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., Astrup, A., Sjödin, A. M., & 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