Ingestion of Casein in a Milk Matrix Modulates Dietary Protein Digestion and Absorption Kinetics but Does Not Modulate Postprandial Muscle Protein Synthesis in Older Men

Churchward‐Venne, Tyler A.; Snijders, Tim; Linkens, Armand M.A.; Hamer, Henrike M.; Kranenburg, Janneau van; Loon, Luc J. C. van

doi:10.3945/jn.115.213710

Cited by 44 publications

(29 citation statements)

References 34 publications

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“…From these studies, it is not possible to elucidate the food component(s), or mechanism, within the dairy matrix that may have contributed to the differential regulation of post-exercise muscle protein synthesis rates between the ingested food sources. Interestingly, studies have demonstrated that co-ingestion of micellar casein with individual food components such as milk fat [ 40 ], carbohydrates [ 41 ], or milk serum ([ 42 ]; mixture of 10% lactose, 0.3% protein, 0.06% fat, and 1.1% minerals) does not further augment the postprandial muscle protein synthetic response when compared to ingestion of micellar casein alone. It is worth noting, however, that these studies were conducted at rest, and perhaps an exercise stimulus may be required to create a more physiologically relevant interaction between dietary amino acids and the non-protein components of the whole food at the muscle level.…”

Section: Food Matrixmentioning

confidence: 99%

Food-First Approach to Enhance the Regulation of Post-exercise Skeletal Muscle Protein Synthesis and Remodeling

et al. 2019

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Protein recommendations are provided on a daily basis as defined by the recommended dietary allowance (RDA) at 0.80 g protein/kg/day. However, meal-based, as opposed to daily, dietary protein recommendations are likely more informative given the role of the daily protein distribution pattern in modulating the post-exercise muscle protein synthetic response. Current protein meal recommendations to plateau post-exercise muscle protein synthesis rates are based on the ingestion of isolated protein sources, and not protein-rich whole foods. It is generally more common to eat whole food sources of dietary protein within a normal eating pattern to meet dietary protein requirements. Yet, there is a need to define how dietary protein action on muscle protein synthesis rates can be modulated by other nutrients within a food matrix to achieve protein requirements for optimal muscle adaptations. Recent developments suggest that the identification of an “optimal” protein source should likely consider the characteristics of the protein and the food matrix in which it is consumed. This review aims to discuss recent concepts related to protein quality, and the potential interactive effects of the food matrix, to achieve optimal protein requirements and elicit a robust postprandial muscle protein synthetic response with an emphasis on the post-exercise recovery window.

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Section: Food Matrixmentioning

confidence: 99%

Food-First Approach to Enhance the Regulation of Post-exercise Skeletal Muscle Protein Synthesis and Remodeling

et al. 2019

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“…Three studies in older adults have manipulated the form of an amino acid/protein source and measured resting postprandial rates of MPS [ 17 , 52 , 53 , 54 ]. Koopman et al [ 52 ] compared liquid supplements of intact casein and casein hydrolysate and reported a greater blood amino acid availability, and a trend for a greater response of MPS, to ingestion of casein hydrolysate.…”

Section: Synthesis Of Findingsmentioning

confidence: 99%

“…Koopman et al [ 52 ] compared liquid supplements of intact casein and casein hydrolysate and reported a greater blood amino acid availability, and a trend for a greater response of MPS, to ingestion of casein hydrolysate. The same research group recently reported that ingestion of casein in its naturally occurring milk matrix form resulted in a reduced blood amino acid availability (possibly due to delayed amino acid digestion/absorption kinetics), but did not modulate postprandial rates of MPS compared with ingestion of isolated intact micellar casein [ 53 ]. A similar result was reported by Pennings et al [ 54 ] whereby the ingestion of minced beef, that is easily masticated and digested, stimulated a more rapid increase in arterialised blood EAA availability compared with an equivalent amount of intact steak, however no difference in the 6 h postprandial response of MPS was observed between conditions.…”

Section: Synthesis Of Findingsmentioning

confidence: 99%

“…A similar result was reported by Pennings et al [ 54 ] whereby the ingestion of minced beef, that is easily masticated and digested, stimulated a more rapid increase in arterialised blood EAA availability compared with an equivalent amount of intact steak, however no difference in the 6 h postprandial response of MPS was observed between conditions. These findings [ 17 , 53 ] suggest that, at least in the early resting postprandial period, the rate of blood amino acid availability does not translate into an increased stimulation of MPS. However, it must be recognised that these findings are in the context of a single feeding period under resting conditions.…”

Section: Synthesis Of Findingsmentioning

confidence: 99%

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Protein Considerations for Optimising Skeletal Muscle Mass in Healthy Young and Older Adults

et al. 2016

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Skeletal muscle is critical for human health. Protein feeding, alongside resistance exercise, is a potent stimulus for muscle protein synthesis (MPS) and is a key factor that regulates skeletal muscle mass (SMM). The main purpose of this narrative review was to evaluate the latest evidence for optimising the amino acid or protein source, dose, timing, pattern and macronutrient coingestion for increasing or preserving SMM in healthy young and healthy older adults. We used a systematic search strategy of PubMed and Web of Science to retrieve all articles related to this review objective. In summary, our findings support the notion that protein guidelines for increasing or preserving SMM are more complex than simply recommending a total daily amount of protein. Instead, multifactorial interactions between protein source, dose, timing, pattern and macronutrient coingestion, alongside exercise, influence the stimulation of MPS, and thus should be considered in the context of protein recommendations for regulating SMM. To conclude, on the basis of currently available scientific literature, protein recommendations for optimising SMM should be tailored to the population or context of interest, with consideration given to age and resting/post resistance exercise conditions.

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“…Extensive research performed throughout the past two decades has revealed distinct differences in the digestion and absorption kinetics of different milk proteins. Previous work has shown that plasma amino acid responses differ following the ingestion of casein v. whey protein (6,9) , casein v. casein hydrolysate (4) and casein ingested within or separate from the milk matrix (11) . Throughout the literature, substantial differences have been observed in the post-prandial plasma amino acid responses following the ingestion of such proteins or protein fractions (4)(5)(6)9,12) .…”

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confidence: 99%

The glycation level of milk protein strongly modulates post-prandial lysine availability in humans

et al. 2019

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Industrial heat treatment of milk results in protein glycation. A high protein glycation level has been suggested to compromise the post-prandial rise in plasma amino acid availability following protein ingestion. In the present study, we assessed the impact of glycation level of milk protein on post-prandial plasma amino acid responses in humans. Fifteen healthy, young men (age 26 (SEM 1) years, BMI 24 (SEM 1) kg/m2) participated in this randomised cross-over study and ingested milk protein powder with protein glycation levels of 3, 20 and 50 % blocked lysine. On each trial day, arterialised blood samples were collected at regular intervals during a 6-h post-prandial period to assess plasma amino acid concentrations using ultra-performance liquid chromatography. Plasma essential amino acid (EAA) concentrations increased following milk protein ingestion, with the 20 and 50 % glycated milk proteins showing lower overall EAA responses compared with the 3 % glycated milk protein (161 (SEM 7) and 142 (SEM 7) v. 178 (SEM 9) mmol/l × 6 h, respectively; P ≤ 0·011). The lower post-prandial plasma amino acid responses were fully attributed to an attenuated post-prandial rise in circulating plasma lysine concentrations. Plasma lysine responses (incremental AUC) following ingestion of the 20 and 50 % glycated milk proteins were 35 (SEM 4) and 92 (SEM 2) % lower compared with the 3 % glycated milk protein (21·3 (SEM 1·4) and 2·8 (SEM 0·7) v. 33·3 (SEM 1·7) mmol/l × 6 h, respectively; P < 0·001). Milk protein glycation lowers post-prandial plasma lysine availability in humans. The lower post-prandial availability of lysine following ingestion of proteins with a high glycation level may compromise the anabolic properties of a protein source.

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Ingestion of Casein in a Milk Matrix Modulates Dietary Protein Digestion and Absorption Kinetics but Does Not Modulate Postprandial Muscle Protein Synthesis in Older Men

Abstract: Casein ingestion in a milk matrix delays protein digestion and absorption but does not modulate postprandial muscle protein synthesis when compared to the ingestion of micellar casein only in healthy older men. This trial was registered at Nederlands Trial Register as NTR4429.

Cited by 44 publications

References 34 publications

Food-First Approach to Enhance the Regulation of Post-exercise Skeletal Muscle Protein Synthesis and Remodeling

Food-First Approach to Enhance the Regulation of Post-exercise Skeletal Muscle Protein Synthesis and Remodeling

Protein Considerations for Optimising Skeletal Muscle Mass in Healthy Young and Older Adults

The glycation level of milk protein strongly modulates post-prandial lysine availability in humans

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