Graded Replacement of Carbohydrate-Rich Breakfast Products with Dairy Products: Effects on Postprandial Aminoacidemia, Glycemic Control, Bone Metabolism, and Satiety.

BACKGROUND: Postprandial metabolic responses following dairy consumption have mostly been studied using stand-alone dairy products or milk-derived nutrients. OBJECTIVE: Assessing the impact of ingesting dairy products as part of a common breakfast on postprandial aminoacidemia, glycemic control, markers of bone metabolism, and satiety. METHODS: In this randomized, crossover study, 20 healthy young males and females consumed on 3 separate occasions an iso-energetic breakfast containing no dairy (NO-D), 1 dairy (ONE-D), or 2 dairy (TWO-D) products. Postprandial concentrations of amino acids, glucose, insulin, glucagon-like peptide-1 (GLP-1), calcium, parathyroid hormone (PTH), and markers of bone formation (P1NP) and resorption (CTX-I) were measured before and up to 300 min after initiating the breakfast, along with VAS-scales to assess satiety. RESULTS: Plasma essential and branched-chained amino acids availability (expressed as total area under the curve (tAUC)) increased in a dose-dependent manner (P<0.05 for all comparisons). Plasma glucose tAUCs were lower in ONE-D and TWO-D compared with NO-D (P<0.05 for both comparisons). Plasma GLP-1 tAUC increased in a dose-dependent manner (P<0.05 for all comparisons), whereas no differences were observed in plasma insulin tAUC between conditions (P>0.05 for all comparisons). Serum calcium tAUCs were higher in ONE-D and TWO-D compared with NO-D (P<0.05 for both comparisons), along with lower PTH tAUCs in ONE-D and TWO-D compared with NO-D (P=0.001 for both comparisons). In accordance, serum CTX-I concentrations were lower in the late postprandial period in ONE-D and TWO-D compared with NO-D (P<0.01 for both comparisons). No differences were observed in P1NP tAUCs between conditions (P>0.05). The tAUC for satiety was higher in TWO-D compared with NO-D and ONE-D (P<0.05 for both comparisons). CONCLUSIONS: Iso-energetic replacement of a carbohydrate-rich breakfast component with one serving of dairy improves postprandial amino acid availability, glycemic control, and bone metabolism. Adding a second serving of dairy in lieu of carbohydrates augments postprandial amino acid and GLP-1 concentrations while further promoting satiety. This study was registered at https://doi.org/10.1186/ISRCTN13531586 with Clinical Trial Registry number ISRCTN13531586.

Administration of Free Amino Acids Improves Exogenous Amino Acid Availability when Compared with Intact Protein in Critically Ill Patients: A Randomized Controlled Study.

BACKGROUND: Protein digestion and amino acid absorption appear compromised in critical illness. The provision of enteral feeds with free amino acids rather than intact protein may improve postprandial amino acid availability. OBJECTIVE: Our objective was to quantify the uptake of diet-derived phenylalanine after the enteral administration of intact protein compared with an equivalent amount of free amino acids in critically ill patients. METHODS: Sixteen patients who were mechanically ventilated in intensive care unit (ICU) at risk of malabsorption received a primed continuous infusion of L-[ring-2H5]-phenylalanine and L-[ring-3,5-2H2]-tyrosine after an overnight fast. Patients were randomly allocated to receive 20 g intrinsically L-[1-13C]-phenylalanine-labeled milk protein or an equivalent amount of amino acids labeled with free L-[1-13C]-phenylalanine via a nasogastric tube over a 2-h period. Protein digestion and amino acid absorption kinetics and whole-body protein net balance were assessed throughout a 6-h period. RESULTS: After enteral nutrient infusion, both plasma phenylalanine and leucine concentrations increased (P-time < 0.001), with a more rapid and greater rise after free amino acid compared with intact protein administration (P-time × treatment = 0.003). Diet-derived phenylalanine released into the circulation was 25% greater after free amino acids compared with intact protein administration [68.7% (confidence interval {CI}: 62.3, 75.1%) compared with 43.8% (CI: 32.4, 55.2%), respectively; P < 0.001]. Whole-body protein net balance became positive after nutrient administration (P-time < 0.001) and tended to be more positive after free amino acid in provision (P-time × treatment = 0.07). CONCLUSIONS: The administration of free amino acids as opposed to intact protein further increases postprandial plasma amino acid availability in critically ill patients, allowing more diet-derived phenylalanine to become available to peripheral tissues. This trial was registered at clinicaltrials.gov as NCT04791774.

Acute Quark Ingestion Increases Muscle Protein Synthesis Rates at Rest with a Further Increase after Exercise in Young and Older Adult Males in a Parallel-Group Intervention Trial.

BACKGROUND: Ingestion of protein concentrates or isolates increases muscle protein synthesis rates in young and older adults. There is far less information available on the anabolic response following the ingestion of dairy wholefoods, which are commonly consumed in a normal diet. OBJECTIVES: This study investigates whether ingestion of 30 g protein provided as quark increases muscle protein synthesis rates at rest and whether muscle protein synthesis rates are further increased after resistance exercise in young and older adult males. METHODS: In this parallel-group intervention trial, 14 young (18-35 y) and 15 older (65-85 y) adult males ingested 30 g protein provided as quark after a single-legged bout of resistance exercise on leg press and leg extension machines. Primed, continuous intravenous L-[ring-13C6]-phenylalanine infusions were combined with the collection of blood and muscle tissue samples to assess postabsorptive and 4-h postprandial muscle protein synthesis rates at rest and during recovery from exercise. Data represent means ± SDs; η2 was used to measure the effect size. RESULTS: Plasma total amino acid and leucine concentrations increased after quark ingestion in both groups (both time: P < 0.001; η2 > 0.8), with no differences between groups (time × group: P = 0.127 and P = 0.172, respectively; η2<0.1). Muscle protein synthesis rates increased following quark ingestion at rest in both young (from 0.030 ± 0.011 to 0.051 ± 0.011 %·h-1) and older adult males (from 0.036 ± 0.011 to 0.062 ± 0.013 %·h-1), with a further increase in the exercised leg (to 0.071 ± 0.023 %·h-1 and to 0.078 ± 0.019 %·h-1, respectively; condition: P < 0.001; η2 = 0.716), with no differences between groups (condition × group: P = 0.747; η2 = 0.011). CONCLUSIONS: Quark ingestion increases muscle protein synthesis rates at rest with a further increase following exercise in both young and older adult males. The postprandial muscle protein synthetic response following quark ingestion does not differ between healthy young and older adult males when an ample amount of protein is ingested. This trial was registered at the Dutch Trial register, which is accessible via trialsearch.who.int www.trialregister.nl as NL8403.

Higher Muscle Protein Synthesis Rates Following Ingestion of an Omnivorous Meal Compared with an Isocaloric and Isonitrogenous Vegan Meal in Healthy, Older Adults.

BACKGROUND: Plant-derived proteins are considered to have fewer anabolic properties when compared with animal-derived proteins. The anabolic properties of isolated proteins do not necessarily reflect the anabolic response to the ingestion of whole foods. The presence or absence of the various components that constitute the whole-food matrix can strongly impact protein digestion and amino acid absorption and, as such, modulate postprandial muscle protein synthesis rates. So far, no study has compared the anabolic response following ingestion of an omnivorous compared with a vegan meal. OBJECTIVES: This study aimed to compare postprandial muscle protein synthesis rates following ingestion of a whole-food omnivorous meal providing 100 g lean ground beef with an isonitrogenous, isocaloric whole-food vegan meal in healthy, older adults. METHODS: In a randomized, counter-balanced, cross-over design, 16 older (65-85 y) adults (8 males, 8 females) underwent 2 test days. On one day, participants consumed a whole-food omnivorous meal containing beef as the primary source of protein (0.45 g protein/kg body mass; MEAT). On the other day, participants consumed an isonitrogenous and isocaloric whole-food vegan meal (PLANT). Primed continuous L-[ring-13C6]-phenylalanine infusions were applied with blood and muscle biopsies being collected frequently for 6 h to assess postprandial plasma amino acid profiles and muscle protein synthesis rates. Data are presented as means ± standard deviations and were analyzed by 2 way-repeated measures analysis of variance and paired-samples t tests. RESULTS: MEAT increased plasma essential amino acid concentrations more than PLANT over the 6-h postprandial period (incremental area under curve 87 ± 37 compared with 38 ± 54 mmol·6 h/L, respectively; P-interaction < 0.01). Ingestion of MEAT resulted in ∼47% higher postprandial muscle protein synthesis rates when compared with the ingestion of PLANT (0.052 ± 0.023 and 0.035 ± 0.021 %/h, respectively; paired-samples t test: P = 0.037). CONCLUSIONS: Ingestion of a whole-food omnivorous meal containing beef results in greater postprandial muscle protein synthesis rates when compared with the ingestion of an isonitrogenous whole-food vegan meal in healthy, older adults. This study was registered at clinicaltrials.gov as NCT05151887.

Raw Eggs To Support Postexercise 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).

The effect of minimally invasive surgical aortic valve replacement on postoperative pulmonary and skeletal muscle function.

NEW FINDINGS: What is the central question of this study? How does surgical aortic valve replacement affect cardiopulmonary and muscle function during exercise? What is the main finding and its importance? Early after the surgical replacement of the aortic valve a significant decline in pulmonary function was observed, which was followed by a decline in skeletal muscle function in the subsequent weeks of recovery. These date reiterate, despite restoration of aortic valve function, the need for a tailored rehabilitation programme for the respiratory and peripheral muscular system. ABSTRACT: Suboptimal post-operative improvements in functional capacity are often observed after minimally invasive aortic valve replacement (mini-AVR). It remains to be studied how AVR affects the cardiopulmonary and skeletal muscle function during exercise to explain these clinical observations and to provide a basis for improved/tailored post-operative rehabilitation. Twenty-two patients with severe aortic stenosis (AS) (aortic valve area (AVA) <1.0 cm²) were pre-operatively compared to 22 healthy controls during submaximal constant-workload endurance-type exercise for oxygen uptake ( V̇O2 ), carbon dioxide output ( V̇CO2 ), respiratory gas exchange ratio, expiratory volume ( V̇E ), ventilatory equivalents for O2 ( V̇E / V̇O2 ) and CO2 ( V̇E / V̇CO2 ), respiratory rate (RR), tidal volume (Vt ), heart rate (HR), oxygen pulse ( V̇O2 /HR), blood lactate, Borg ratings of perceived exertion (RPE) and exercise-onset V̇O2 kinetics. These exercise tests were repeated at 5 and 21 days after AVR surgery (n = 14), along with echocardiographic examinations. Respiratory exchange ratio and ventilatory equivalents ( V̇E / V̇O2 and V̇E / V̇CO2 ) were significantly elevated, V̇O2 and V̇O2 /HR were significantly lowered, and exercise-onset V̇O2 kinetics were significantly slower in AS patients vs. healthy controls (P < 0.05). Although the AVA was restored by mini-AVR in AS patients, V̇E / V̇O2 and V̇E / V̇CO2 further worsened significantly within 5 days after surgery, accompanied by elevations in Borg RPE, V̇E and RR, and lowered Vt . At 21 days after mini-AVR, exercise-onset V̇O2 kinetics further slowed significantly (P < 0.05). A decline in pulmonary function was observed early after mini-AVR surgery, which was followed by a decline in skeletal muscle function in the subsequent weeks of recovery. Therefore, a tailored rehabilitation programme should include training modalities for the respiratory and peripheral muscular system.

Protein Ingestion before Sleep Increases Overnight Muscle Protein Synthesis Rates in Healthy Older Men: A Randomized Controlled Trial.

Background: The loss of skeletal muscle mass with aging has been attributed to the blunted anabolic response to protein intake. Presleep protein ingestion has been suggested as an effective strategy to compensate for such anabolic resistance.Objective: We assessed the efficacy of presleep protein ingestion on dietary protein digestion and absorption kinetics and overnight muscle protein synthesis rates in older men.Methods: In a randomized, double-blind, parallel design, 48 older men (mean ± SEM age: 72 ± 1 y) ingested 40 g casein (PRO40), 20 g casein (PRO20), 20 g casein plus 1.5 g leucine (PRO20+LEU), or a placebo before sleep. Ingestion of intrinsically l-[1-13C]-phenylalanine- and l-[1-13C]-leucine-labeled protein was combined with intravenous l-[ring-2H5]-phenylalanine and l-[1-13C]-leucine infusions during sleep. Muscle and blood samples were collected throughout overnight sleep.Results: Exogenous phenylalanine appearance rates increased after protein ingestion, but to a greater extent in PRO40 than in PRO20 and PRO20+LEU (P < 0.05). Overnight myofibrillar protein synthesis rates (based on l-[ring-2H5]-phenylalanine) were 0.033% ± 0.002%/h, 0.037% ± 0.003%/h, 0.039% ± 0.002%/h, and 0.044% ± 0.003%/h in placebo, PRO20, PRO20+LEU, and PRO40, respectively, and were higher in PRO40 than in placebo (P = 0.02). Observations were similar based on l-[1-13C]-leucine tracer (placebo: 0.047% ± 0.004%/h and PRO40: 0.058% ± 0.003%/h, P = 0.08). More protein-derived amino acids (l-[1-13C]-phenylalanine) were incorporated into myofibrillar protein in PRO40 than in PRO20 (0.033 ± 0.002 and 0.019 ± 0.002 MPE, respectively, P < 0.001) and tended to be higher than in PRO20+LEU (0.025 ± 0.002 MPE, P = 0.06).Conclusions: Protein ingested before sleep is properly digested and absorbed throughout the night, providing precursors for myofibrillar protein synthesis during sleep in healthy older men. Ingestion of 40 g protein before sleep increases myofibrillar protein synthesis rates during overnight sleep. These findings provide the scientific basis for a novel nutritional strategy to support muscle mass preservation in aging and disease. This trial was registered at www.trialregister.nl as NTR3885.

Nitrate-Rich Vegetables Increase Plasma Nitrate and Nitrite Concentrations and Lower Blood Pressure in Healthy Adults.

BACKGROUND: Dietary nitrate is receiving increased attention due to its reported ergogenic and cardioprotective properties. The extent to which ingestion of various nitrate-rich vegetables increases postprandial plasma nitrate and nitrite concentrations and lowers blood pressure is currently unknown. OBJECTIVE: We aimed to assess the impact of ingesting different nitrate-rich vegetables on subsequent plasma nitrate and nitrite concentrations and resting blood pressure in healthy normotensive individuals. METHODS: With the use of a semirandomized crossover design, 11 men and 7 women [mean ± SEM age: 28 ± 1 y; mean ± SEM body mass index (BMI, in kg/m(2)): 23 ± 1; exercise: 1-10 h/wk] ingested 4 different beverages, each containing 800 mg (∼12.9 mmol) nitrate: sodium nitrate (NaNO3), concentrated beetroot juice, a rocket salad beverage, and a spinach beverage. Plasma nitrate and nitrite concentrations and blood pressure were determined before and up to 300 min after beverage ingestion. Data were analyzed using repeated-measures ANOVA. RESULTS: Plasma nitrate and nitrite concentrations increased after ingestion of all 4 beverages (P < 0.001). Peak plasma nitrate concentrations were similar for all treatments (all values presented as means ± SEMs: NaNO3: 583 ± 29 µmol/L; beetroot juice: 597 ± 23 µmol/L; rocket salad beverage: 584 ± 24 µmol/L; spinach beverage: 584 ± 23 µmol/L). Peak plasma nitrite concentrations were different between treatments (NaNO3: 580 ± 58 nmol/L; beetroot juice: 557 ± 57 nmol/L; rocket salad beverage: 643 ± 63 nmol/L; spinach beverage: 980 ± 160 nmol/L; P = 0.016). When compared with baseline, systolic blood pressure declined 150 min after ingestion of beetroot juice (from 118 ± 2 to 113 ± 2 mm Hg; P < 0.001) and rocket salad beverage (from 122 ± 3 to 116 ± 2 mm Hg; P = 0.007) and 300 min after ingestion of spinach beverage (from 118 ± 2 to 111 ± 3 mm Hg; P < 0.001), but did not change with NaNO3 Diastolic blood pressure declined 150 min after ingestion of all beverages (P < 0.05) and remained lower at 300 min after ingestion of rocket salad (P = 0.045) and spinach (P = 0.001) beverages. CONCLUSIONS: Ingestion of nitrate-rich beetroot juice, rocket salad beverage, and spinach beverage effectively increases plasma nitrate and nitrite concentrations and lowers blood pressure to a greater extent than sodium nitrate. These findings show that nitrate-rich vegetables can be used as dietary nitrate supplements. This trial was registered at clinicaltrials.gov as NCT02271633.

Ingestion of Wheat Protein Increases In Vivo Muscle Protein Synthesis Rates in Healthy Older Men in a Randomized Trial.

BACKGROUND: Muscle mass maintenance is largely regulated by basal muscle protein synthesis and the capacity to stimulate muscle protein synthesis after food intake. The postprandial muscle protein synthetic response is modulated by the amount, source, and type of protein consumed. It has been suggested that plant-based proteins are less potent in stimulating postprandial muscle protein synthesis than animal-derived proteins. However, few data support this contention. OBJECTIVE: We aimed to assess postprandial plasma amino acid concentrations and muscle protein synthesis rates after the ingestion of a substantial 35-g bolus of wheat protein hydrolysate compared with casein and whey protein. METHODS: Sixty healthy older men [mean ± SEM age: 71 ± 1 y; body mass index (in kg/m(2)): 25.3 ± 0.3] received a primed continuous infusion of l-[ring-(13)C6]-phenylalanine and ingested 35 g wheat protein (n = 12), 35 g wheat protein hydrolysate (WPH-35; n = 12), 35 g micellar casein (MCas-35; n = 12), 35 g whey protein (Whey-35; n = 12), or 60 g wheat protein hydrolysate (WPH-60; n = 12). Plasma and muscle samples were collected at regular intervals. RESULTS: The postprandial increase in plasma essential amino acid concentrations was greater after ingesting Whey-35 (2.23 ± 0.07 mM) than after MCas-35 (1.53 ± 0.08 mM) and WPH-35 (1.50 ± 0.04 mM) (P < 0.01). Myofibrillar protein synthesis rates increased after ingesting MCas-35 (P < 0.01) and were higher after ingesting MCas-35 (0.050% ± 0.005%/h) than after WPH-35 (0.032% ± 0.004%/h) (P = 0.03). The postprandial increase in plasma leucine concentrations was greater after ingesting Whey-35 than after WPH-60 (peak value: 580 ± 18 compared with 378 ± 10 µM, respectively; P < 0.01), despite similar leucine contents (4.4 g leucine). Nevertheless, the ingestion of WPH-60 increased myofibrillar protein synthesis rates above basal rates (0.049% ± 0.007%/h; P = 0.02). CONCLUSIONS: The myofibrillar protein synthetic response to the ingestion of 35 g casein is greater than after an equal amount of wheat protein. Ingesting a larger amount of wheat protein (i.e., 60 g) substantially increases myofibrillar protein synthesis rates in healthy older men. This trial was registered at clinicaltrials.gov as NCT01952639.

Physical Activity Performed in the Evening Increases the Overnight Muscle Protein Synthetic Response to Presleep Protein Ingestion in Older Men.

BACKGROUND: The age-related decline in skeletal muscle mass is partly attributed to anabolic resistance to food intake. Dietary protein ingestion before sleep could be used as a nutritional strategy to compensate for anabolic resistance. OBJECTIVE: The present study assessed whether physical activity performed in the evening can augment the overnight muscle protein synthetic response to presleep protein ingestion in older men. METHODS: In a parallel group design, 23 healthy older men (mean ± SEM age: 71 ± 1 y) were randomly assigned to ingest 40 g protein intrinsically labeled with l-[1-(13)C]-phenylalanine and l-[1-(13)C]-leucine before going to sleep with (PRO+EX) or without (PRO) performing physical activity earlier in the evening. Overnight protein digestion and absorption kinetics and myofibrillar protein synthesis rates were assessed by combining primed, continuous infusions of l-[ring-(2)H5]-phenylalanine, l-[1-(13)C]-leucine, and l-[ring-(2)H2]-tyrosine with the ingestion of intrinsically labeled casein protein. Muscle and blood samples were collected throughout overnight sleep. RESULTS: Protein ingested before sleep was normally digested and absorbed, with 54% ± 2% of the protein-derived amino acids appearing in the circulation throughout overnight sleep. Overnight myofibrillar protein synthesis rates were 31% (0.058% ± 0.002%/h compared with 0.044% ± 0.003%/h; P < 0.01; based on l-[ring-(2)H5]-phenylalanine) and 27% (0.074% ± 0.004%/h compared with 0.058% ± 0.003%/h; P < 0.01; based on l-[1-(13)C]-leucine) higher in the PRO+EX than in the PRO treatment. More dietary protein-derived amino acids were incorporated into de novo myofibrillar protein during overnight sleep in PRO+EX than in PRO treatment (0.042 ± 0.002 compared with 0.033 ± 0.002 mole percent excess; P < 0.05). CONCLUSIONS: Physical activity 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 muscle protein synthesis during overnight sleep in older men. This trial was registered at Nederlands Trial Register as NTR3885.

Habituation to low or high protein intake does not modulate basal or postprandial muscle protein synthesis rates: a randomized trial.

BACKGROUND: Muscle mass maintenance is largely regulated by basal muscle protein synthesis rates and the ability to increase muscle protein synthesis after protein ingestion. To our knowledge, no previous studies have evaluated the impact of habituation to either low protein intake (LOW PRO) or high protein intake (HIGH PRO) on the postprandial muscle protein synthetic response. OBJECTIVE: We assessed the impact of LOW PRO compared with HIGH PRO on basal and postprandial muscle protein synthesis rates after the ingestion of 25 g whey protein. DESIGN: Twenty-four healthy, older men [age: 62 ± 1 y; body mass index (in kg/m2): 25.9 ± 0.4 (mean ± SEM)] participated in a parallel-group randomized trial in which they adapted to either a LOW PRO diet (0.7 g · kg-1 · d-1; n = 12) or a HIGH PRO diet (1.5 g · kg-1 · d-1; n = 12) for 14 d. On day 15, participants received primed continuous l-[ring-2H5]-phenylalanine and l-[1-13C]-leucine infusions and ingested 25 g intrinsically l-[1-13C]-phenylalanine- and l-[1-13C]-leucine-labeled whey protein. Muscle biopsies and blood samples were collected to assess muscle protein synthesis rates as well as dietary protein digestion and absorption kinetics. RESULTS: Plasma leucine concentrations and exogenous phenylalanine appearance rates increased after protein ingestion (P < 0.01) with no differences between treatments (P > 0.05). Plasma exogenous phenylalanine availability over the 5-h postprandial period was greater after LOW PRO than after HIGH PRO (61% ± 1% compared with 56% ± 2%, respectively; P < 0.05). Muscle protein synthesis rates increased from 0.031% ± 0.004% compared with 0.039% ± 0.007%/h in the fasted state to 0.062% ± 0.005% compared with 0.057% ± 0.005%/h in the postprandial state after LOW PRO compared with HIGH PRO, respectively (P < 0.01), with no differences between treatments (P = 0.25). CONCLUSION: Habituation to LOW PRO (0.7 g · kg-1 · d-1) compared with HIGH PRO (1.5 g · kg-1 · d-1) augments the postprandial availability of dietary protein-derived amino acids in the circulation and does not lower basal muscle protein synthesis rates or increase postprandial muscle protein synthesis rates after ingestion of 25 g protein in older men. This trial was registered at clinicaltrials.gov as NCT01986842.

Jejunal feeding is followed by a greater rise in plasma cholecystokinin, peptide YY, glucagon-like peptide 1, and glucagon-like peptide 2 concentrations compared with gastric feeding in vivo in humans: a randomized trial.

BACKGROUND: Jejunal feeding is preferred instead of gastric feeding in patients who are intolerant to gastric feeding or at risk of aspiration. However, the impact of gastric feeding compared with that of jejunal feeding on postprandial circulating plasma glucose and amino acid concentrations and the associated endocrine response in vivo in humans remains largely unexplored. OBJECTIVE: We compared the impact of administering enteral nutrition as either gastric feeding or jejunal feeding on endocrine responses in vivo in humans. DESIGN: In a randomized, crossover study design, 12 healthy young men (mean ± SD age: 21 ± 2 y) received continuous enteral nutrition that contained noncoagulating proteins for 12 h via a nasogastric tube or a nasojejunal tube placed 30-40 cm distal to the ligament of Treitz. Blood samples were collected during the 12-h postprandial period to assess the rise in plasma glucose, amino acid, and gastrointestinal hormone concentrations. RESULTS: No differences were observed in the postprandial rise in circulating plasma amino acid and glucose concentrations between regimens. Jejunal feeding resulted in higher peak plasma insulin concentrations than did gastric feeding (392 ± 53 compared with 326 ± 54 pmol/L, respectively; P < 0.05). The postprandial rise in plasma cholecystokinin, peptide YY (PYY), glucagon-like peptide 1 (GLP-1), and glucagon-like peptide 2 (GLP-2) concentrations was greater after jejunal feeding than after gastric feeding, with higher peak concentrations and a greater postprandial incremental AUC for GLP-1 and cholecystokinin (all P < 0.05). Plasma ghrelin concentrations did not differ between regimens. CONCLUSIONS: Enteral nutrition with gastric or jejunal feeding in healthy young men results in similar postprandial plasma amino acid and glucose concentrations. However, the endocrine response differs substantially, with higher peak plasma cholecystokinin, PYY, GLP-1, and GLP-2 concentrations being attained after jejunal feeding. This effect may result in an improved anabolic response, greater insulin sensitivity, and an improved intestinotropic effect. Nevertheless, it may also lead to delayed gastric emptying. This trial was registered at trialregister.nl as NTR2801.

Differences in postprandial protein handling after beef compared with milk ingestion during postexercise recovery: a randomized controlled trial.

BACKGROUND: Protein consumed after resistance exercise increases postexercise muscle protein synthesis rates. To date, dairy protein has been studied extensively, with little known about the capacity of other protein-dense foods to augment postexercise muscle protein synthesis rates. OBJECTIVE: We aimed to compare protein digestion and absorption kinetics, postprandial amino acid availability, anabolic signaling, and the subsequent myofibrillar protein synthetic response after the ingestion of milk compared with beef during recovery from resistance-type exercise. DESIGN: In crossover trials, 12 healthy young men performed a single bout of resistance exercise. Immediately after cessation of exercise, participants ingested 30 g protein by consuming isonitrogenous amounts of intrinsically l-[1-(13)C]phenylalanine-labeled beef or milk. Blood and muscle biopsy samples were collected at rest and after exercise during primed continuous infusions of l-[ring-(2)H5]phenylalanine and l-[ring-3,5-(2)H2]tyrosine to assess protein digestion and absorption kinetics, plasma amino acid availability, anabolic signaling, and subsequent myofibrillar protein synthesis rates in vivo in young men. RESULTS: Beef protein-derived phenylalanine appeared more rapidly in circulation compared with milk ingestion (P < 0.001). The availability of phenylalanine during the 5-h postexercise period tended to be higher after beef (64% ± 3%) ingestion than after milk ingestion (57% ± 3%; P = 0.08). Both beef and milk ingestion were followed by an increase in the phosphorylation of mammalian target of rapamycin complex 1 and 70-kDa S6 protein kinase 1 during postexercise recovery. Milk ingestion increased myofibrillar protein synthesis rates to a greater extent than did beef ingestion during the 0- to 2-h postexercise phase (P = 0.013). However, the increase in myofibrillar protein synthesis rates did not differ between milk and beef ingestion during the entire 0- to 5-h postexercise phase (P = 0.114). CONCLUSIONS: Both milk and beef ingestion augment the postexercise myofibrillar protein synthetic response in young men, with a stronger stimulation of myofibrillar protein synthesis during the early postprandial stage after milk ingestion. This trial was registered at www.clinicaltrials.gov as NCT01578590.

Protein and healthy aging.

Our understanding of the potential benefits and challenges of optimizing dietary protein intake in older adults continues to evolve. An overarching hypothesis generated during Protein Summit 2.0 was that consuming an adequate amount of high-quality protein at each meal, in combination with physical activity, may delay the onset of sarcopenia, slow its progression, reduce the magnitude of its functional consequences, or all of these. The potential benefits of young and middle-aged adults adopting a diet pattern whereby adequate protein is consumed at each meal as a countermeasure to sarcopenia are presented and discussed. For example, meeting a protein threshold (∼25-30 g/meal) represents a promising, yet still largely unexplored dietary strategy to help maintain muscle mass and function. For many older adults, breakfast is a carbohydrate-dominated lower-protein meal and represents an opportunity to improve and more evenly distribute daily protein intake. Although both animal and plant-based proteins can provide the required essential amino acids for health, animal proteins generally have a higher proportion of the amino acid leucine. Leucine plays a key role in stimulating translation initiation and muscle protein anabolism and is the focus of ongoing research. Protein requirements should be assessed in the light of habitual physical activity. An evenly distributed protein diet provides a framework that allows older adults to benefit from the synergistic anabolic effect of protein and physical activity. To fully understand the role of dietary protein intake in healthy aging, greater efforts are needed to coordinate and integrate research design and data acquisition and interpretation from a variety of disciplines.

Carbohydrate co-ingestion with protein does not further augment post-prandial muscle protein accretion in older men.

BACKGROUND: A blunted muscle protein synthetic response to protein ingestion may contribute to the age related loss of muscle tissue. We hypothesized that the greater endogenous insulin release following co-ingestion of carbohydrate facilitates post-prandial muscle protein accretion after ingesting a meal-like bolus of protein in older males. METHODS: Twenty-four healthy older men (75±1 y) were randomly assigned to ingest 20 g intrinsically L-[1-13C] phenylalanine-labeled casein protein with (PRO-CHO) or without (PRO) 40 g carbohydrate. Ingestion of specifically produced intrinsically L-[1-13C] phenylalanine labeled protein allowed us to assess post-prandial incorporation of dietary protein derived amino acids into muscle protein. Blood samples were collected at regular intervals, with muscle biopsies being obtained prior to and 2 and 6 h after protein ingestion. RESULTS: Plasma glucose and insulin concentrations showed a greater increase in PRO-CHO compared with PRO (P<0.001). Muscle protein-bound L-[1-13C] phenylalanine enrichments tended to increase to a greater extent in PRO-CHO compared with PRO during the first 2 h after protein ingestion (0.0072±0.0013 vs 0.0046±0.010 MPE, respectively; P=0.13). However, 6 h after protein ingestion, differences in muscle protein-bound L-[1-13C] phenylalanine enrichments were no longer observed between experiments (0.0213±0.0024 vs 0.0185±0.0010 MPE, respectively; P=0.30). CONCLUSIONS: This study shows that carbohydrate ingestion may accelerate, but does not further augment post-prandial incorporation of dietary protein derived amino acids into muscle protein in healthy elderly men.