Resistance Exercise Augments Postprandial Overnight Muscle Protein Synthesis Rates

Trommelen, Jorn; Holwerda, Andrew M.; Kouw, Imre W. K.; Langer, Henning T.; Halson, Shona L.; Rollo, Ian; Verdijk, Lex B.; Loon, Luc J. C. van

doi:10.1249/mss.0000000000001045

“…In the present study, we provided a bolus of 20 g of intrinsically labelled milk protein (together with 45 g of carbohydrates) after resistance-type exercise. In line with previous research (Gorissen et al 2014;Groen et al 2015;Trommelen et al 2016), we showed that the dietary protein-derived amino acids are effectively being taken up and released in the systemic circulation ( Fig. 4), thereby providing precursors for de novo myofibrillar protein synthesis (Fig.…”

Section: Discussionsupporting

confidence: 91%

Postexercise cooling impairs muscle protein synthesis rates in recreational athletes

Fuchs

¹

,

Kouw

²

,

Churchward‐Venne

³

et al. 2019

The Journal of Physiology

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Key points Protein ingestion and cooling are strategies employed by athletes to improve postexercise recovery and, as such, to facilitate muscle conditioning. However, whether cooling affects postprandial protein handling and subsequent muscle protein synthesis rates during recovery from exercise has not been assessed. We investigated the effect of postexercise cooling on the incorporation of dietary protein‐derived amino acids into muscle protein and acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during recovery from resistance‐type exercise over 2 weeks. Cold‐water immersion during recovery from resistance‐type exercise lowers the capacity of the muscle to take up and/or direct dietary protein‐derived amino acids towards de novo myofibrillar protein accretion. In addition, cold‐water immersion during recovery from resistance‐type exercise lowers myofibrillar protein synthesis rates during prolonged resistance‐type exercise training. Individuals aiming to improve skeletal muscle conditioning should reconsider applying cooling as a part of their postexercise recovery strategy. Abstract We measured the impact of postexercise cooling on acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during adaptation to resistance‐type exercise over 2 weeks. Twelve healthy males (aged 21 ± 2 years) performed a single resistance‐type exercise session followed by water immersion of both legs for 20 min. One leg was immersed in cold water (8°C: CWI), whereas the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g of intrinsically (l‐[1‐13C]‐phenylalanine and l‐[1‐13C]‐leucine) labelled milk protein with 45 g of carbohydrates. In addition, primed continuous l‐[ring‐2H5]‐phenylalanine and l‐[1‐13C]‐leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5 h recovery period. In addition, deuterated water (2H2O) was applied with the collection of saliva, blood and muscle biopsies over 2 weeks to assess the effects of postexercise cooling with protein intake on myofibrillar protein synthesis rates during more prolonged resistance‐type exercise training (thereby reflecting short‐term training adaptation). Incorporation of dietary protein‐derived l‐[1‐13C]‐phenylalanine into myofibrillar protein was significantly lower in CWI compared to CON (0.016 ± 0.006 vs. 0.021 ± 0.007 MPE; P = 0.016). Postexercise myofibrillar protein synthesis rates were lower in CWI compared to CON based upon l‐[1‐13C]‐leucine (0.058 ± 0.011 vs. 0.072 ± 0.017% h−1, respectively; P = 0.024) and l‐[ring‐2H5]‐phenylalanine (0.042 ± 0.009 vs. 0.053 ± 0.013% h−1, respectively; P = 0.025). Daily myofibrillar protein synthesis rates assessed over 2 weeks were significantly lower in CWI compared to CON (1.48 ± 0.17 vs. 1.67 ± 0.36% day−1, respectively; P = 0.042). Cold‐water immersion during recovery from resistance‐type e...

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“…In line with previous research (Gorissen et al 2014;Groen et al 2015;Trommelen et al 2016), we showed that the dietary protein-derived amino acids are effectively being taken up and released in the systemic circulation (Fig. In line with previous research (Gorissen et al 2014;Groen et al 2015;Trommelen et al 2016), we showed that the dietary protein-derived amino acids are effectively being taken up and released in the systemic circulation (Fig.…”

Section: Discussionsupporting

confidence: 91%

Post-exercise Cooling Impairs Muscle Protein Synthesis Rates In Healthy Young Males

Fuchs

¹

,

Kouw

²

,

Churchward‐Venne

³

et al. 2019

Medicine &Amp; Science in Sports &Amp; Exercise

Self Cite

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Key points Protein ingestion and cooling are strategies employed by athletes to improve postexercise recovery and, as such, to facilitate muscle conditioning. However, whether cooling affects postprandial protein handling and subsequent muscle protein synthesis rates during recovery from exercise has not been assessed. We investigated the effect of postexercise cooling on the incorporation of dietary protein‐derived amino acids into muscle protein and acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during recovery from resistance‐type exercise over 2 weeks. Cold‐water immersion during recovery from resistance‐type exercise lowers the capacity of the muscle to take up and/or direct dietary protein‐derived amino acids towards de novo myofibrillar protein accretion. In addition, cold‐water immersion during recovery from resistance‐type exercise lowers myofibrillar protein synthesis rates during prolonged resistance‐type exercise training. Individuals aiming to improve skeletal muscle conditioning should reconsider applying cooling as a part of their postexercise recovery strategy. Abstract We measured the impact of postexercise cooling on acute postprandial (hourly) as well as prolonged (daily) myofibrillar protein synthesis rates during adaptation to resistance‐type exercise over 2 weeks. Twelve healthy males (aged 21 ± 2 years) performed a single resistance‐type exercise session followed by water immersion of both legs for 20 min. One leg was immersed in cold water (8°C: CWI), whereas the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g of intrinsically (l‐[1‐13C]‐phenylalanine and l‐[1‐13C]‐leucine) labelled milk protein with 45 g of carbohydrates. In addition, primed continuous l‐[ring‐2H5]‐phenylalanine and l‐[1‐13C]‐leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5 h recovery period. In addition, deuterated water (2H2O) was applied with the collection of saliva, blood and muscle biopsies over 2 weeks to assess the effects of postexercise cooling with protein intake on myofibrillar protein synthesis rates during more prolonged resistance‐type exercise training (thereby reflecting short‐term training adaptation). Incorporation of dietary protein‐derived l‐[1‐13C]‐phenylalanine into myofibrillar protein was significantly lower in CWI compared to CON (0.016 ± 0.006 vs. 0.021 ± 0.007 MPE; P = 0.016). Postexercise myofibrillar protein synthesis rates were lower in CWI compared to CON based upon l‐[1‐13C]‐leucine (0.058 ± 0.011 vs. 0.072 ± 0.017% h−1, respectively; P = 0.024) and l‐[ring‐2H5]‐phenylalanine (0.042 ± 0.009 vs. 0.053 ± 0.013% h−1, respectively; P = 0.025). Daily myofibrillar protein synthesis rates assessed over 2 weeks were significantly lower in CWI compared to CON (1.48 ± 0.17 vs. 1.67 ± 0.36% day−1, respectively; P = 0.042). Cold‐water immersion during recovery from resistance‐type e...

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“…It should be noted, however, that most postprandial plasma amino acid parameters (with the exception of total essential amino acids) and insulin levels were numerically higher when compared with the 60 g mycoprotein condition, and remained consistently elevated for the entire 4 h postprandial period (selected as a typical 'real world' postprandial period before subsequent meal consumption) in the 80 g mycoprotein condition only. This may be of relevance when considering postprandial periods expected to extend beyond 4 h. For example, pre-sleep protein is an increasingly popular strategy for augmenting muscle protein synthesis rates during the extended overnight period (52)(53)(54)(55)(56) , an approach also shown to augment the adaptive response to prolonged training (57) . Likely as a consequence of this extended overnight postprandial period, these studies have suggested that 'slower proteins' capable of facilitating more prolonged hyperaminoacidaemia, and in relatively larger doses, may be optimal for the stimulation of muscle protein synthesis rates.…”

Section: Discussionmentioning

confidence: 99%

Mycoprotein represents a bioavailable and insulinotropic non-animal-derived dietary protein source: a dose–response study

Dunlop

¹

,

Kilroe

²

,

Bowtell

³

et al. 2017

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The anabolic potential of a dietary protein is determined by its ability to elicit postprandial rises in circulating essential amino acids and insulin. Minimal data exist regarding the bioavailability and insulinotropic effects of non-animal-derived protein sources. Mycoprotein is a sustainable and rich source of non-animal-derived dietary protein. We investigated the impact of mycoprotein ingestion, in a dose-response manner, on acute postprandial hyperaminoacidaemia and hyperinsulinaemia. In all, twelve healthy young men completed five experimental trials in a randomised, single-blind, cross-over design. During each trial, volunteers consumed a test drink containing either 20 g milk protein (MLK20) or a mass matched (not protein matched due to the fibre content) bolus of mycoprotein (20 g; MYC20), a protein matched bolus of mycoprotein (40 g; MYC40), 60 g (MYC60) or 80 g (MYC80) mycoprotein. Circulating amino acid, insulin and uric acid concentrations, and clinical chemistry profiles, were assessed in arterialised venous blood samples during a 4-h postprandial period. Mycoprotein ingestion resulted in slower but more sustained hyperinsulinaemia and hyperaminoacidaemia compared with milk when protein matched, with overall bioavailability equivalent between conditions (P > 0·05). Increasing the dose of mycoprotein amplified these effects, with some evidence of a plateau at 60-80 g. Peak postprandial leucine concentrations were 201 (SEM 24) (30 min), 118 (SEM 10) (90 min), 150 (SEM 14) (90 min), 173 (SEM 23) (45 min) and 201 (SEM 21 (90 min) µmol/l for MLK20, MYC20, MYC40, MYC60 and MYC80, respectively. Mycoprotein represents a bioavailable and insulinotropic dietary protein source. Consequently, mycoprotein may be a useful source of dietary protein to stimulate muscle protein synthesis rates.

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Resistance Exercise Augments Postprandial Overnight Muscle Protein Synthesis Rates

Abstract: Resistance-type exercise performed in the evening augments the overnight muscle protein synthetic response to presleep protein ingestion and allows more of the ingested protein-derived amino acids to be used for de novo myofibrillar protein synthesis during overnight sleep.

Cited by 61 publications

References 27 publications

Postexercise cooling impairs muscle protein synthesis rates in recreational athletes

Postexercise cooling impairs muscle protein synthesis rates in recreational athletes

Post-exercise Cooling Impairs Muscle Protein Synthesis Rates In Healthy Young Males

Mycoprotein represents a bioavailable and insulinotropic non-animal-derived dietary protein source: a dose–response study

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