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      Cheese Ingestion Increases Muscle Protein Synthesis Rates Both at Rest and During Recovery from Exercise in Healthy, Young Males: A Randomized Parallel-Group Trial

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          ABSTRACT

          Background

          Protein ingestion increases muscle protein synthesis rates. The food matrix in which protein is provided can strongly modulate the postprandial muscle protein synthetic response. So far, the muscle protein synthetic response to the ingestion of whole foods remains largely unexplored.

          Objectives

          To compare the impact of ingesting 30 g protein provided as milk protein or cheese on postprandial plasma amino acid concentrations and muscle protein synthesis rates at rest and during recovery from exercise in vivo in young males.

          Methods

          In this randomized, parallel-group intervention trial, 20 healthy males aged 18–35 y ingested 30 g protein provided as cheese or milk protein concentrate following a single-legged resistance-type exercise session consisting of 12 sets of leg press and leg extension exercises. Primed, continuous intravenous L-[ ring- 13C 6]-phenylalanine infusions were combined with the collection of blood and muscle tissue samples to assess postabsorptive and 4-h postprandial muscle protein synthesis rates at rest and during recovery from exercise. Data were analyzed using repeated measures Time × Group (× Leg) ANOVA.

          Results

          Plasma total amino acid concentrations increased after protein ingestion (Time: P < 0.001), with 38% higher peak concentrations following milk protein than cheese ingestion (Time × Group: P < 0.001). Muscle protein synthesis rates increased following both cheese and milk protein ingestion from 0.037 ± 0.014 to 0.055 ± 0.018%·h –1 and 0.034 ± 0.008 to 0.056 ± 0.010%·h –1 at rest and even more following exercise from 0.031 ± 0.010 to 0.067 ± 0.013%·h –1 and 0.030 ± 0.008 to 0.063 ± 0.010%·h –1, respectively (Time: all P < 0.05; Time × Leg: P = 0.002), with no differences between cheese and milk protein ingestion (Time × Group: both P > 0.05).

          Conclusion

          Cheese ingestion increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial muscle protein synthetic response to the ingestion of cheese or milk protein does not differ when 30 g protein is ingested at rest or during recovery from exercise in healthy, young males.

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          Most cited references43

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          Percutaneous needle biopsy of skeletal muscle in physiological and clinical research.

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            The digestion rate of protein is an independent regulating factor of postprandial protein retention.

            To evaluate the importance of protein digestion rate on protein deposition, we characterized leucine kinetics after ingestion of "protein" meals of identical amino acid composition and nitrogen contents but of different digestion rates. Four groups of five or six young men received an L-[1-13C]leucine infusion and one of the following 30-g protein meals: a single meal of slowly digested casein (CAS), a single meal of free amino acid mimicking casein composition (AA), a single meal of rapidly digested whey proteins (WP), or repeated meals of whey proteins (RPT-WP) mimicking slow digestion rate. Comparisons were made between "fast" (AA, WP) and "slow" (CAS, RPT-WP) meals of identical amino acid composition (AA vs. CAS, and WP vs. RPT-WP). The fast meals induced a strong, rapid, and transient increase of aminoacidemia, leucine flux, and oxidation. After slow meals, these parameters increased moderately but durably. Postprandial leucine balance over 7 h was higher after the slow than after the fast meals (CAS: 38 +/- 13 vs. AA: -12 +/- 11, P < 0.01; RPT-WP: 87 +/- 25 vs. WP: 6 +/- 19 micromol/kg, P < 0.05). Protein digestion rate is an independent factor modulating postprandial protein deposition.
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              Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men.

              This study was designed to compare the acute response of mixed muscle protein synthesis (MPS) to rapidly (i.e., whey hydrolysate and soy) and slowly (i.e., micellar casein) digested proteins both at rest and after resistance exercise. Three groups of healthy young men (n = 6 per group) performed a bout of unilateral leg resistance exercise followed by the consumption of a drink containing an equivalent content of essential amino acids (10 g) as either whey hydrolysate, micellar casein, or soy protein isolate. Mixed MPS was determined by a primed constant infusion of l-[ring-(13)C(6)]phenylalanine. Ingestion of whey protein resulted in a larger increase in blood essential amino acid, branched-chain amino acid, and leucine concentrations than either casein or soy (P soy > casein); MPS following whey consumption was approximately 122% greater than casein (P < 0.01) and 31% greater than soy (P < 0.05). MPS was also greater with soy consumption at rest (64%) and following resistance exercise (69%) compared with casein (both P < 0.01). We conclude that the feeding-induced simulation of MPS in young men is greater after whey hydrolysate or soy protein consumption than casein both at rest and after resistance exercise; moreover, despite both being fast proteins, whey hydrolysate stimulated MPS to a greater degree than soy after resistance exercise. These differences may be related to how quickly the proteins are digested (i.e., fast vs. slow) or possibly to small differences in leucine content of each protein.
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                Author and article information

                Contributors
                Journal
                J Nutr
                J Nutr
                jn
                The Journal of Nutrition
                Oxford University Press
                0022-3166
                1541-6100
                April 2022
                10 January 2022
                10 January 2022
                : 152
                : 4
                : 1022-1030
                Affiliations
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University , Maastricht, The Netherlands
                Author notes
                Address correspondence to LJCvL (E-mail: l.vanloon@ 123456maastrichtuniversity.nl ).
                Author information
                https://orcid.org/0000-0003-1822-6828
                https://orcid.org/0000-0002-3401-465X
                https://orcid.org/0000-0001-5692-8711
                https://orcid.org/0000-0001-8543-282X
                https://orcid.org/0000-0001-5078-506X
                https://orcid.org/0000-0002-9196-8767
                https://orcid.org/0000-0002-6768-9231
                Article
                nxac007
                10.1093/jn/nxac007
                8971000
                35020907
                611c80c5-4636-4482-832f-6b36b4efd422
                © The Author(s) 2022. Published by Oxford University Press on behalf of the American Society for Nutrition.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 16 October 2021
                : 06 December 2021
                : 07 January 2022
                Page count
                Pages: 9
                Funding
                Funded by: Dutch Dairy Association, DOI 10.13039/501100003266;
                Categories
                Nutrient Physiology, Metabolism, and Nutrient-Nutrient Interactions
                AcademicSubjects/MED00060
                AcademicSubjects/SCI00960

                Nutrition & Dietetics
                stable isotope tracers,protein metabolism,muscle metabolism,whole foods,dietary protein,dairy,fermented dairy,food processing,food matrix,healthy young males

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