» Articles » PMID: 30698812

Myofibrillar and Mitochondrial Protein Synthesis Rates Do Not Differ in Young Men Following the Ingestion of Carbohydrate with Whey, Soy, or Leucine-Enriched Soy Protein After Concurrent Resistance- and Endurance-Type Exercise

Overview
Journal J Nutr
Publisher Elsevier
Date 2019 Jan 31
PMID 30698812
Citations 20
Authors
Affiliations
Soon will be listed here.
Abstract

Background: Protein ingestion during recovery from resistance-type exercise increases postexercise muscle protein synthesis rates. Whey protein has been reported to have greater anabolic properties than soy protein, an effect which may be attributed to the higher leucine content of whey.

Objective: The objective of this study was to compare postprandial myofibrillar (MyoPS) and mitochondrial (MitoPS) protein synthesis rates after ingestion of carbohydrate with whey, soy, or soy protein enriched with free leucine (to match the leucine content of whey) during recovery from a single bout of concurrent resistance- and endurance-type exercise in young healthy men.

Methods: In a randomized, double-blind, parallel-group design, 36 healthy young recreationally active men (mean ± SEM age: 23 ± 0.4 y) received a primed continuous infusion of l-[ring-13C6]-phenylalanine and l-[ring-3,5-2H2]-tyrosine and ingested 45 g carbohydrate with 20 g protein from whey (WHEY), soy (SOY), or leucine-enriched soy (SOY + LEU) after concurrent resistance- and endurance-type exercise. Blood and muscle biopsies were collected over a 360 min postexercise recovery period to assess MyoPS and MitoPS rates, and associated signaling through the mammalian target of rapamycin complex 1 (mTORC1).

Results: Postprandial peak plasma leucine concentrations were significantly higher in WHEY (mean ± SEM: 322 ± 10 μmol/L) and SOY + LEU (328 ± 14 μmol/L) compared with SOY (216 ± 6 μmol/L) (P < 0.05). Despite the apparent differences in plasma leucinemia, MyoPS (WHEY: 0.054 ± 0.002; SOY: 0.053 ± 0.004; SOY + LEU: 0.056 ± 0.004%·h-1; P = 0.83), and MitoPS (WHEY: 0.061 ± 0.004; SOY: 0.061 ± 0.006; SOY + LEU: 0.063 ± 0.004%·h-1; P = 0.96) rates over the entire 360 min recovery period did not differ between treatments. Similarly, signaling through mTORC1Ser2448, p70S6kThr389, 4E-BP1Thr37/46, and rpS6Ser235/236 was similar between treatments.

Conclusion: Postexercise MyoPS and MitoPS rates do not differ after co-ingestion of carbohydrate with 20 g protein from whey, soy, or leucine-enriched soy protein during 360 min of recovery from concurrent resistance- and endurance-type exercise in young, recreationally active men. This trial was registered at Nederlands Trial Register as NTR5098.

Citing Articles

The efficacy and safety of leucine-enriched essential amino acids in knee osteoarthritis patients: A randomized controlled trial.

Park S, Nam C, Ahn H, Kim T Medicine (Baltimore). 2024; 103(19):e38168.

PMID: 38728455 PMC: 11081624. DOI: 10.1097/MD.0000000000038168.


Plant Protein Blend Ingestion Stimulates Postexercise Myofibrillar Protein Synthesis Rates Equivalently to Whey in Resistance-Trained Adults.

van der Heijden I, Monteyne A, West S, Morton J, Langan-Evans C, Hearris M Med Sci Sports Exerc. 2024; 56(8):1467-1479.

PMID: 38537270 PMC: 11810040. DOI: 10.1249/MSS.0000000000003432.


Acute Microbial Protease Supplementation Increases Net Postprandial Plasma Amino Acid Concentrations After Pea Protein Ingestion in Healthy Adults: A Randomized, Double-Blind, Placebo-Controlled Trial.

Paulussen K, Askow A, Deutz M, McKenna C, Garvey S, Guice J J Nutr. 2024; 154(5):1549-1560.

PMID: 38467279 PMC: 11130700. DOI: 10.1016/j.tjnut.2024.03.009.


The muscle protein synthetic response following corn protein ingestion does not differ from milk protein in healthy, young adults.

Pinckaers P, Weijzen M, Houben L, Zorenc A, Kouw I, de Groot L Amino Acids. 2024; 56(1):8.

PMID: 38315260 PMC: 10844360. DOI: 10.1007/s00726-023-03377-z.


Post-prandial muscle protein synthesis rates following the ingestion of pea-derived protein do not differ from ingesting an equivalent amount of milk-derived protein in healthy, young males.

Pinckaers P, Smeets J, Kouw I, Goessens J, Gijsen A, de Groot L Eur J Nutr. 2024; 63(3):893-904.

PMID: 38228945 PMC: 10948472. DOI: 10.1007/s00394-023-03295-6.


References
1.
Reidy P, Rasmussen B . Role of Ingested Amino Acids and Protein in the Promotion of Resistance Exercise-Induced Muscle Protein Anabolism. J Nutr. 2016; 146(2):155-83. PMC: 4725426. DOI: 10.3945/jn.114.203208. View

2.
Yang Y, Churchward-Venne T, Burd N, Breen L, Tarnopolsky M, Phillips S . Myofibrillar protein synthesis following ingestion of soy protein isolate at rest and after resistance exercise in elderly men. Nutr Metab (Lond). 2012; 9(1):57. PMC: 3478988. DOI: 10.1186/1743-7075-9-57. View

3.
Tipton K, Ferrando A, Phillips S, Doyle Jr D, Wolfe R . Postexercise net protein synthesis in human muscle from orally administered amino acids. Am J Physiol. 1999; 276(4):E628-34. DOI: 10.1152/ajpendo.1999.276.4.E628. View

4.
Burd N, Yang Y, Moore D, Tang J, Tarnopolsky M, Phillips S . Greater stimulation of myofibrillar protein synthesis with ingestion of whey protein isolate v. micellar casein at rest and after resistance exercise in elderly men. Br J Nutr. 2012; 108(6):958-62. DOI: 10.1017/S0007114511006271. View

5.
Boirie Y, Dangin M, Gachon P, Vasson M, Maubois J, Beaufrere B . Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A. 1998; 94(26):14930-5. PMC: 25140. DOI: 10.1073/pnas.94.26.14930. View