Potato protein ingestion increases muscle protein synthesis rates at rest and during recovery from exercise in humans

Introduction Plant-derived proteins have received considerable attention as an alternative to animal-based proteins and are now frequently used in both plant-based diets and sports nutrition products. However, little information is available on the anabolic properties of potato-derived protein. This study compares muscle protein synthesis rates after the ingestion of 30 g potato protein versus 30 g milk protein at rest and during recovery from a single bout of resistance exercise in healthy, young males. Methods In a randomized, double-blind, parallel-group design, 24 healthy young males (24 ± 4 yr) received primed continuous l-[ring-13C6]-phenylalanine infusions while ingesting 30 g potato-derived protein or 30 g milk protein after a single bout of unilateral resistance exercise. Blood and muscle biopsies were collected for 5 h after protein ingestion to assess postprandial plasma amino acid profiles and mixed muscle protein synthesis rates at rest and during recovery from exercise. Results Ingestion of both potato and milk protein increased mixed muscle protein synthesis rates when compared with basal postabsorptive values (from 0.020% ± 0.011% to 0.053% ± 0.017%·h−1 and from 0.021% ± 0.014% to 0.050% ± 0.012%·h−1, respectively; P < 0.001), with no differences between treatments (P = 0.54). In the exercised leg, mixed muscle protein synthesis rates increased to 0.069% ± 0.019% and 0.064% ± 0.015%·h−1 after ingesting potato and milk protein, respectively (P < 0.001), with no differences between treatments (P = 0.52). The muscle protein synthetic response was greater in the exercised compared with the resting leg (P < 0.05). Conclusions Ingestion of 30 g potato protein concentrate increases muscle protein synthesis rates at rest and during recovery from exercise in healthy, young males. Muscle protein synthesis rates after the ingestion of 30 g potato protein do not differ from rates observed after ingesting an equivalent amount of milk protein

Potato Protein Ingestion Increases Muscle Protein Synthesis Rates at Rest and during Recovery from Exercise in Humans

INTRODUCTION: Plant-derived proteins have received considerable attention as an alternative to animal-based proteins and are now frequently used in both plant-based diets and sports nutrition products. However, little information is available on the anabolic properties of potato-derived protein. This study compares muscle protein synthesis rates after the ingestion of 30 g potato protein versus 30 g milk protein at rest and during recovery from a single bout of resistance exercise in healthy, young males. METHODS: In a randomized, double-blind, parallel-group design, 24 healthy young males (24 ± 4 yr) received primed continuous l-[ring-(13)C(6)]-phenylalanine infusions while ingesting 30 g potato-derived protein or 30 g milk protein after a single bout of unilateral resistance exercise. Blood and muscle biopsies were collected for 5 h after protein ingestion to assess postprandial plasma amino acid profiles and mixed muscle protein synthesis rates at rest and during recovery from exercise. RESULTS: Ingestion of both potato and milk protein increased mixed muscle protein synthesis rates when compared with basal postabsorptive values (from 0.020% ± 0.011% to 0.053% ± 0.017%·h(−1) and from 0.021% ± 0.014% to 0.050% ± 0.012%·h(−1), respectively; P < 0.001), with no differences between treatments (P = 0.54). In the exercised leg, mixed muscle protein synthesis rates increased to 0.069% ± 0.019% and 0.064% ± 0.015%·h(−1) after ingesting potato and milk protein, respectively (P < 0.001), with no differences between treatments (P = 0.52). The muscle protein synthetic response was greater in the exercised compared with the resting leg (P < 0.05). CONCLUSIONS: Ingestion of 30 g potato protein concentrate increases muscle protein synthesis rates at rest and during recovery from exercise in healthy, young males. Muscle protein synthesis rates after the ingestion of 30 g potato protein do not differ from rates observed after ingesting an equivalent amount of milk protein

NK Cell–Like Behavior of Vα14i NK T Cells during MCMV Infection

Immunity to the murine cytomegalovirus (MCMV) is critically dependent on the innate response for initial containment of viral replication, resolution of active infection, and proper induction of the adaptive phase of the anti-viral response. In contrast to NK cells, the Vα14 invariant natural killer T cell response to MCMV has not been examined. We found that Vα14i NK T cells become activated and produce significant levels of IFN-γ, but do not proliferate or produce IL-4 following MCMV infection. In vivo treatment with an anti-CD1d mAb and adoptive transfer of Vα14i NK T cells into MCMV-infected CD1d−/− mice demonstrate that CD1d is dispensable for Vα14i NK T cell activation. In contrast, both IFN-α/β and IL-12 are required for optimal activation. Vα14i NK T cell–derived IFN-γ is partially dependent on IFN-α/β but highly dependent on IL-12. Vα14i NK T cells contribute to the immune response to MCMV and amplify NK cell–derived IFN-γ. Importantly, mortality is increased in CD1d−/− mice in response to high dose MCMV infection when compared to heterozygote littermate controls. Collectively, these findings illustrate the plasticity of Vα14i NK T cells that act as effector T cells during bacterial infection, but have NK cell–like behavior during the innate immune response to MCMV infection

Raw Eggs to Support Post-Exercise Recovery in Healthy Young Men: Did Rocky Get It Right or Wrong?

BACKGROUND: Egg protein is ingested during recovery from exercise to facilitate the post-exercise increase in muscle protein synthesis rates and, as such, to support the skeletal muscle adaptive response to exercise training. The impact of cooking egg protein on post-exercise muscle protein synthesis is unknown. OBJECTIVES: To compare the impact of ingesting unboiled (raw) versus boiled eggs during post-exercise recovery on postprandial myofibrillar protein synthesis rates. METHODS: In a parallel design, forty-five healthy, resistance trained young men (age: 24 (95%CI: 23-25) y) were randomly assigned to ingest 5 raw eggs (∼30 g protein), 5 boiled eggs (∼30 g protein), or a control breakfast (∼5 g protein) during recovery from a single session of whole-body resistance-type exercise. Primed continuous L-[ring-13C6]-phenylalanine infusions were applied, with frequent blood sampling. Muscle biopsies were collected immediately after cessation of resistance exercise and at 2 and 5 h into the post-exercise recovery period. Primary (myofibrillar protein synthesis rates) and secondary (plasma amino acid concentrations) outcomes were analyzed using repeated-measures (Time*Group) ANOVA. RESULTS: Ingestion of eggs significantly increased plasma essential amino acid concentrations, with 20% higher peak concentrations following ingestion of boiled compared with raw eggs (Time*Group: P < 0.001). Myofibrillar protein synthesis rates were significantly increased during the post-exercise period when compared to basal, post-absorptive values in all groups (2-4 fold increase: P < 0.001). Postprandial myofibrillar protein synthesis rates were 20% higher after ingesting raw eggs (0.067%/h (95%CI:0.056-0.077); effect size (Cohen's d): 0.63), and 18% higher after ingesting boiled eggs (0.065%/h (95%CI:0.058-0.073); effect size: 0.69) when compared to the control breakfast (0.056%/h (95%CI:0.048-0.063), with no significant differences between groups (Time*Group: P = 0.077). CONCLUSIONS: The ingestion of raw, as opposed to boiled, eggs attenuates the postprandial rise in circulating essential amino acid concentrations. However, post-exercise muscle protein synthesis rates do not differ after ingestion of 5 raw versus 5 boiled eggs in healthy young men. Trial registration: NL6506

Raw Eggs to Support Post-Exercise Recovery in Healthy Young Men:Did Rocky Get It Right or Wrong?

Background Egg protein is ingested during recovery from exercise to facilitate the postexercise increase in muscle protein synthesis rates and, as such, to support the skeletal muscle adaptive response to exercise training. The impact of cooking egg protein on postexercise muscle protein synthesis is unknown. Objectives We sought to compare the impact of ingesting unboiled (raw) compared with boiled eggs during postexercise recovery on postprandial myofibrillar protein synthesis rates. Methods In a parallel design, 45 healthy, resistance-trained young men (age: 24 y; 95% CI: 23, 25 y) were randomly assigned to ingest 5 raw eggs (∼30 g protein), 5 boiled eggs (∼30 g protein), or a control breakfast (∼5 g protein) during recovery from a single session of whole-body resistance-type exercise. Primed continuous L-[ring-13C6]-phenylalanine infusions were applied, with frequent blood sampling. Muscle biopsies were collected immediately after cessation of resistance exercise and at 2 and 5 h into the postexercise recovery period. Primary (myofibrillar protein synthesis rates) and secondary (plasma amino acid concentrations) outcomes were analyzed using repeated-measures (time × group) ANOVA. Results Ingestion of eggs significantly increased plasma essential amino acid (EAA) concentrations, with 20% higher peak concentrations following ingestion of boiled compared with raw eggs (time × group: P < 0.001). Myofibrillar protein synthesis rates were significantly increased during the postexercise period when compared with basal, postabsorptive values in all groups (2–4-fold increase: P < 0.001). Postprandial myofibrillar protein synthesis rates were 20% higher after ingesting raw eggs [0.067%/h; 95% CI: 0.056, 0.077%/h; effect size (Cohen d): 0.63], and 18% higher after ingesting boiled eggs (0.065%/h; 95% CI: 0.058, 0.073%/h; effect size: 0.69) when compared with the control breakfast (0.056%/h; 95% CI: 0.048, 0.063%/h), with no significant differences between groups (time × group: P = 0.077). Conclusions The ingestion of raw, as opposed to boiled, eggs attenuates the postprandial rise in circulating EAA concentrations. However, postexercise muscle protein synthesis rates do not differ after ingestion of 5 raw compared with 5 boiled eggs in healthy young men. This trial was registered at the Nederlands Trial Register as NL6506 (www.trialregister.nl)

Potato Protein Ingestion Increases Muscle Protein Synthesis Rates at Rest and during Recovery from Exercise in Humans

INTRODUCTION: Plant-derived proteins have received considerable attention as an alternative to animal based proteins and are now frequently used in both plant-based diets and sports nutrition products. However, little information is available on the anabolic properties of potato-derived protein. This study compares muscle protein synthesis rates following the ingestion of 30 g potato protein versus 30 g milk protein at rest and during recovery from a single bout of resistance exercise in healthy, young males. METHODS: In a randomized, double blind, parallel-group design, 24 healthy young males (24 ± 4y) received primed continuous L-[ring-13C6]-phenylalanine infusions while ingesting 30 g potato derived protein or 30 g milk protein following a single bout of unilateral resistance exercise. Blood and muscle biopsies were collected for 5 hours following protein ingestion to assess post-prandial plasma amino acid profiles and mixed muscle protein synthesis rates at rest and during recovery from exercise. RESULTS: Ingestion of both potato and milk protein increased mixed muscle protein synthesis rates when compared to basal post-absorptive values (from 0.020 ± 0.011 to 0.053 ± 0.017 %·h-1 and from 0.021 ± 0.014 to 0.050 ± 0.012 %·h-1, respectively (P < 0.001)), with no differences between treatments (P = 0.54). In the exercised leg, mixed muscle protein synthesis rates increased to 0.069 ± 0.019 and 0.064 ± 0.015 %·h-1 after ingesting potato and milk protein, respectively (P < 0.001), with no differences between treatments (P = 0.52). The muscle protein synthetic response was greater in the exercised compared with the resting leg (P < 0.05). CONCLUSIONS: Ingestion of 30 g potato protein concentrate increases muscle protein synthesis rates at rest and during recovery from exercise in healthy, young males. Muscle protein synthesis rates following the ingestion of 30 g potato protein do not differ from rates observed after ingesting an equivalent amount of milk protein

Insects are a viable protein source for human consumption : From insect protein digestion to postprandial muscle protein synthesis in vivo in humans : A double-blind randomized trial

Background Insects have recently been identified as a more sustainable protein-dense food source and may represent a viable alternative to conventional animal-derived proteins. Objectives We aimed to compare the impacts of ingesting lesser mealworm– and milk-derived protein on protein digestion and amino acid absorption kinetics, postprandial skeletal muscle protein synthesis rates, and the incorporation of dietary protein–derived amino acids into de novo muscle protein at rest and during recovery from exercise in vivo in humans. Methods In this double-blind randomized controlled trial, 24 healthy, young men ingested 30 g specifically produced, intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled lesser mealworm– or milk-derived protein after a unilateral bout of resistance-type exercise. Primed continuous L-[ring-2H5]-phenylalanine, L-[ring-3,5-2H2]-tyrosine, and L-[1-13C]-leucine infusions were applied, with frequent collection of blood and muscle tissue samples. Results A total of 73% ± 7% and 77% ± 7% of the lesser mealworm and milk protein–derived phenylalanine was released into the circulation during the 5 h postprandial period, respectively, with no significant differences between groups (P 0.05). Incorporation of mealworm and milk protein-derived L-[1-13C]-phenylalanine into de novo muscle protein was greater after exercise than at rest (P 0.05). Conclusions Ingestion of a meal-like amount of lesser mealworm–derived protein is followed by rapid protein digestion and amino acid absorption and increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial protein handling of lesser mealworm does not differ from ingesting an equivalent amount of milk protein concentrate in vivo in humans. This trial was registered at www.trialregister.nl as NL6897

Branched-chain amino acid and branched-chain ketoacid ingestion increases muscle protein synthesis rates in vivo in older adults:a double-blind, randomized trial

BACKGROUND: Protein ingestion increases muscle protein synthesis rates. However, limited data are currently available on the effects of branched-chain amino acid (BCAA) and branched-chain ketoacid (BCKA) ingestion on postprandial muscle protein synthesis rates. OBJECTIVE: The aim of this study was to compare the impact of ingesting 6 g BCAA, 6 g BCKA, and 30 g milk protein (MILK) on the postprandial rise in circulating amino acid concentrations and subsequent myofibrillar protein synthesis rates in older males. METHODS: In a parallel design, 45 older males (age: 71 ± 1 y; BMI: 25.4 ± 0.8 kg/m2) were randomly assigned to ingest a drink containing 6 g BCAA, 6 g BCKA, or 30 g MILK. Basal and postprandial myofibrillar protein synthesis rates were assessed by primed continuous l-[ring-13C6]phenylalanine infusions with the collection of blood samples and muscle biopsies. RESULTS: Plasma BCAA concentrations increased following test drink ingestion in all groups, with greater increases in the BCAA and MILK groups compared with the BCKA group (P  0.05). Myofibrillar protein synthesis rates during the late postprandial phase (2-5 h) remained elevated in the MILK group (0.039 ± 0.004%/h; P  0.05). CONCLUSIONS: Ingestion of 6 g BCAA, 6 g BCKA, and 30 g MILK increases myofibrillar protein synthesis rates during the early postprandial phase (0-2 h) in vivo in healthy older males. The postprandial increase following the ingestion of 6 g BCAA and BCKA is short-lived, with higher myofibrillar protein synthesis rates only being maintained following the ingestion of an equivalent amount of intact milk protein. This trial was registered at Nederlands Trial Register (www.trialregister.nl) as NTR6047