|No matter how much you supplement, running will probably never be the "most anabolic" sport of all. On the other hand, it's certainly less catabolic than broscienctific horror stories of muscle loss and weakness would tell.|
As the authors point out, "the purpose of this study was to determine if a reduced dose of protein and leucine ingested following endurance exercise resulted in a similar anabolic signal impulse for the stimulation of skeletal muscle myofibrillar protein FSR, relative to the higher protein-leucine dose associated previously with improved recovery of performance." (Rowlands. 2014)
In addition Rowlands and colleagues examined the phosphorylation (as a surrogate marker of activity)of signaling proteins within the mammalian target of rapamycin complex 1 (mTORC1) pathway to study the associations between plasma amino acids, translational signaling and myofibrillar FSR. The scientists' hypothesis was that the lower ingested quantity of protein (23 g) plus leucine (5g) would be sufficient to stimulate myofibrillar FSR to an equivalent magnitude to a 3-fold higher amount.
If the latter was possible, Rowland et al. assumed that the mTORC1 pathway phosphorylation between the two protein-leucine would be identical, as well.
The subjects were 12 endurance-trained male cyclists with mean age 30 y, stature 179 cm, and weight 78.1 kg (7.8) completed the study. Mean VO 2 max was 60.4 mL/kg /min with a corresponding Wmax of 323 W.
Following this ride and for the remainder of day and day following (Figure 1B), participants performed no training and were provided with a preweighed diet providing sufficient energy to balanceindividual caloric requirements based on the Harris-Benedict equation for activity factor of 1.6.
"The research design was a randomized single-blind triple crossover. Details of one of the three 7-d experimental blocks and the experimental testing protocol are provided in Figure 1. Two weeks prior to the first experimental block, participants completed a standard test on a Velotron ergometer (Racer Mate, Seattle, USA) to determine VO2 max and Wmax. The next day participants completed a familiarization of the testing procedure (100-min cycle, see below) (Figure 1A).
Figure 1: Graphical overview of the experimental procedure (Rowlands. 2014)
Physical activity and diet were standardized for 4.5-d prior to a 2-d period of control prior toeach experimental testing day. Standardization was prescribed by way of verbal and writing instructions and record in training and dietary recall diaries; participants were asked to replicate on days -6 to -2 (outcomes not recorded). Control of exercise on protocol day -2 (Figure 1A) comprised a 90-min ride with a warm up of 10 min at 30% (Wmax), 8 min at 40%, 2 min at 50%, then intervals (4 x 5 min at 70%) interspersed with three blocks of 3 x 2-min intervals at 85%, 80%, and 75%, respectively, interspersed with 2-min periods at 50%, followed by 5 min at 40%."
Don't be fooled by the amino acid additions: While there is plenty of evidence that "optimized amino acid blends" or "enhancements" are great for supplement producers to justify why they're selling you cheap whey protein / bullshit amino acid products at a crazy price, there is no evidence that they are superior to plain whey protein (see "Are You Still Wasting Money on Amino Acid Products?" | read more)... What? Oh, you want to know why Rowlands et al. do it in the study at hand? Well, because they work for Nestec Ltd. aka Nestlé - I guess that's also why there was no 30g of pure whey isolate control ;-)The 100 min of cycling comprised a warm-up (as above), intervals (%Wmax) of 8 x 2-min (90%), 2 x 5 min (70%), 2 x 2 min (80%) and 3 x 1 min (100%), interspersed with recovery 2-min (50%); and 8 min cool-down (40%). During exercise, participants consumed 800 ml /h of artificially sweetened electrolyte solution to maintain hydration and were fan cooled.
The supplementation regimen
Following exercise, participants showered, and then ingested the first nutrition serving 10-min after cessation of exercise and subsequently every 30 min over the first 90 min of the 240-min assessed recovery (Figure 1B).
As the data in Figure 3 shows, even the "small" shake was potent enough to achieve (almost) maximal fractional 0.95%/h protein synthesis rates.
"The experimental beverages consisted of milk-based drinks containing milk protein concentrat and whey protein isolate (2:1 w/w), L-leucine, maltodextrin and fructose (1:1 w/w), and freeze dried canola oil. Four equal servings of 300 ml of the beverages were consumed during the recovery period for a total volume of 1200 ml.[...] The 15LEU supplement was compared to one-third of the protein-leucine quantity (23.3/5/180/30 g, 5LEU) - an intake hypothesised to yield a bioequivalent similar myofibrillar FSR, and to a nonnitrogenous, isocaloric control (0/0/274/30 g, CON). All beverages also contained 1.4 g NaCl, 14.4 g vanilla essence, and 3.6 g of emulsifier (Paalsgard 0096, Paalsgard A/S, Denmark) per 1200 mL."
Figure 2: Nutrient composition of the test drinks, which contained a whey + milk mixture that was enriched with leucine and spiked with maltodextrine, fructose and canola oil (Rowlands. 2014)
|Figure 3: mTOR (C1+C2) response to protein ingestion (left) corresponding mean fractional protein synthesis (%/h; right) in the 12 healthy male subjects (Rowlands. 2014)|
"The current myofibrillar FSR appeared to be limited by an undefined intramuscular mechanism since only a small and bioequivalent increase in FSR occurred with 15LEU despite sustained 1.4- to 1.9-fold higher plasma leucine and amino-acid concentrations and higher p70S6K-rpS6 phosphorylation." (Rowlands. 2014)With reference to previous research by Atherton et al., Rowlands et. al. speculate that they may have encountered a "muscle full" effect (Atherton. 2010) to explain the discordance between human muscle protein synthesis and mtorc1 signaling.
- Atherton, Philip J., et al. "Muscle full effect after oral protein: time-dependent concordance and discordance between human muscle protein synthesis and mTORC1 signaling." The American journal of clinical nutrition 92.5 (2010): 1080-1088.
- Drummond, Micah J., et al. "Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis." The Journal of physiology 587.7 (2009): 1535-1546.
- Rowlands, David S., et al. "Protein-Leucine Fed Dose Effects on Muscle Protein Synthesis After Endurance Exercise." Medicine & Science in Sports & Exercise (2014).
- Tang, Jason E., et al. "Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men." Journal of Applied Physiology 107.3 (2009): 987-992.