intuitively i would like to think that a certain abount of food onboard allows you to work out long, harder, and more effectively. we also know that BCAAs prior to working out in a fasted state will prevent muscle wasting. her is a provocative study (small sample and limited conclusions) that indicates heavy workouts in a fasted state improve the anabolic potential of a carbohydrate/protein meal post workout:
jb
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Eur J Appl Physiol. 2010 Mar;108(4):791-800.
Increased p70s6k phosphorylation during intake of a protein-carbohydrate drink following resistance exercise in the fasted state.
Deldicque L, De Bock K, Maris M, Ramaekers M, Nielens H, Francaux M, Hespel P.
Department of Biomedical Kinesiology, Research Center for Exercise and Health, FABER, K.U.Leuven, Tervuursevest 101, 3001 Leuven (Heverlee), Belgium.
The present study aimed at comparing the responses of myogenic regulatory factors and signaling pathways involved in muscle protein synthesis after a resistance training session performed in either the fasted or fed state. According to a randomized crossover study design, six young male subjects participated in two experimental sessions separated by 3 weeks. In each session, they performed a standardized resistance training. After the sessions, they received during a 4-h recovery period 6 ml/kg b.w. h of a solution containing carbohydrates (50 g/l), protein hydrolysate (33 g/l), and leucine (16.6 g/l). On one occasion, the resistance exercise session was performed after the intake of a carbohydrate-rich breakfast (B), whereas in the other session they remained fasted (F). Needle biopsies from m. vastus lateralis were obtained before (Rest), and 1 h (+1h) and 4 h (+4h) after exercise. Myogenin, MRF4, and MyoD1 mRNA contents were determined by RT-PCR. Phosphorylation of PKB (protein kinase B), GSK3, p70(s6k) (p70 ribosomal S6 kinase), eIF2B, eEF2 (eukaryotic elongation factor 2), ERK1/2, and p38 was measured via western blotting. Compared with F, the pre-exercise phosphorylation states of PKB and p70(s6k) were higher in B, whereas those of eIF2B and eEF2 were lower. During recovery, the phosphorylation state of p70(s6k) was lower in B than in F (p = 0.02). There were no differences in basal mRNA contents between B and F. However, compared with F at +1h, MyoD1 and MRF4 mRNA contents were lower in B (p < 0.05). Our results indicate that prior fasting may stimulate the intramyocellular anabolic response to ingestion of a carbohydrate/protein/leucine mixture following a heavy resistance training session.
Counter-intuitive. Good read jb. Thanks!
"In any contest between power and patience, bet on patience."
~W.B. Prescott
"Only two things are infinite, the universe and human stupidity, and I'm not sure about the former."
~Albert Einstein
Ive always worked out on an empty stomach. However I always nursed a homade protein shake 2 scoops of pure whey with on packet of weighltoss oatmel. Not the greatest tasting but fuels like a muther fucker
i was the 1997 International Spelling Bee Winnur
im not sure its the fasting more so than the lack of carbohydrates as the breakfast was carb rich
in theory you should be able to recreate an exceptional intracellular anabolic response daily by precisely timing carbs at peak times
fasted workouts improve endurance gains via upregulation of the "thrifty" genes (AMPK etc.) but it is metabolically very stressful & I'm not sure how it aplies to body building- usually AMPK has the opposite effect of mTOR- feeding increases mTOR activity & reduces AMPK, so for BB anything that activates mTOR would be a good thing
it appears that P70 is upregulated post workout in the fasted paradigm whereas it is up regulated during the workout in the carbohydrate paradigm but not post workout. since P70 is downstream of the Akt/mTOR pathway and is a positive correlator of increased mTOR this leads me to believe that this might be a good thing for bbrs since mTOR is pivotal in muscle hypertrophy.
jb
we know that bcaas taken prior to workout in a fasted state will prevent muscle wasting so it might be a good stratedgy to take bcaas prior to working out in a fasted state followed by bcaas.carns.protein.
just in case anyone is interested, here is a study showing a mechanism of action of Testosterone mediating akt via the androgen receptor. i mention it because we were just talking about akt mediating mTOR leading to muscle hypertrophy.
jb
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Endocrinology. 2010 Mar 1. [Epub ahead of print]
Androgen Receptor-Dependent Activation of Endothelial Nitric Oxide Synthase in Vascular Endothelial Cells: Role of Phosphatidylinositol 3-Kinase/Akt Pathway.
Yu J, Akishita M, Eto M, Ogawa S, Son BK, Kato S, Ouchi Y, Okabe T.
Departments of Integrated Traditional Medicine (J.Y., T.O.) and Geriatric Medicine (M.A., M.E., S.O., B.-K.S., Y.O.), Graduate School of Medicine, and the Institute of Molecular and Cellular Bioscience (S.K.), The University of Tokyo, Tokyo 113-8655, Japan.
The mechanisms of testosterone-induced vasodilatation are not fully understood. This study investigated the effect of testosterone on nitric oxide (NO) synthesis and its molecular mechanism using human aortic endothelial cells (HAEC). Testosterone at physiological concentrations (1-100 nM) induced a rapid (15-30 min) increase in NO production, which was associated with phosphorylation and activation of endothelial NO synthase (eNOS). Then, the involvement of the androgen receptor (AR), which is abundantly expressed in HAEC, was examined. The effect of testosterone on eNOS activation and NO production were abolished by pretreatment with an AR antagonist nilutamide and by transfection with AR small interference RNA. In contrast, testosterone-induced eNOS phosphorylation was unchanged by pretreatment with an aromatase inhibitor or by transfection with ERalpha small interference RNA. 5alpha-Dihydrotestosterone, a nonaromatizable androgen, also stimulated eNOS phosphorylation. Next, the signaling cascade that leads to eNOS phosphorylation was explored. Testosterone stimulated rapid phosphorylation of Akt in a time- and dose-dependent manner, with maximal response at 15-60 min. The rapid phosphorylation of eNOS or NO production induced by testosterone was inhibited by Akt inhibitor SH-5 or by phosphatidylinositol (PI) 3-kinase inhibitor wortmannin. Co-immunoprecipitation assays revealed a testosterone-dependent interaction between AR and the p85alpha subunit of PI3-kinase. In conclusion, testosterone rapidly induces NO production via AR-dependent activation of eNOS in HAEC. Activation of PI3-kinase/Akt signaling and the direct interaction of AR with p85alpha are involved, at least in part, in eNOS phosphorylation.
interesting link between test & eNOS/ NO, perhaps preloading with NO donors could help the T response
like citrulline? we know their is a performace enhancement, be interesting to see if there is anything out there on hypertrophy.
jb
BINGO!
J Nutr. 2007 Jun;137(6 Suppl 2):1621S-1625S.
Citrulline: a new player in the control of nitrogen homeostasis.
Moinard C, Cynober L.
Laboratoire de Biologie de la Nutrition, EA 2498, Facult� de Pharmacie, Universit� Paris Descartes, and Laboratoire Biochimie, H�tel-Dieu, AP-HP, Paris 75004, France. [email protected]
Citrulline (CIT) is an amino acid that is not involved in protein synthesis but that is tightly linked to arginine (ARG) metabolism. CIT displays a very specific metabolism: In the 1980s, Windmuller demonstrated that the small intestine releases CIT, which is mainly taken up by the kidney and metabolized into ARG. Because CIT is not taken up by the liver, this ARG-CIT-ARG cycle can be seen as a means of protecting dietary ARG from liver degradation and of sustaining protein homeostasis. These observations have led to the concept that plasma CIT concentration would be a good marker of intestinal failure in short bowel syndrome. Hence, in massive intestinal resection, citrullinemia is greatly reduced, and this is proportional to the severity of the intestinal disease. This concept was then extended to other situations in which the intestinal function is compromised. The data strongly suggest that CIT may be a conditionally essential amino acid in situations where the intestinal function is compromised. Recent data support this idea. Thus, CIT supplementation is able to restore nitrogen balance, generate large amounts of ARG in rats with short bowel syndrome, and increase muscle protein content (+20%) as well as muscle protein synthesis (+90%) in elderly malnourished rats. Finally, recent data indicate that CIT per se could be able to stimulate muscle protein synthesis. Hence, CIT could play a pivotal role in maintaining protein homeostasis, and the determination of the underlying mechanisms involved in its action should be important for the development of new nutritional strategies in malnourished patients with compromised intestinal functions.
So leucine preworkout. Dextrose, whey, leucine, arginine,ornithine,creatine and citrulline post workout?
Seabiscuit Hogg is a fictious internet character. It is not recommended that you receive medical advice from fictious internet characters.
SBH :)
Arginine in the pre workout stack could only be a good thing
arginine...Nitric Oxide... probably about 10,00 hits on pubmed!
Best thing I've ever had for NO release is sodium nitrite, massive flush about 5 mins after ingesting, i think its from stomach acid conversion of nitrite
Citrulline and ornithine actually convert to a higher blood level of arginine than arginine itselt. Anyway, it would be better to take NO aminos preworkout? Or pre and post like leucine? Where do you get sodium nitrite?
Seabiscuit Hogg is a fictious internet character. It is not recommended that you receive medical advice from fictious internet characters.
SBH :)
i would still take leucine pre workout as well as post. i would also skip the arginine and ornithine in favor of citrulline maleate or l citrulline pre-workout. i just came across another ++study on NOS and muscle building, will post up tonight.