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 Q.; Thorning, Tanja K.; Reitelseder, Søren; Ritz, Christian; Hansen, Erik T.; van Hall, Gerrit; Astrup, Arne; Sjödin, Anders; Holm, Lars.

In: Nutrients, Vol. 11, No. 5, 989, 30.04.2019.

Research output: Contribution to journalArticlepeer-review

Harvard

Bendtsen, LQ, Thorning, TK, Reitelseder, S, Ritz, C, Hansen, ET, van Hall, G, Astrup, A, Sjödin, A & Holm, L 2019, 'Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins-a randomized controlled trial', Nutrients, vol. 11, no. 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., & 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

Author

Bendtsen, Line Q. ; Thorning, Tanja K. ; Reitelseder, Søren ; Ritz, Christian ; Hansen, Erik T. ; van Hall, Gerrit ; Astrup, Arne ; Sjödin, Anders ; Holm, Lars. / Human muscle protein synthesis rates after intake of hydrolyzed porcine-derived and cows' milk whey proteins-a randomized controlled trial. In: Nutrients. 2019 ; Vol. 11, No. 5.

Bibtex

@article{8f912e2e4d414814ab9767aee161cd49,
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/m 2) 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- 13C 6) 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 = "FSR, amino acids, dietary proteins, muscle protein synthesis, porcine proteins",
author = "Bendtsen, {Line Q.} and Thorning, {Tanja K.} and S{\o}ren Reitelseder and Christian Ritz and Hansen, {Erik T.} and {van Hall}, Gerrit and Arne Astrup and Anders Sj{\"o}din and Lars Holm",
year = "2019",
month = apr,
day = "30",
doi = "10.3390/nu11050989",
language = "English",
volume = "11",
journal = "Nutrients",
issn = "2072-6643",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
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 Q.

AU - Thorning, Tanja K.

AU - Reitelseder, Søren

AU - Ritz, Christian

AU - Hansen, Erik T.

AU - van Hall, Gerrit

AU - Astrup, Arne

AU - Sjödin, Anders

AU - Holm, Lars

PY - 2019/4/30

Y1 - 2019/4/30

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/m 2) 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- 13C 6) 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/m 2) 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- 13C 6) 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 - FSR

KW - amino acids

KW - dietary proteins

KW - muscle protein synthesis

KW - porcine proteins

UR - http://www.scopus.com/inward/record.url?scp=85065676397&partnerID=8YFLogxK

U2 - 10.3390/nu11050989

DO - 10.3390/nu11050989

M3 - Article

C2 - 31052297

VL - 11

JO - Nutrients

JF - Nutrients

SN - 2072-6643

IS - 5

M1 - 989

ER -