Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial

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Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial. / Bendtsen, Line Quist; Thorning, Tanja Kongerslev; Reitelseder, Søren; Ritz, Christian; Hansen, Erik T; van Hall, Gerrit; Astrup, Arne; Sjödin, Anders Mikael; Holm, Lars.

I: Nutrients, Bind 11, Nr. 5, 989, 2019.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Bendtsen, LQ, Thorning, TK, Reitelseder, S, Ritz, C, Hansen, ET, van Hall, G, Astrup, A, Sjödin, AM & Holm, L 2019, 'Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial', Nutrients, bind 11, nr. 5, 989. https://doi.org/10.3390/nu11050989

APA

Bendtsen, L. Q., Thorning, T. K., Reitelseder, S., Ritz, C., Hansen, E. T., van Hall, G., ... Holm, L. (2019). Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial. Nutrients, 11(5), [989]. https://doi.org/10.3390/nu11050989

Vancouver

Bendtsen LQ, Thorning TK, Reitelseder S, Ritz C, Hansen ET, van Hall G o.a. Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial. Nutrients. 2019;11(5). 989. https://doi.org/10.3390/nu11050989

Author

Bendtsen, Line Quist ; Thorning, Tanja Kongerslev ; Reitelseder, Søren ; Ritz, Christian ; Hansen, Erik T ; van Hall, Gerrit ; Astrup, Arne ; Sjödin, Anders Mikael ; Holm, Lars. / Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial. I: Nutrients. 2019 ; Bind 11, Nr. 5.

Bibtex

@article{13105ee49a6949f8a37ad9b6ab1366c0,
title = "Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial",
abstract = "Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects.Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein.Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m2) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-13C6) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion.Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008{\%}/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 {\%}/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013{\%}/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05).Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.",
keywords = "Faculty of Science, Dietary proteins, Porcine proteins, Muscle protein synthesis, Amino acids, FSR",
author = "Bendtsen, {Line Quist} and Thorning, {Tanja Kongerslev} and S{\o}ren Reitelseder and Christian Ritz and Hansen, {Erik T} and {van Hall}, Gerrit and Arne Astrup and Sj{\"o}din, {Anders Mikael} and Lars Holm",
note = "CURIS 2019 NEXS 153",
year = "2019",
doi = "10.3390/nu11050989",
language = "English",
volume = "11",
journal = "Nutrients",
issn = "2072-6643",
publisher = "M D P I AG",
number = "5",

}

RIS

TY - JOUR

T1 - Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins - a randomized controlled trial

AU - Bendtsen, Line Quist

AU - Thorning, Tanja Kongerslev

AU - Reitelseder, Søren

AU - Ritz, Christian

AU - Hansen, Erik T

AU - van Hall, Gerrit

AU - Astrup, Arne

AU - Sjödin, Anders Mikael

AU - Holm, Lars

N1 - CURIS 2019 NEXS 153

PY - 2019

Y1 - 2019

N2 - Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects.Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein.Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m2) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-13C6) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion.Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008%/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 %/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013%/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05).Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.

AB - Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects.Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein.Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m2) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-13C6) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion.Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008%/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 %/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013%/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05).Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.

KW - Faculty of Science

KW - Dietary proteins

KW - Porcine proteins

KW - Muscle protein synthesis

KW - Amino acids

KW - FSR

U2 - 10.3390/nu11050989

DO - 10.3390/nu11050989

M3 - Journal article

C2 - 31052297

VL - 11

JO - Nutrients

JF - Nutrients

SN - 2072-6643

IS - 5

M1 - 989

ER -

ID: 217550325