scholarly journals Carbohydrate Coingestion Delays Dietary Protein Digestion and Absorption but Does Not Modulate Postprandial Muscle Protein Accretion

2014 ◽  
Vol 99 (6) ◽  
pp. 2250-2258 ◽  
Author(s):  
Stefan H. M. Gorissen ◽  
Nicholas A. Burd ◽  
Henrike M. Hamer ◽  
Annemie P. Gijsen ◽  
Bart B. Groen ◽  
...  
2020 ◽  
Vol 150 (8) ◽  
pp. 2041-2050 ◽  
Author(s):  
Stefan H M Gorissen ◽  
Jorn Trommelen ◽  
Imre W K Kouw ◽  
Andrew M Holwerda ◽  
Bart Pennings ◽  
...  

ABSTRACT Background Dietary protein ingestion stimulates muscle protein synthesis by providing amino acids to the muscle. The magnitude and duration of the postprandial increase in muscle protein synthesis rates are largely determined by dietary protein digestion and amino acid absorption kinetics. Objective We assessed the impact of protein type, protein dose, and age on dietary protein digestion and amino acid absorption kinetics in vivo in humans. Methods We included data from 18 randomized controlled trials with a total of 602 participants [age: 53 ± 23 y; BMI (kg/m2): 24.8 ± 3.3] who consumed various quantities of intrinsically l-[1-13C]-phenylalanine–labeled whey (n = 137), casein (n = 393), or milk (n = 72) protein and received intravenous infusions of l-[ring-2H5]-phenylalanine, which allowed us to assess protein digestion and phenylalanine absorption kinetics and the postprandial release of dietary protein–derived phenylalanine into the circulation. The effect of aging on these processes was assessed in a subset of 82 young (aged 22 ± 3 y) and 83 older (aged 71 ± 5 y) individuals. Results A total of 50% ± 14% of dietary protein–derived phenylalanine appeared in the circulation over a 5-h postprandial period. Casein ingestion resulted in a smaller (45% ± 11%), whey protein ingestion in an intermediate (57% ± 10%), and milk protein ingestion in a greater (65% ± 13%) fraction of dietary protein–derived phenylalanine appearing in the circulation (P < 0.001). The postprandial availability of dietary protein–derived phenylalanine in the circulation increased with the ingestion of greater protein doses (P < 0.05). Protein digestion and phenylalanine absorption kinetics were attenuated in older when compared with young individuals, with 45% ± 10% vs. 51% ± 14% of dietary protein–derived phenylalanine appearing in the circulation, respectively (P = 0.001). Conclusions Protein type, protein dose, and age modulate dietary protein digestion and amino acid absorption kinetics and subsequent postprandial plasma amino acid availability in vivo in humans. These trials were registered at clinicaltrials.gov as NCT00557388, NCT00936039, NCT00991523, NCT01317511, NCT01473576, NCT01576848, NCT01578590, NCT01615276, NCT01680146, NCT01820975, NCT01986842, and NCT02596542, and at http://www.trialregister.nl as NTR3638, NTR3885, NTR4060, NTR4429, and NTR4492.


2015 ◽  
Vol 145 (7) ◽  
pp. 1438-1445 ◽  
Author(s):  
Tyler A Churchward-Venne ◽  
Tim Snijders ◽  
Armand MA Linkens ◽  
Henrike M Hamer ◽  
Janneau van Kranenburg ◽  
...  

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Stefan H Gorissen ◽  
Nicholas A Burd ◽  
Henrike M Hamer ◽  
Annemie P Gijsen ◽  
Luc JC Loon

2009 ◽  
Vol 139 (9) ◽  
pp. 1707-1713 ◽  
Author(s):  
René Koopman ◽  
Stéphane Walrand ◽  
Milou Beelen ◽  
Annemie P. Gijsen ◽  
Arie K. Kies ◽  
...  

2012 ◽  
Vol 302 (1) ◽  
pp. E52-E60 ◽  
Author(s):  
Bart B. L. Groen ◽  
Peter T. Res ◽  
Bart Pennings ◽  
Elisabeth Hertle ◽  
Joan M. G. Senden ◽  
...  

The loss of skeletal muscle mass with aging has been attributed to an impaired muscle protein synthetic response to food intake. Therefore, nutritional strategies are targeted to modulate postprandial muscle protein accretion in the elderly. The purpose of this study was to assess the impact of protein administration during sleep on in vivo protein digestion and absorption kinetics and subsequent muscle protein synthesis rates in elderly men. Sixteen healthy elderly men were randomly assigned to an experiment during which they were administered a single bolus of intrinsically l-[1-13C]phenylalanine-labeled casein protein (PRO) or a placebo (PLA) during sleep. Continuous infusions with l-[ ring-2H5]phenylalanine and l-[ ring-2H2]tyrosine were applied to assess in vivo dietary protein digestion and absorption kinetics and subsequent muscle protein synthesis rates during sleep. We found that exogenous phenylalanine appearance rates increased following protein administration. The latter stimulated protein synthesis, resulting in a more positive overnight whole body protein balance (0.30 ± 0.1 vs. 11.8 ± 1.0 μmol phenylalanine·kg−1·h−1 in PLA and PRO, respectively; P < 0.05). In agreement, overnight muscle protein fractional synthesis rates were much greater in the PRO experiment (0.045 ± 0.002 vs. 0.029 ± 0.002%/h, respectively; P < 0.05) and showed abundant incorporation of the amino acids ingested via the intrinsically labeled protein (0.058 ± 0.006%/h). This is the first study to show that dietary protein administration during sleep is followed by normal digestion and absorption kinetics, thereby stimulating overnight muscle protein synthesis. Dietary protein administration during sleep stimulates muscle protein synthesis and improves overnight whole body protein balance. These findings may provide a basis for novel interventional strategies to attenuate muscle mass loss.


2017 ◽  
Vol 42 (7) ◽  
pp. 738-743 ◽  
Author(s):  
Andrew M. Holwerda ◽  
Kaatje Lenaerts ◽  
Jörgen Bierau ◽  
Will K.W.H. Wodzig ◽  
Luc J.C. van Loon

Dietary protein digestion and absorption kinetics determine the postprandial increase in muscle protein synthesis. We recently demonstrated that body position during feeding can modulate the postprandial rise in plasma amino acid availability. Here we investigated whether protein ingestion in an upright sitting body position accelerates gastric emptying and improves dietary protein digestion and subsequent amino acid absorption compared with feeding in a supine lying body position. In a crossover design, 8 young males (age, 26 ± 1 years; body mass index, 24.0 ± 0.9 kg·m−2) ingested 20 g intrinsically l-[1-13C]-phenylalanine–labeled milk protein plus 1.5 g paracetamol while sitting in an upright position or lying down in a supine position. Blood samples were collected frequently during a 5-h postprandial period. Gastric emptying rates and dietary protein digestion and absorption were assessed using plasma paracetamol and amino acid concentrations as well as plasma l-[1-13C]-phenylalanine enrichments. Peak plasma leucine concentrations were higher when protein was ingested in an upright sitting versus lying position (213 ± 15 vs 193 ± 12 μmol·L−1, P < 0.05), which was accompanied by a trend for a greater overall leucine response (13 989 ± 720 vs 11 875 ± 1073 AU, respectively; P = 0.05). Peak plasma paracetamol concentrations were higher in the sitting versus lying treatment (11.6 ± 0.5 vs 9.3 ± 0.6 mg·L−1, P < 0.05). Protein ingestion in an upright sitting position accelerates gastric emptying and increases the postprandial rise in plasma amino acid availability by increasing protein digestion and amino acid absorption rates. Therefore, feeding in an upright body position as opposed to a lying position is an important prerequisite to allow proper postprandial muscle protein accretion.


Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.


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