Leucine co-ingestion improves post-prandial muscle protein accretion in elderly men

Wall, Benjamin T.; Hamer, Henrike M.; Lange, Anneke de; Kiskini, Alexandra; Groen, Bart B. L.; Senden, Joan M.; Gijsen, Annemie P.; Verdijk, Lex B.; Loon, Luc J. C. van

doi:10.1016/j.clnu.2012.09.002

Cited by 186 publications

(164 citation statements)

References 48 publications

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“…The postprandial rise in plasma essential amino acids, and leucine in particular, is a key factor for driving the stimulation of postprandial muscle protein synthesis (Dreyer et al 2008, Wall et al 2013. In the present study, ingestion of a meal-like amount of protein rapidly principle data from our lab comparing plasma amino acid availability after protein ingestion in an upright sitting versus head-tilted down body position (Holwerda et al 2016).…”

Section: Discussionmentioning

confidence: 85%

“…The post-prandial increase in muscle protein synthesis rate has been attributed to the rise in circulating (essential) amino acid concentrations, with the post-prandial rise in circulating plasma leucine concentrations being of particular relevance (Dreyer et al 2008, Wall et al 2013. Regulation of the post-prandial muscle protein synthetic response occurs on multiple levels, ranging from protein digestion and amino acid absorption (Koopman et al 2009), post-prandial insulin release and subsequent muscle perfusion (Rasmussen et al 2006), amino acid uptake in muscle (Dickinson et al 2013), activation of anabolic signaling pathways (Fry et al 2011), and subsequent myofibrillar protein synthesis (Yang et al 2012b, 2012a, Burd et al 2015.…”

Section: Introductionmentioning

confidence: 99%

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Food ingestion in an upright sitting position increases postprandial amino acid availability when compared with food ingestion in a lying down position

Holwerda

Lenaerts

Bierau

et al. 2017

Appl. Physiol. Nutr. Metab.

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Section: Discussionmentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Food ingestion in an upright sitting position increases postprandial amino acid availability when compared with food ingestion in a lying down position

Holwerda

Lenaerts

Bierau

et al. 2017

Appl. Physiol. Nutr. Metab.

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“…It is important to note that acute studies examining phosphorylation or insulin availability after resistance exercise and/or amino acid ingestion are primarily used to predict longer-term training outcomes (i.e., skeletal muscle hypertrophy) and as such, there may be a disconnect between these anabolic signals and end-point measures of protein synthesis [42]. Nevertheless, insulinotropic effects of leucine and/or BCAA may help to improve net muscle protein balance by increasing muscle protein synthesis [31,39,40], decreasing muscle protein breakdown [42], or both. This may be particularly important in long-standing T2D patients where insulin levels are chronically low.…”

Section: Branched Chain Amino Acidsmentioning

confidence: 99%

Insulinotropic and Muscle Protein Synthetic Effects of Branched-Chain Amino Acids: Potential Therapy for Type Diabetes and Sarcopenia

Manders¹,

Little²,

Forbes³

et al. 2016

Clinical Nutrition and Aging

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Abstract:The loss of muscle mass and strength with aging (i.e., sarcopenia) has a negative effect on functional independence and overall quality of life. One main contributing factor to sarcopenia is the reduced ability to increase skeletal muscle protein synthesis in response to habitual feeding, possibly due to a reduction in postprandial insulin release and an increase in insulin resistance. Branched-chain amino acids (BCAA), primarily leucine, increases the activation of pathways involved in muscle protein synthesis through insulin-dependent and independent mechanisms, which may help counteract the -anabolic resistance‖ to feeding in older adults. Leucine exhibits strong insulinotropic characteristics, which may increase amino acid availability for muscle protein synthesis, reduce muscle protein breakdown, and enhance glucose disposal to help maintain blood glucose homeostasis.

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“…13 C]labeled phenylalanine, respectively (42). Standard regression curves were applied from a series of known standard enrichment values against the measured values to assess the linearity of the mass spectrometer and to account for any isotope fractionation that may have occurred during the analysis.…”

Section: Preparation Of Intrinsically Labeled Protein Intrinsically mentioning

confidence: 99%

“…This "anabolic resistance" to food intake is now regarded as a key factor in the etiology of sarcopenia (26,41). Accordingly, we (18,23,42) and many others (8,25,29,32) have begun to investigate ways to overcome anabolic resistance in older individuals in an effort to develop more effective strategies to attenuate age-related muscle loss and support healthy aging.…”

mentioning

confidence: 99%

A single session of neuromuscular electrical stimulation does not augment postprandial muscle protein accretion

Dirks

Wall

Krämer

et al. 2016

American Journal of Physiology-Endocrinology and Metabolism

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-The loss of muscle mass and strength that occurs with aging, termed sarcopenia, has been (at least partly) attributed to an impaired muscle protein synthetic response to food intake. Previously, we showed that neuromuscular electrical stimulation (NMES) can stimulate fasting muscle protein synthesis rates and prevent muscle atrophy during disuse. We hypothesized that NMES prior to protein ingestion would increase postprandial muscle protein accretion. Eighteen healthy elderly (69 Ϯ 1 yr) males participated in this study. After a 70-min unilateral NMES protocol was performed, subjects ingested 20 g of intrinsically L-[1-13 C] phenylalanine-labeled casein. Plasma samples and muscle biopsies were collected to assess postprandial mixed muscle and myofibrillar protein accretion as well as associated myocellular signaling during a 4-h postprandial period in both the control (CON) and stimulated (NMES) leg. Protein ingestion resulted in rapid increases in both plasma phenylalanine concentrations and L-[1-13 C]phenylalanine enrichments, which remained elevated during the entire 4-h postprandial period (P Ͻ 0.05). Mixed-muscle protein-bound L-[1-13 C]phenylalanine enrichments increased significantly over time following protein ingestion, with no differences between the CON (0.0164 Ϯ 0.0019 MPE) and NMES (0.0164 Ϯ 0.0019 MPE) leg (P Ͼ 0.05). In agreement, no differences were observed in the postprandial rise in myofibrillar protein bound L-[1-13 C]phenylalanine enrichments between the CON and NMES legs (0.0115 Ϯ 0.0014 vs. 0.0133 Ϯ 0.0013 MPE, respectively, P Ͼ 0.05). Significant increases in mTOR and P70S6K phosphorylation status were observed in the NMESstimulated leg only (P Ͻ 0.05). We conclude that a single session of NMES prior to food intake does not augment postprandial muscle protein accretion in healthy older men. neuromuscular electrical stimulation; muscle protein synthesis; skeletal muscle; sarcopenia; disuse AGING IS ACCOMPANIED BY DECLINES in skeletal muscle mass and strength, termed sarcopenia (24). A less than optimal diet and sedentary lifestyle are factors contributing to sarcopenia (24,30). However, the underlying mechanisms remain to be elucidated. From a physiological perspective, any loss of muscle mass must be attributed to an imbalance between muscle protein synthesis and breakdown rates. Research has generally demonstrated that basal (i.e., postabsorptive) muscle protein synthesis (8,18,36,41) and breakdown (37, 48) rates do not change with advancing age. As such, research has since focused on the impact of aging on the anabolic response to food intake. Recent work has shown that the skeletal muscle protein synthetic response to dietary protein ingestion is impaired in older individuals (8,20,41). This "anabolic resistance" to food intake is now regarded as a key factor in the etiology of sarcopenia (26, 41). Accordingly, we (18, 23, 42) and many others (8,25,29,32) have begun to investigate ways to overcome anabolic resistance in older individuals in an effort to develop more effective strategi...

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Leucine co-ingestion improves post-prandial muscle protein accretion in elderly men

Cited by 186 publications

References 48 publications

Food ingestion in an upright sitting position increases postprandial amino acid availability when compared with food ingestion in a lying down position

Food ingestion in an upright sitting position increases postprandial amino acid availability when compared with food ingestion in a lying down position

Insulinotropic and Muscle Protein Synthetic Effects of Branched-Chain Amino Acids: Potential Therapy for Type Diabetes and Sarcopenia

A single session of neuromuscular electrical stimulation does not augment postprandial muscle protein accretion

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