletal muscle. Central to these changes is an increase in the metabolism of the BCAA leucine. During exercise, muscle protein synthesis decreases together with a net increase in protein degradation and stimulation of BCAA oxidation. The decrease in protein synthesis is associated with inhibition of translation initiation factors 4E and 4G and ribosomal protein S6 under regulatory controls of intracellular insulin signaling and leucine concentrations. BCAA oxidation increases through activation of the branched-chain {alpha}-keto acid dehydrogenase (BCKDH). BCKDH activity increases with exercise, reducing plasma and intracellular leucine concentrations. After exercise, recovery of muscle protein synthesis requires dietary protein or BCAA to increase tissue levels of leucine in order to release the inhibition of the initiation factor 4 complex through activation of the protein kinase mammalian target of rapamycin (mTOR). Leucine's effect on mTOR is synergistic with insulin via the phosphoinositol 3-kinase signaling pathway. Together, insulin and leucine allow skeletal muscle to coordinate protein synthesis with physiological state and dietary intake.

Shinola, I can't find exactly method what I'm looking for although I have seen it.



.135 * 90kg = 12.5g free form leucine

I think it makes more rational sense to consume leucine and BCAAs steadily throughout the day rather than as a one-shot mega dose. Granted, a large bump in BCAAs pre/post workout makes sense, but your body undergoes protein turnover 24/7, so why not keep it optimized? FWIW, I mix 5g BCAAs with my SyntheSIZE...Watermelon Xtend + Synth is pretty damn tasty.

That is a good study. I haven't really noticed one like this that dealt with protein FSR so much as this one does.

I havent read the studies grass, I just heard from an experienced dude like layne or someone else, that they used 10g or something.

I guess bolus it around and post workout and spread it nicely throughout the day like lethaljd.

I'd take in at least 6g of BCAA's at any one time, or 3g of leucine, as I think the studies show that 3g of leucine is enough to crank up protein synthesis. FWIW, I think SyntheSIZE already has about 3g of leucine in it.

----------------------
for sure (i think,the best combination , Leucine + Carbs)
----------------------


Am J Physiol Endocrinol Metab. 2005 Apr;288(4):E645-53.

Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects.

Koopman R, Wagenmakers AJ, Manders RJ, Zorenc AH, Senden JM, Gorselink M, Keizer HA, van Loon LJ.

Department of Human Biology, Maastricht University, PO Box 616, 6200 MD Maastricht, The Netherlands.

The present study was designed to determine postexercise muscle protein synthesis and whole body protein balance following the combined ingestion of carbohydrate with or without protein and/or free leucine. Eight male subjects were randomly assigned to three trials in which they consumed drinks containing either carbohydrate (CHO), carbohydrate and protein (CHO+PRO), or carbohydrate, protein, and free leucine (CHO+PRO+Leu) following 45 min of resistance exercise. A primed, continuous infusion of L-[ring-13C6]phenylalanine was applied, with blood samples and muscle biopsies collected to assess fractional synthetic rate (FSR) in the vastus lateralis muscle as well as whole body protein turnover during 6 h of postexercise recovery. Plasma insulin response was higher in the CHO+PRO+Leu compared with the CHO and CHO+PRO trials (+240 +/- 19% and +77 +/- 11%, respectively, P < 0.05). Whole body protein breakdown rates were lower, and whole body protein synthesis rates were higher, in the CHO+PRO and CHO+PRO+Leu trials compared with the CHO trial (P < 0.05). Addition of leucine in the CHO+PRO+Leu trial resulted in a lower protein oxidation rate compared with the CHO+PRO trial. Protein balance was negative during recovery in the CHO trial but positive in the CHO+PRO and CHO+PRO+Leu trials. In the CHO+PRO+Leu trial, whole body net protein balance was significantly greater compared with values observed in the CHO+PRO and CHO trials (P < 0.05). Mixed muscle FSR, measured over a 6-h period of postexercise recovery, was significantly greater in the CHO+PRO+Leu trial compared with the CHO trial (0.095 +/- 0.006 vs. 0.061 +/- 0.008%/h, respectively, P < 0.05), with intermediate values observed in the CHO+PRO trial (0.0820 +/- 0.0104%/h). We conclude that coingestion of protein and leucine stimulates muscle protein synthesis and optimizes whole body protein balance compared with the intake of carbohydrate only.

http://ajpendo.physiology.org/cgi/content/full/288/4/E645



--------------------------------
post prandrial rise in glucose, stimulate protein synthesis through an AMPK- and mTOR-independent process,
plus leucine increase muscle protein synthesis, reduces AMPK phosphorylation, and increases Akt/PKB and mTOR phosphorylation, insulin stimulate mTOR too.
--------------------------------



Biosci Biotechnol Biochem. 2007 Jul;71(7):1650-6.

AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes.

Nakashima K, Yakabe Y.

Molecular Nutrition Research Team, National Institute of Livestock and Grassland Science, Ikenoda, Tsukuba, Japan.

In skeletal muscle, AMP-activated protein kinase (AMPK) is a metabolic master switch regulating glucose and lipid metabolism. Recently, AMPK has been implicated in the control of protein synthesis in skeletal muscle, but the effect of AMPK activation on myofibrillar protein degradation has yet to be elucidated. The present study was designed to examine the effect of 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside (AICAR)-induced AMPK signaling on effector mechanisms of myofibrillar protein degradation and the expression of atrophy-related genes (atrogin-1/MAFbx, MuRF1, proteasome C2 subunit, calpains, cathepsin B, and caspase-3) in C2C12 myotubes. AICAR stimulated myofibrillar protein degradation (as measured by N(tau)-methylhistidine release), while also increasing the levels of atrogin-1/MAFbx and MuRF1 mRNA, but the expression of other atrophy-related genes was not enhanced by AICAR treatment in C2C12 myotubes. AICAR also stimulated the level of FOXO transcription factors mRNA and protein in C2C12 myotubes. These results indicate that activation of AMPK stimulates myofibrillar protein degradation through the expression of atrogin-1/MAFbx and MuRF1 by increasing FOXO transcription factors in skeletal muscles.


Biochem Biophys Res Commun. 2005 Oct 21;336(2):660-6.

Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles.

Nakashima K, Ishida A, Yamazaki M, Abe H.

Department of Animal Physiology and Nutrition, National Institute of Livestock and Grassland Science, Tsukuba 305-0901,

In skeletal muscle, amino acids, together with hormones, are key regulators of protein metabolism. Leucine, in particular, has inhibitory effects of protein degradation in skeletal muscles, but the mechanisms are poorly understood. The present study addressed the role of leucine as a regulator of myofibrillar proteolysis in cultured chick myotubes and chick skeletal muscles, and aimed to determine which cellular responses regulate the process. In chick myotubes, leucine suppressed myofibrillar proteolysis (as measured by N(tau)-methylhistidine release), while also decreasing ubiquitin and proteasome C2 subunit mRNA. Oral administration of leucine also suppressed myofibrillar proteolysis (as measured by plasma N(tau)-methylhistidine concentration), while also decreasing proteasome C2 subunit mRNA in chick skeletal muscle. Leucine activated the phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC) (but not the mammalian target of rapamycin) inhibition of these pathways and increased myofibrillar proteolysis, ubiquitin and proteasome C2 subunit mRNA. Thus, an important component of muscle proteolysis inhibition by leucine, through the PI3K and PKC, is its ability to suppress transcription of the ubiquitin and proteasome C2 subunit, and degradation of myofibrillar protein.



J Physiol. 2007 Jul 15;582(Pt 2):813-23.

Nutrient signalling in the regulation of human muscle protein synthesis.

Fujita S, Dreyer HC, Drummond MJ, Glynn EL, Cadenas JG, Yoshizawa F, Volpi E, Rasmussen BB.

University of Texas Medical Branch, Department of Internal Medicine, Galveston, TX 77555-1144, USA.

The mammalian target of rapamycin (mTOR) and AMP-activated protein kinase (AMPK) are important nutrient- and energy-sensing and signalling proteins in skeletal muscle. AMPK activation decreases muscle protein synthesis by inhibiting mTOR signalling to regulatory proteins associated with translation initiation and elongation. On the other hand, essential amino acids (leucine in particular) and insulin stimulate mTOR signalling and protein synthesis. We hypothesized that anabolic nutrients would be sensed by both AMPK and mTOR, resulting in an acute and potent stimulation of human skeletal muscle protein synthesis via enhanced translation initiation and elongation






.

J Nutr. 2006 Jul;136(7):1792-9.

Leucine activates pancreatic translational machinery in rats and mice through mTOR independently of CCK and insulin.

Sans MD, Tashiro M, Vogel NL, Kimball SR, D'Alecy LG, Williams JA.

Department of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, PA 17033, USA.

Feeding stimulates pancreatic digestive enzyme synthesis at the translational level, and this is thought to be mediated by hormones and neurotransmitters. However, BCAAs, particularly leucine, stimulate protein synthesis in several tissues. We investigated whether BCAA stimulated the translational machinery in murine pancreas and whether their effects were independent of hormones. Rats and mice were administered (i.g. gavage) individual BCAA at 1.35 mg/g (body weight) and rat isolated pancreatic acini were incubated with BCAA under different conditions. Activation of translation initiation factors and total protein synthesis were analyzed. BCAA gavage stimulated the phosphorylation of the initiation factor 4E (eIF4E) binding protein 1 (4E-BP1) and the ribosomal protein S6 kinase (S6K), with leucine being the most effective. Leucine also increased the association of the initiation factors eIF4E and eIF4G, but did not affect the activity of the guanine nucleotide exchange factor eIF2B, nor total protein synthesis. BCAA acted independently of insulin signaling on isolated pancreatic acini from diabetic rats. The ability of leucine to promote phosphorylation of 4E-BP1 and S6K as well as enhance the assembly of the eIF4F complex was unimpaired in CCK-deficient mice. Finally, rapamycin (0.75 mg/kg) administered to rats 2 h before leucine gavage inhibited the phosphorylation of S6 and 4E-BP1 induced by leucine. We conclude that leucine may participate, as a signal as well as a substrate, in activating the translational machinery in pancreatic acinar cells independently of hormonal effects and that this action is through the mTOR pathway.



J Nutr. 2007 Aug;137(8):1880-6.

Protein ingestion further augments S6K1 phosphorylation in skeletal muscle following resistance type exercise in males.

Koopman R, Pennings B, Zorenc AH, van Loon LJ.

Department of Movement Sciences, Nutrition and Toxicology Research Institute Maastricht (NUTRIM), Maastricht University, Maastricht 6200 MD, The Netherlands.

Our objective was to determine the impact of carbohydrate and/or protein ingestion before and after exercise on ribosomal protein S6 kinase (S6K1) and S6 phosphorylation status in human skeletal muscle tissue. Seven healthy, untrained men (22.5 +/- 0.9 y) were randomly assigned to 2 cross-over experiments. Before, immediately after, and 1 h after a single bout of resistance exercise, subjects consumed 0.3 g x kg(-1) carbohydrate with or without 0.3 g x kg(-1) protein hydrolysate (CHO+PRO and CHO, respectively). Muscle biopsies were taken before and immediately after exercise and after 1 and 4 h of postexercise recovery to determine 4E-BP1, S6K1 (both T(421)/S(424) and T(389)), and S6 phosphorylation status. Following resistance exercise, 4E-BP1 phosphorylation was reduced to a greater extent in the CHO treatment (-48 +/- 7%) than in the CHO+PRO treatment (-15 +/- 14%, P < 0.01). During recovery, 4E-BP1 phosphorylation increased in both experiments (P < 0.01), and tended to be higher in the CHO+PRO test (P = 0.08). S6K1 phosphorylation at T(421)/S(424) substantially increased following exercise and remained elevated during recovery with no differences between treatments. In contrast to the CHO treatment (-4 +/- 2%), S6K1 phosphorylation at T(389) was higher following exercise in the CHO+PRO treatment only (+78 +/- 2%, P < 0.01). During recovery, S6K1 phosphorylation at T(389) remained higher in CHO+PRO than in CHO (P < 0.05). S6 phosphorylation was substantially higher following exercise in the CHO+PRO (1.69 +/- 0.35) than in the CHO experiment (0.45 +/- 0.07, P < 0.01) and remained elevated during recovery (P < 0.05). We conclude that the availability of dietary protein further enhances phosphorylation of S6K1 during recovery from resistance type exercise.






.

I am not exactly sure why you are posting these studies ...

These studies tell a well known story.

They also don't contradict what Spook has posted above.

I don't mind seeing studies new and repeated. A bit more discussion from oswaldo would be nice though.

I'm confused as well. I'll second the request for Oswaldocomments!

I have never used PW carbs. I eat my meals as scheduled regardless of when I workout. My PW meal is usually Brocolli, Protein Shake and almonds. Good results since doing this.

------------------------------------
I read all posts in this thread, i consider all the people, i learn of each one; questions, assertions, propositions, ruminations
i learn cos are original perspectives, then i can go deeper (with my previous knowledge) and to extend the knowledge, and to reach conclusions beneficial for all of us.

simple objectivity.............


Take this one, a great find:
-------------------------------------



--------------------------------------------
take this other one (posted, by me):
--------------------------------------------

J Nutr. 2006 Jul;136(7):1792-9.

Leucine activates pancreatic translational machinery in rats and mice through mTOR independently of CCK and insulin.

Sans MD, Tashiro M, Vogel NL, Kimball SR, D'Alecy LG, Williams JA.

Department of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, PA 17033, USA.

Feeding stimulates pancreatic digestive enzyme synthesis at the translational level, and this is thought to be mediated by hormones and neurotransmitters. However, BCAAs, particularly leucine, stimulate protein synthesis in several tissues. We investigated whether BCAA stimulated the translational machinery in murine pancreas and whether their effects were independent of hormones. Rats and mice were administered (i.g. gavage) individual BCAA at 1.35 mg/g (body weight) and rat isolated pancreatic acini were incubated with BCAA under different conditions. Activation of translation initiation factors and total protein synthesis were analyzed. BCAA gavage stimulated the phosphorylation of the initiation factor 4E (eIF4E) binding protein 1 (4E-BP1) and the ribosomal protein S6 kinase (S6K), with leucine being the most effective. Leucine also increased the association of the initiation factors eIF4E and eIF4G, but did not affect the activity of the guanine nucleotide exchange factor eIF2B, nor total protein synthesis. BCAA acted independently of insulin signaling on isolated pancreatic acini from diabetic rats. The ability of leucine to promote phosphorylation of 4E-BP1 and S6K as well as enhance the assembly of the eIF4F complex was unimpaired in CCK-deficient mice. Finally, rapamycin (0.75 mg/kg) administered to rats 2 h before leucine gavage inhibited the phosphorylation of S6 and 4E-BP1 induced by leucine. We conclude that leucine may participate, as a signal as well as a substrate, in activating the translational machinery in pancreatic acinar cells independently of hormonal effects and that this action is through the mTOR pathway.


------------------------------------------
they are in agreement (as low as ).


as high as :
-----------------------------------------

Am J Physiol Endocrinol Metab. 2002 May;282(5):E1092-101.

Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine.

Anthony JC, Lang CH, Crozier SJ, Anthony TG, MacLean DA, Kimball SR, Jefferson LS.

Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, USA.

Enhanced protein synthesis in skeletal muscle after ingestion of a balanced meal in postabsorptive rats is mimicked by oral leucine administration. To assess the contribution of insulin to the protein synthetic response to leucine, food-deprived (18 h) male rats (approximately 200 g) were intravenously administered a primed-constant infusion of somatostatin (60 microg + 3 microg.kg(-1).h(-1)) or vehicle beginning 1 h before administration of leucine (1.35 g L-leucine/kg) or saline (control). Rats were killed 15, 30, 45, 60, or 120 min after leucine administration. Compared with controls, serum insulin concentrations were elevated between 15 and 45 min after leucine administration but returned to basal values by 60 min. Somatostatin maintained insulin concentrations at basal levels throughout the time course. Protein synthesis was increased between 30 and 60 min, and this effect was blocked by somatostatin. Enhanced assembly of the mRNA cap-binding complex (composed of eukaryotic initiation factors eIF4E and eIF4G) and hyperphosphorylation of the eIF4E-binding protein 1 (4E-BP1), the 70-kDa ribosomal protein S6 kinase (S6K1), and the ribosomal protein S6 (rp S6) were observed as early as 15 min and persisted for at least 60 min. Somatostatin attenuated the leucine-induced changes in 4E-BP1 and S6K1 phosphorylation and completely blocked the change in rp S6 phosphorylation but had no effect on eIF4G small middle dot eIF4E assembly. Overall, the results suggest that the leucine-induced enhancement of protein synthesis and the phosphorylation states of 4E-BP1 and S6K1 are facilitated by the transient increase in serum insulin. In contrast, assembly of the mRNA cap-binding complex occurs independently of increases in insulin and, by itself, is insufficient to stimulate rates of protein synthesis in skeletal muscle after leucine administration.

-----------------------------
as high as:
1.35 gr x kg
----------------------------



-------------------------------------------
Post carbs are no a waste, cos
carbs produces a rise in insulin, bigger than leucine, anyway leucine can work through insulin independent mechanisms.
we need more studies but done on leucine + carbs.
-------------------------------------------


Diabetes. 2002 Apr;51(4):928-36.

Orally administered leucine enhances protein synthesis in skeletal muscle of diabetic rats in the absence of increases in 4E-BP1 or S6K1 phosphorylation.

Anthony JC, Reiter AK, Anthony TG, Crozier SJ, Lang CH, MacLean DA, Kimball SR, Jefferson LS.

Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, USA.

In this study, food-deprived (18 h) control rats and rats with alloxan-induced diabetes were orally administered saline or the amino acid leucine to assess whether it regulates protein synthesis independently of a change in serum insulin concentrations. Immediately after leucine administration, diabetic rats were infused with insulin (0.0, 4.0, or 20 pmol small middle dot min(-1) small middle dot kg(-1)) for 1 h to examine the role of the hormone in the protein synthetic response to leucine. In control rats, leucine stimulated protein synthesis by 58% and increased phosphorylation of the translational repressor, eukaryotic initiation factor (eIF) 4E-binding protein (BP)-1, 4E-BP1, fivefold. Consequently, association of the mRNA cap-binding protein eukaryotic initiation factor (eIF)4E with 4E-BP1 was reduced to 50% of control values, and eIF4G*eIF4E complex assembly was increased 80%. Furthermore, leucine increased the phosphorylation of the 70-kDa ribosomal protein S6 (rp S6) and the ribosomal protein S6 kinase (S6K1). Diabetes attenuated protein synthesis compared with control rats. Nonetheless, in diabetic rats, leucine increased protein synthesis by 53% without concomitant changes in the phosphorylation of 4E-BP1 or S6K1. Skeletal muscle protein synthesis was stimulated in diabetic rats infused with insulin, but rates of synthesis remained less than values in nondiabetic controls that were administered leucine. Phosphorylation of 4E-BP1 and S6K1 was increased in diabetic rats infused with insulin in a dose-dependent manner, and the response was enhanced by leucine. The results suggest that leucine enhances protein synthesis in skeletal muscle through both insulin-dependent and -independent mechanisms. The insulin-dependent mechanism is associated with increased phosphorylation of 4E-BP1 and S6K1. In contrast, the insulin-independent effect on protein synthesis is mediated by an unknown mechanism.


----------------------------------------
Protein synthesis requires two steps: transcription and translation, then:

in the mTOR pathway, there are proteins that regulate the translational machinery, one is the translational repressor protein, 4E-BP1 (eukaryotic initiation factor 4E-binding protein). Binding of 4E-BP1 to eIF4E prevents the latter protein from engaging with other partners, such eIF4G, and therefore blocks mRNA translation initiation. 4E-BP1 undergoes phosphorylation at multiple sites, and phosphorylation at some of them disrupts its ability to bind eIF4E, leading to release of 4E-BP1 and allowing eIF4E to bind eIF4G.
Phosphorylation of 4E-BP1 at several sites is stimulated by agents such as insulin, and, in many cell types, this effect requires the presence in the cells' medium of amino acids,then it is deduced that we need 4E-BP1 phosphorylation to begin translation.


and respect transcription :
-----------------------------------------


Mol Cell Biol. 2006 Aug;26(16):6248-60.

Smad7 promotes and enhances skeletal muscle differentiation.

Kollias HD, Perry RL, Miyake T, Aziz A, McDermott JC.

Department of Biology, 327 Farquharson, LSB, York University, 4700 Keele St., Toronto M3J 1P3 Ontario, Canada.

Transforming growth factor beta1 (TGF-beta1) and myostatin signaling, mediated by the same Smad downstream effectors, potently repress skeletal muscle cell differentiation. Smad7 inhibits these cytokine signaling pathways. The role of Smad7 during skeletal muscle cell differentiation was assessed. In these studies, we document that increased expression of Smad7 abrogates myostatin- but not TGF-beta1-mediated repression of myogenesis. Further, constitutive expression of exogenous Smad7 potently enhanced skeletal muscle differentiation and cellular hypertrophy. Conversely, targeting of endogenous Smad7 by small interfering RNA inhibited C2C12 muscle cell differentiation, indicating an essential role for Smad7 during myogenesis. Congruent with a role for Smad7 in myogenesis, we observed that the muscle regulatory factor (MyoD) binds to and transactivates the Smad7 proximal promoter region. Finally, we document that Smad7 directly interacts with MyoD and enhances MyoD transcriptional activity. Thus, Smad7 cooperates with MyoD, creating a positive loop to induce Smad7 expression and to promote MyoD driven myogenesis. Taken together, these data implicate Smad7 as a fundamental regulator of differentiation in skeletal muscle cells.




.

So anymore discussion on this? There's one study showing PWO carbs didn't do much and what people have been doing for years is flat out wrong because of one study? The other studies showing the benefits mean nothing anymore? Maybe I'm missing something...so someone please explain.

While I won't go into so much detail as to drool endlessly over Pubmed abstracts but I'm inclined to think that as long as you have a clean meal asap post workout then over thinking all of this is waste.

Taking is a meal of slow releasing cho and casien (oatmeal in low carb milk) a few hours pre-work out and alternating between drinking ample water and a shaker with 20 grams of whey during then everything will be as close to perfection as needed.

Anyone who blathers on otherwise with more studies and so forth may lick my balls

Oswaldo, I'm still not sure what you're getting at. Those studies you posted still don't seem to contradict the study that Spook has posted.

.



succintly.



*relevance of carbohydrates.








*relevance of carbohydrates.





.

I'm not sure what Oswaldo's last point here is...relevance of carbs? Yes, they are relevant...but what is the point of you saying what you said? I don't follow. "Relevance of carbs" isn't a complete thought or sentence.

Want to try that again?
*edit: clarify your thoughts and position*

try to grow without carbs.

That's still not relevant to what's being discussed here.

Please clarify that statement,Oswald because it's either self explanatory or you didn't finish your thought.

Note that I suggested slow,low GI CHO pre several hours w/o so the CHO could be readily utilized when needed during and post w/o,the latter to a lesser degree but still of relevance.*

See,I can use "your words" and the asterisk function as well

sure !

you can eat carbs, before or after, then if you eat carbs after,
are then a waste?






.

English is not his first language, so hop off his dick no homo.

What's with this new "no homo" thing? I'm pretty sure we know you all aren't gay so you don't need to say it. Very weird.

Again, I don't understand Oswaldo's last comments...

Oswaldo: Are you saying carbs pre and post are necessary? Is that all your trying to say?

No homo is just letting you know that I'm not gay. Meet Cameron Giles.

http://www.youtube.com/watch?v=WUxMuk-T0gk