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

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 30g 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, twenty healthy, 18–35y old males ingested 30g 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 exercise. Primed, continuous intravenous L-[ring-13C6]-phenylalanine infusions were combined with the collection of blood and muscle tissue samples to assess postabsorptive and 4h 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 x 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 x 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 30g protein are ingested at rest or during recovery from exercise in healthy, young males. This trial was registered at www.trialregister.nl as NL7941 (https://www.trialregister.nl/trial/7941).

Mycoprotein ingestion within or without its wholefood matrix results in equivalent stimulation of myofibrillar protein synthesis rates in resting and exercised muscle of young men

“…Though the timing of the biopsies in the present study prohibited us from being able to detect a potential earlier (e.g. 2 rather than 4 h) stimulation of MyoPS and mTOR phosphorylaion in the PCM condition, our data contribute towards a growing number of studies that imply the plasma leucinaemic response is more, but not consistently so (30,31) , predictive of postprandial MPS rates when comparing consumption of isolated rather than whole-food protein sources (12,13,26,29,32) . However, taking the pivotal role of leucine at facevalue, it is interesting to speculate as to the role that the wholefood matrix may still have played in the stimulation of MyoPS in the present study.…”

Gastric emptying and nutrient absorption of pea protein products differing in heat treatment and texture: a randomizedin vivocrossover trial andin vitrodigestion study

“…The attenuated rise in postprandial AA concentrations after consumption of a solid versus liquid form was reported in multiple studies (Conley, et al, 2011; de Hart, et al, 2021; Hermans, et al, 2022; A. M. H. Horstman, et al, 2021). However, these studies compared products that did not only differ in texture, but also macro- and micronutrient composition, protein composition and/or volume.…”

Association of postprandial postexercise muscle protein synthesis rates with dietary leucine: A systematic review

“…Figure 1 shows the process of article selection with 38 studies ultimately included. Within these 38 studies, there were 77 study arms (i.e., total number of eligible intervention groups), to determine aspects relating to the leucine threshold hypothesis (Supplementary Information—https://doi.org/10.6084/m9.figshare.22203514, Agergaard et al, 2017; Areta et al, 2014; Atherton et al, 2017; Beals et al, 2018; Borack et al, 2016; Brook et al, 2021; Bukhari et al, 2015; Burd et al, 2010, 2015; Burd, Andrews, et al, 2012; Burd, Yang, et al, 2012; Chan et al, 2019; Churchward‐Venne, Breen, et al, 2014; Churchward‐Venne, Cotie, et al, 2014; Devries et al, 2018a, 2018b; Dickinson et al, 2014; Dideriksen et al, 2016; Dreyer et al, 2008; Fujita et al, 2009; Gwin et al, 2021; Hermans et al, 2021, 2022; Luiking et al, 2014; McGlory et al, 2016; McKendry et al, 2016; Mikkelsen et al, 2015; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Finnigan, et al, 2020; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Jackman, et al, 2020; Moore, Tang, et al, 2009; Oikawa et al, 2020; Pinckaers et al, 2022; Reidy et al, 2013; Reitelseder et al, 2019; Symons et al, 2011; Van Vliet et al, 2017; West et al, 2009; Wilkinson et al, 2018). Studies which met all the inclusion criteria except not taking a basal muscle biopsy (i.e., Dideriksen et al, 2011) were excluded in order to calculate delta change from basal MPS.…”

“…Bolus doses of orally administered isolated proteins comprised: whey (33 study arms), casein (three study arms), milk protein concentrate (10 study arms), crystalline essential amino acid mixtures (nine study arms), and isolated protein blends (four study arms). Other sources included protein‐rich foods: pork (two study arms; Beals et al, 2018), beef (three study arms; Burd et al, 2015; Symons et al, 2011), mycoprotein (two study arms; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Finnigan, et al, 2020; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Jackman, et al, 2020), protein‐rich meal replacements (four study arms; Atherton et al, 2017), cheese (Hermans et al, 2022), meal worms (Hermans et al, 2021), collagen protein, potato protein (Pinckaers et al, 2022), egg white (Van Vliet et al, 2017), and egg yolk (Van Vliet et al, 2017), all with one study arm each.…”