Increasing Insulin Availability Does Not Augment Postprandial Muscle Protein Synthesis Rates in Healthy Young and Older Men

Groen, Bart B. L.; Horstman, Astrid M.; Hamer, Henrike M.; Haan, Michiel de; Kranenburg, Janneau van; Bierau, Jörgen; Poeze, Martijn; Wodzig, Will K. W. H.; Rasmussen, Blake B.; Loon, Luc J. C. van

doi:10.1210/jc.2016-1436

Cited by 22 publications

(18 citation statements)

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“…To define the impact of age on dietary protein digestion and phenylalanine absorption kinetics and the subsequent availability of dietary protein–derived phenylalanine in the circulation, we combined data from 4 RCTs that compared young and older individuals within the same study ( 27 , 32 , 35 , 42 ). Peak protein digestion and phenylalanine absorption rates were similar between young and older men.…”

Section: Discussionmentioning

confidence: 99%

“…Finally, for the comparison between young and older individuals, we included 4 RCTs that compared young and older individuals all within the RCT. These 4 studies were conducted in healthy young and older men ingesting 35 g ( 27 ) or 20 g ( 32 , 35 , 42 ) intrinsically labeled casein, measured for ≥5 h, and included experimental arms that also involved exercise ( 42 ), carbohydrate co-ingestion ( 32 ), or local insulin infusion ( 35 ). This approach yielded data from n = 82 young and n = 83 older individuals (see Table 4 for participants’ characteristics).…”

Section: Methodsmentioning

confidence: 99%

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Protein Type, Protein Dose, and Age Modulate Dietary Protein Digestion and Phenylalanine Absorption Kinetics and Plasma Phenylalanine Availability in Humans

Gorissen

Trommelen

Kouw

et al. 2020

The Journal of Nutrition

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Protein Type, Protein Dose, and Age Modulate Dietary Protein Digestion and Phenylalanine Absorption Kinetics and Plasma Phenylalanine Availability in Humans

Gorissen

Trommelen

Kouw

et al. 2020

The Journal of Nutrition

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“…The post-prandial reduction in whole-body protein breakdown rates is attenuated in older adults when compared to younger adults (32) . In line, older adults display less of a post-prandial increase in whole-body net balance when compared to younger adults (37) . Finally, obese individuals seem to display less of a post-prandial increase in whole-body net protein balance when compared to lean individuals following ingestion of 25 g protein.…”

Section: Post-prandial Whole-body Protein Metabolismmentioning

confidence: 92%

“…Carbohydrate co-ingestion has been shown to further reduce whole-body protein breakdown and amino acid oxidation (32) . This may in part be attributed to its insulinotropic properties (37) .…”

Section: Post-prandial Whole-body Protein Metabolismmentioning

confidence: 99%

Comprehensive assessment of post-prandial protein handling by the application of intrinsically labelled protein in vivo in human subjects

et al. 2021

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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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“…[7] In this paper, we present an ew method based on stable isotope-labeling,w hich enables detection of localized amino acid metabolism over time for the first time.Stable isotopes of l-phenylalanine (Phe) are commonly used in clinical studies to measure protein turnover. [8] In liver,P he is enzymatically hydroxylated into l-tyrosine (Tyr), and altered levels are related to nonalcoholic steatohepatitis,n onalcoholic fatty liver disease,c irrhosis,a nd several cancer phenotypes. [9] A bolus of ring-13 C 6 -labeled l-phenylalanine ( 13 C 6 -Phe) was injected into 11 mice and healthy liver tissue was collected at three time points (10, 30, and 60 min) after injection to track the incorporation of 13 C 6 -Phe into tissue using MALDI.…”

mentioning

confidence: 99%

Detection of Localized Hepatocellular Amino Acid Kinetics by using Mass Spectrometry Imaging of Stable Isotopes

et al. 2017

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Mass spectrometry imaging (MSI) simultaneously detects and identifies the spatial distribution of numerous molecules throughout tissues. Currently, MSI is limited to providing a static and ex vivo snapshot of highly dynamic systems in which molecules are constantly synthesized and consumed. Herein, we demonstrate an innovative MSI methodology to study dynamic molecular changes of amino acids within biological tissues by measuring the dilution and conversion of stable isotopes in a mouse model. We evaluate the method specifically on hepatocellular metabolism of the essential amino acid l‐phenylalanine, associated with liver diseases. Crucially, the method reveals the localized dynamics of l‐phenylalanine metabolism, including its in vivo hydroxylation to l‐tyrosine and co‐localization with other liver metabolites in a time course of samples from different animals. This method thus enables the dynamics of localized biochemical synthesis to be studied directly from biological tissues.

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Increasing Insulin Availability Does Not Augment Postprandial Muscle Protein Synthesis Rates in Healthy Young and Older Men

Cited by 22 publications

References 50 publications

Protein Type, Protein Dose, and Age Modulate Dietary Protein Digestion and Phenylalanine Absorption Kinetics and Plasma Phenylalanine Availability in Humans

Protein Type, Protein Dose, and Age Modulate Dietary Protein Digestion and Phenylalanine Absorption Kinetics and Plasma Phenylalanine Availability in Humans

Comprehensive assessment of post-prandial protein handling by the application of intrinsically labelled protein in vivo in human subjects

Detection of Localized Hepatocellular Amino Acid Kinetics by using Mass Spectrometry Imaging of Stable Isotopes

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