Publications by authors named "Luc J C VAN Loon"

349 Publications

A White Paper on Collagen Hydrolyzates and Ultrahydrolyzates: Potential Supplements to Support Joint Health in Osteoarthritis?

Curr Rheumatol Rep 2021 10 30;23(11):78. Epub 2021 Oct 30.

Colorado Program for Musculoskeletal Research, Department of Orthopedics, University of Colorado Anschutz Medical Campus, Aurora, CO, USA.

Purpose Of Review: Osteoarthritis (OA) is the most common forms of arthritis in the general population, accounting for more pain and functional disability than any other musculoskeletal disease. There are currently no approved disease modifying drugs for OA. In the absence of effective pharmacotherapy, many patients with OA turn to nutritional supplements and nutraceuticals, including collagen derivatives. Collagen hydrolyzates and ultrahydrolyzates are terms used to describe collagens that have been broken down into small peptides and amino acids in the presence of collagenases and high pressure.

Recent Findings: This article reviews the relevant literature and serves as a White Paper on collagen hydrolyzates and ultrahydrolyzates as emerging supplements often advertised to support joint health in OA. Collagen hydrolyzates have demonstrated some evidence of efficacy in a handful of small scale clinical trials, but their ability to treat and reverse advanced joint disease remains highly speculative, as is the case for other nutritional supplements. The aim of this White Paper is to stimulate research and development of collagen-based supplements for patients with OA and other musculoskeletal diseases at academic and industrial levels. This White Paper does not make any treatment recommendations for OA patients in the clinical context, but simply aims to highlight opportunities for scientific innovation and interdisciplinary collaboration, which are crucial for the development of novel products and nutritional interventions based on the best available and published evidence.
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http://dx.doi.org/10.1007/s11926-021-01042-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8556166PMC
October 2021

Hepatic Steatosis Contributes to the Development of Muscle Atrophy Inter-Organ Crosstalk.

Front Endocrinol (Lausanne) 2021 11;12:733625. Epub 2021 Oct 11.

Department of Human Biology, School of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University, Maastricht, Netherlands.

Individuals with hepatic steatosis often display several metabolic abnormalities including insulin resistance and muscle atrophy. Previously, we found that hepatic steatosis results in an altered hepatokine secretion profile, thereby inducing skeletal muscle insulin resistance inter-organ crosstalk. In this study, we aimed to investigate whether the altered secretion profile in the state of hepatic steatosis also induces skeletal muscle atrophy effects on muscle protein turnover. To investigate this, eight-week-old male C57BL/6J mice were fed a chow (4.5% fat) or a high-fat diet (HFD; 45% fat) for 12 weeks to induce hepatic steatosis, after which the livers were excised and cut into ~200-µm slices. Slices were cultured to collect secretion products (conditioned medium; CM). Differentiated L6-GLUT4myc myotubes were incubated with chow or HFD CM to measure glucose uptake. Differentiated C2C12 myotubes were incubated with chow or HFD CM to measure protein synthesis and breakdown, and gene expression RNA sequencing. Furthermore, proteomics analysis was performed in chow and HFD CM. It was found that HFD CM caused insulin resistance in L6-GLUT4myc myotubes compared with chow CM, as indicated by a blunted insulin-stimulated increase in glucose uptake. Furthermore, protein breakdown was increased in C2C12 cells incubated with HFD CM, while there was no effect on protein synthesis. RNA profiling of C2C12 cells indicated that 197 genes were differentially expressed after incubation with HFD CM, compared with chow CM, and pathway analysis showed that pathways related to anatomical structure and function were enriched. Proteomics analysis of the CM showed that 32 proteins were differentially expressed in HFD CM compared with chow CM. Pathway enrichment analysis indicated that these proteins had important functions with respect to insulin-like growth factor transport and uptake, and affect post-translational processes, including protein folding, protein secretion and protein phosphorylation. In conclusion, the results of this study support the hypothesis that secretion products from the liver contribute to the development of muscle atrophy in individuals with hepatic steatosis.
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http://dx.doi.org/10.3389/fendo.2021.733625DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8542925PMC
October 2021

Impact of magnesium on bone health in older adults: A systematic review and meta-analysis.

Bone 2021 Oct 16;154:116233. Epub 2021 Oct 16.

Division of Human Nutrition and Health, Wageningen University & Research, P.O. Box 17, 6700 AA Wageningen, the Netherlands.

Background: Magnesium plays a key role in bone health and may, therefore, represent an interesting nutrient for the prevention of bone loss and osteoporosis. The aim of this systematic review and meta-analysis was to investigate the impact of magnesium intake from any source on bone mineral density (BMD), bone mineral content (BMC), bone turnover markers, and fracture risk in older adults.

Methods: A systematic search was conducted using Embase, Medline Ovid and Cochrane Central from database inception to October 2020. All studies that related magnesium intake with bone health outcomes among adults aged ≥60 years were included. Two investigators independently conducted abstract and full-text screenings, data extractions, and risk of bias assessments. Authors were contacted for missing data.

Results: Once 787 records were screened, six cohort studies, one case-control study and five cross-sectional studies were included. Qualitative evaluation demonstrated a positive trend between higher magnesium intake and higher hip and femoral neck BMD. Meta-analysis of four studies showed a significant positive association between magnesium intake and hip BMD (pooled beta: 0.03, 95% CI: 0.01-0.06, p < 0.05).

Conclusions: This systematic review indicates that a higher magnesium intake may support an increase in hip and femoral neck BMD. Due to limited research no associations with BMD at other sites or fractures were found. There is a need for properly designed cohort studies to determine the association between magnesium intake and bone health in older adults. Next, large and long-term randomized controlled trials in older adults are needed to determine whether an increase in magnesium (supplementation) intake can improve bone health. The combination of several bone nutrients (calcium, vitamin D, protein, magnesium and potentially more) may be needed for the most optimal effect on bone health and to delay or prevent the development of osteoporosis.
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http://dx.doi.org/10.1016/j.bone.2021.116233DOI Listing
October 2021

L-arabinose co-ingestion delays glucose absorption derived from sucrose in healthy men and women: a double-blind, randomised crossover trial.

Br J Nutr 2021 Oct 18:1-10. Epub 2021 Oct 18.

Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University, Universiteitssingel 50, 6229 ERMaastricht, The Netherlands.

Dietary interventions to delay carbohydrate digestion or absorption can effectively prevent hyperglycaemia in the early postprandial phase. L-arabinose can specifically inhibit sucrase. It remains to be assessed whether co-ingestion of L-arabinose with sucrose delays sucrose digestion, attenuates subsequent glucose absorption and impacts hepatic glucose output. In this double-blind, randomised crossover study, we assessed blood glucose kinetics following ingestion of a 200-ml drink containing 50 g of sucrose with 7·5 g of L-arabinose (L-ARA) or without L-arabinose (CONT) in twelve young, healthy participants (24 ± 1 years; BMI: 22·2 ± 0·5 kg/m2). Plasma glucose kinetics were determined by a dual stable isotope methodology involving ingestion of (U-13C6)-glucose-enriched sucrose, and continuous intravenous infusion of (6,6-2H2)-glucose. Peak glucose concentrations reached 8·18 ± 0·29 mmol/l for CONT 30 min after ingestion. In contrast, the postprandial rise in plasma glucose was attenuated for L-ARA, because peak glucose concentrations reached 6·62 ± 0·18 mmol/l only 60 min after ingestion. The rate of exogenous glucose appearance for L-ARA was 67 and 57 % lower compared with CONT at t = 15 min and 30 min, respectively, whereas it was 214 % higher at t = 150 min, indicating a more stable absorption of exogenous glucose for L-ARA compared with CONT. Total glucose disappearance during the first hour was lower for L-ARA compared with CONT (11 ± 1 v. 17 ± 1 g, P < 0·0001). Endogenous glucose production was not differentially affected at any time point (P = 0·27). Co-ingestion of L-arabinose with sucrose delays sucrose digestion, resulting in a slower absorption of sucrose-derived glucose without causing adverse effects in young, healthy adults.
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http://dx.doi.org/10.1017/S0007114521004153DOI Listing
October 2021

Ingestion of Free Amino Acids Compared with an Equivalent Amount of Intact Protein Results in More Rapid Amino Acid Absorption and Greater Postprandial Plasma Amino Acid Availability Without Affecting Muscle Protein Synthesis Rates in Young Adults in a Double-Blind Randomized Trial.

J Nutr 2021 Oct 12. Epub 2021 Oct 12.

Department of Human Biology, School of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University Medical Centre+, Maastricht, The Netherlands.

Background: The rate of protein digestion and amino acid absorption determines the postprandial rise in circulating amino acids and modulates postprandial muscle protein synthesis rates.

Objective: We sought to compare protein digestion, amino acid absorption kinetics, and the postprandial muscle protein synthetic response following ingestion of intact milk protein or an equivalent amount of free amino acids.

Methods: Twenty-four healthy, young participants (mean ± SD age: 22 ± 3 y and BMI 23 ± 2 kg/m2; sex: 12 male and 12 female participants) received a primed continuous infusion of l-[ring-2H5]-phenylalanine and l-[ring-3,5-2H2]-tyrosine, after which they ingested either 30 g intrinsically l-[1-13C]-phenylalanine-labeled milk protein or an equivalent amount of free amino acids labeled with l-[1-13C]-phenylalanine. Blood samples and muscle biopsies were obtained to assess protein digestion and amino acid absorption kinetics (secondary outcome), whole-body protein net balance (secondary outcome), and mixed muscle protein synthesis rates (primary outcome) throughout the 6-h postprandial period.

Results: Postprandial plasma amino acid concentrations increased after ingestion of intact milk protein and free amino acids (both P < 0.001), with a greater increase following ingestion of the free amino acids than following ingestion of intact milk protein (P-time × treatment < 0.001). Exogenous phenylalanine release into plasma, assessed over the 6-h postprandial period, was greater with free amino acid ingestion (76 ± 9%) than with milk protein treatment (59 ± 10%; P < 0.001). Ingestion of free amino acids and intact milk protein increased mixed muscle protein synthesis rates (P-time < 0.001), with no differences between treatments (from 0.037 ± 0.015%/h to 0.053 ± 0.014%/h and 0.039 ± 0.016%/h to 0.051 ± 0.010%/h, respectively; P-time × treatment = 0.629).

Conclusions: Ingestion of a bolus of free amino acids leads to more rapid amino acid absorption and greater postprandial plasma amino acid availability than ingestion of an equivalent amount of intact milk protein. Ingestion of free amino acids may be preferred over ingestion of intact protein in conditions where protein digestion and amino acid absorption are compromised.
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http://dx.doi.org/10.1093/jn/nxab305DOI Listing
October 2021

The impact of collagen protein ingestion on musculoskeletal connective tissue remodeling: a narrative review.

Nutr Rev 2021 Oct 4. Epub 2021 Oct 4.

NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+, Maastricht, The Netherlands.

Collagen is the central structural component of extracellular connective tissue, which provides elastic qualities to tissues. For skeletal muscle, extracellular connective tissue transmits contractile force to the tendons and bones. Connective tissue proteins are in a constant state of remodeling and have been shown to express a high level of plasticity. Dietary-protein ingestion increases muscle protein synthesis rates. High-quality, rapidly digestible proteins are generally considered the preferred protein source to maximally stimulate myofibrillar (contractile) protein synthesis rates. In contrast, recent evidence demonstrates that protein ingestion does not increase muscle connective tissue protein synthesis. The absence of an increase in muscle connective tissue protein synthesis after protein ingestion may be explained by insufficient provision of glycine and/or proline. Dietary collagen contains large amounts of glycine and proline and, therefore, has been proposed to provide the precursors required to facilitate connective tissue protein synthesis. This literature review provides a comprehensive evaluation of the current knowledge on the proposed benefits of dietary collagen consumption to stimulate connective tissue remodeling to improve health and functional performance.
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http://dx.doi.org/10.1093/nutrit/nuab083DOI Listing
October 2021

The Anabolic Response to Plant-Based Protein Ingestion.

Sports Med 2021 Sep 13;51(Suppl 1):59-74. Epub 2021 Sep 13.

Department of Human Biology, School of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University Medical Centre+, P.O. Box 616, 6200 MD, Maastricht, The Netherlands.

There is a global trend of an increased interest in plant-based diets. This includes an increase in the consumption of plant-based proteins at the expense of animal-based proteins. Plant-derived proteins are now also frequently applied in sports nutrition. So far, we have learned that the ingestion of plant-derived proteins, such as soy and wheat protein, result in lower post-prandial muscle protein synthesis responses when compared with the ingestion of an equivalent amount of animal-based protein. The lesser anabolic properties of plant-based versus animal-derived proteins may be attributed to differences in their protein digestion and amino acid absorption kinetics, as well as to differences in amino acid composition between these protein sources. Most plant-based proteins have a low essential amino acid content and are often deficient in one or more specific amino acids, such as lysine and methionine. However, there are large differences in amino acid composition between various plant-derived proteins or plant-based protein sources. So far, only a few studies have directly compared the muscle protein synthetic response following the ingestion of a plant-derived protein versus a high(er) quality animal-derived protein. The proposed lower anabolic properties of plant- versus animal-derived proteins may be compensated for by (i) consuming a greater amount of the plant-derived protein or plant-based protein source to compensate for the lesser quality; (ii) using specific blends of plant-based proteins to create a more balanced amino acid profile; (iii) fortifying the plant-based protein (source) with the specific free amino acid(s) that is (are) deficient. Clinical studies are warranted to assess the anabolic properties of the various plant-derived proteins and their protein sources in vivo in humans and to identify the factors that may or may not compromise the capacity to stimulate post-prandial muscle protein synthesis rates. Such work is needed to determine whether the transition towards a more plant-based diet is accompanied by a transition towards greater dietary protein intake requirements.
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http://dx.doi.org/10.1007/s40279-021-01540-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8566416PMC
September 2021

Amino acid removal during hemodialysis can be compensated for by protein ingestion and is not compromised by intradialytic exercise: a randomized controlled crossover trial.

Am J Clin Nutr 2021 Sep 12. Epub 2021 Sep 12.

Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University, Maastricht, The Netherlands.

Background: Patients with end-stage renal disease (ESRD) undergoing hemodialysis experience a rapid decline in skeletal muscle mass and strength. Hemodialysis removes amino acids (AAs) from the circulation, thereby lowering plasma AA concentrations and stimulating proteolysis.

Objectives: In the present study, we evaluate the impact of intradialytic protein ingestion at rest and following exercise on AA removal and plasma AA availability in patients with ESRD.

Methods: Ten patients (age: 65 ± 16 y, male/female: 8/2, BMI: 24.2 ± 4.8 kg/m2, serum albumin: 3.4 ± 0.3 g/dL) with ESRD undergoing hemodialysis participated in this randomized controlled crossover trial. During 4 hemodialysis sessions, patients were assigned to ingest 40 g protein or a placebo 60 min after initiation, both at rest (PRO and PLA, respectively) and following exercise (PRO + EX and PLA + EX, respectively). Spent dialysate and blood samples were collected every 30 min throughout hemodialysis to assess AA removal and plasma AA availability.

Results: Plasma AA concentrations declined by 26.1 ± 4.5% within 30 min after hemodialysis initiation during all interventions (P < 0.001, η2p > 0.79). Protein ingestion, but not intradialytic exercise, increased AA removal throughout hemodialysis (9.8 ± 2.0, 10.2 ± 1.6, 16.7 ± 2.2, and 17.3 ± 2.3 g during PLA, PLA + EX, PRO, and PRO + EX interventions, respectively; protein effect P < 0.001, η2p = 0.97; exercise effect P = 0.32, η2p = 0.11). Protein ingestion increased plasma AA concentrations until the end of hemodialysis, whereas placebo ingestion resulted in decreased plasma AA concentrations (time effect P < 0.001, η2p > 0.84). Plasma AA availability (incremental AUC) was greater during PRO and PRO + EX interventions (49 ± 87 and 70 ± 34 mmol/L/240 min, respectively) compared with PLA and PLA + EX interventions (-227 ± 54 and -208 ± 68 mmol/L/240 min, respectively; protein effect P < 0.001, η2p = 0.98; exercise effect P = 0.21, η2p = 0.16).

Conclusions: Protein ingestion during hemodialysis compensates for AA removal and increases plasma AA availability both at rest and during recovery from intradialytic exercise. Intradialytic exercise does not compromise AA removal or reduce plasma AA availability during hemodialysis in a postabsorptive or postprandial state.
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http://dx.doi.org/10.1093/ajcn/nqab274DOI Listing
September 2021

Acute Effects of Dietary Nitrate on Exercise Tolerance, Muscle Oxygenation, and Cardiovascular Function in Patients With Peripheral Arterial Disease.

Int J Sport Nutr Exerc Metab 2021 Jul 20:1-12. Epub 2021 Jul 20.

Radboud University Medical Center.

Previous studies have used supplements to increase dietary nitrate intake in clinical populations. Little is known about whether effects can also be induced through vegetable consumption. Therefore, the aim of this study was to assess the impact of dietary nitrate, through nitrate-rich vegetables (NRV) and beetroot juice (BRJ) supplementation, on plasma nitrate and nitrite concentrations, exercise tolerance, muscle oxygenation, and cardiovascular function in patients with peripheral arterial disease. In a randomized crossover design, 18 patients with peripheral arterial disease (age: 73 ± 8 years) followed a nitrate intake protocol (∼6.5 mmol) through the consumption of NRV, BRJ, and nitrate-depleted BRJ (placebo). Blood samples were taken, blood pressure and arterial stiffness were measured in fasted state and 150 min after intervention. Each intervention was followed by a maximal walking exercise test to determine claudication onset time and peak walking time. Gastrocnemius oxygenation was measured by near-infrared spectroscopy. Blood samples were taken and blood pressure was measured 10 min after exercise. Mean plasma nitrate and nitrite concentrations increased (nitrate; Time × Intervention interaction; p < .001), with the highest concentrations after BRJ (494 ± 110 μmol/L) compared with NRV (202 ± 89 μmol/L) and placebo (80 ± 19 μmol/L; p < .001). Mean claudication onset time and peak walking time did not differ between NRV (413 ± 187 s and 745 ± 220 s, respectively), BRJ (392 ± 154 s and 746 ± 176 s), and placebo (403 ± 176 s and 696 ± 222 s) (p = .762 and p = .165, respectively). Gastrocnemius oxygenation, blood pressure, and arterial stiffness were not affected by the intervention. NRV and BRJ intake markedly increase plasma nitrate and nitrite, but this does not translate to improved exercise tolerance, muscle oxygenation, and/or cardiovascular function.
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http://dx.doi.org/10.1123/ijsnem.2021-0054DOI Listing
July 2021

Eat like an athlete: insights of sports nutrition science to support active aging in healthy older adults.

Geroscience 2021 Oct 20;43(5):2485-2495. Epub 2021 Jul 20.

Gatorade Sports Science Institute, PepsiCo Life Sciences, Global R&D, 5500 34th Street West, Bradenton, FL, 34210, USA.

Skeletal muscle mass losses with age are associated with negative health consequences, including an increased risk of developing metabolic disease and the loss of independence. Athletes adopt numerous nutritional strategies to maximize the benefits of exercise training and enhance recovery in pursuit of improving skeletal muscle quality, mass, or function. Importantly, many of the principles applied to enhance skeletal muscle health in athletes may be applicable to support active aging and prevent sarcopenia in the healthy (non-clinical) aging population. Here, we discuss the anabolic properties of protein supplementation in addition to ingredients that may enhance the anabolic effects of protein (e.g. omega 3 s, creatine, inorganic nitrate) in older persons. We conclude that nutritional strategies used in pursuit of performance enhancement in athletes are often applicable to improve skeletal muscle health in the healthy older population when implemented as part of a healthy active lifestyle. Further research is required to elucidate the mechanisms by which these nutrients may induce favourable changes in skeletal muscle and to determine the appropriate dosing and timing of nutrient intakes to support active aging.
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http://dx.doi.org/10.1007/s11357-021-00419-wDOI Listing
October 2021

Increasing Nitrate-Rich Vegetable Intake Lowers Ambulatory Blood Pressure in (pre)Hypertensive Middle-Aged and Older Adults: A 12-Wk Randomized Controlled Trial.

J Nutr 2021 Sep;151(9):2667-2679

Institute for Health Sciences, Department of Physiology, Radboud University Medical Center, Nijmegen, The Netherlands.

Background: Emerging evidence suggests that increasing dietary nitrate intake may be an effective approach to improve cardiovascular health. However, the effects of a prolonged elevation of nitrate intake through an increase in vegetable consumption are understudied.

Objective: Our primary aim was to determine the impact of 12 wk of increased daily consumption of nitrate-rich vegetables or nitrate supplementation on blood pressure (BP) in (pre)hypertensive middle-aged and older adults.

Methods: In a 12-wk randomized, controlled study (Nijmegen, The Netherlands), 77 (pre)hypertensive participants (BP: 144 ± 13/87 ± 7 mmHg, age: 65 ± 10 y) either received an intervention with personalized monitoring and feedback aiming to consume ∼250-300 g nitrate-rich vegetables/d (∼350-400 mg nitrate/d; n = 25), beetroot juice supplementation (400 mg nitrate/d; n = 26), or no intervention (control; n = 26). Before and after intervention, 24-h ambulatory BP was measured. Data were analyzed using repeated measures ANOVA (time × treatment), followed by within-group (paired t-test) and between-group analyses (1-factor ANOVA) where appropriate.

Results: The 24-h systolic BP (SBP) (primary outcome) changed significantly (P-interaction time × treatment = 0.017) with an increase in the control group (131 ± 8 compared with 135 ± 10 mmHg; P = 0.036); a strong tendency for a decline in the nitrate-rich vegetable group (129 ± 10 compared with 126 ± 9 mmHg; P = 0.051) which was different from control (P = 0.020); but no change in the beetroot juice group (133 ± 11 compared with 132 ± 12 mmHg; P = 0.56). A significant time × treatment interaction was also found for daytime SBP (secondary outcome, P = 0.011), with a significant decline in the nitrate-rich vegetable group (134 ± 10 compared with 129 ± 9 mmHg; P = 0.006) which was different from control (P = 0.010); but no changes in the beetroot juice (138 ± 12 compared with 137 ± 14 mmHg; P = 0.41) and control group (136 ± 10 compared with 137 ± 11 mmHg; P = 0.08). Diastolic BP (secondary outcome) did not change in any of the groups.

Conclusions: A prolonged dietary intervention focusing on high-nitrate vegetable intake is an effective strategy to lower SBP in (pre)hypertensive middle-aged and older adults. This trial was registered at www.trialregister.nl as NL7814.
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http://dx.doi.org/10.1093/jn/nxab157DOI Listing
September 2021

Undeclared Doping Substances are Highly Prevalent in Commercial Sports Nutrition Supplements.

J Sports Sci Med 2021 06 22;20(2):328-338. Epub 2021 Mar 22.

Doping Authority Netherlands, PO Box 5000, 2900 EA Capelle aan den IJssel, The Netherlands.

Sports nutrition supplements have previously been reported to contain undeclared doping substances. The use of such supplements can lead to general health risks and may give rise to unintentional doping violations in elite sports. To assess the prevalence of doping substances in a range of high-risk sports nutrition supplements available from Dutch web shops. A total of 66 sports nutrition supplements - identified as potentially high-risk products claiming to modulate hormone regulation, stimulate muscle mass gain, increase fat loss, and/or boost energy - were selected from 21 different brands and purchased from 17 web shops. All products were analyzed for doping substances by the UK life sciences testing company LGC, formerly known as the Laboratory of the Government Chemist, using an extended version of their ISO17025 accredited nutritional supplement screen. A total of 25 out of the 66 products (38%) contained undeclared doping substances, which included high levels of the stimulants oxilofrine, β-methylphenethylamine (BMPEA) and N,β-dimethylphenethylamine (NBDMPEA), the stimulant 4-methylhexan-2-amine (methylhexaneamine, 1,3-dimethylamylamine, DMAA), the anabolic steroids boldione (1,4-androstadiene-3,17-dione) and 5-androstene-3β,17α-diol (17α-AED), the beta-2 agonist higenamine and the beta-blocker bisoprolol. Based upon the recommended dose and the potential variability of analyte concentration, the ingestion of some products identified within this study could pose a significant risk of unintentional doping violations. In addition to inadvertent doping risks, the prescribed use of 3 products (4.5%) could likely impose general health risks.
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http://dx.doi.org/10.52082/jssm.2021.328DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8219275PMC
June 2021

Last Word on Viewpoint: Fragile bones of elite cyclists: to treat or not to treat?

J Appl Physiol (1985) 2021 07;131(1):34-35

School of Sport and Exercise, HAN University of Applied Sciences, Nijmegen, The Netherlands.

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http://dx.doi.org/10.1152/japplphysiol.00375.2021DOI Listing
July 2021

Mass spectrometry imaging of L-[ring-C]-labeled phenylalanine and tyrosine kinetics in non-small cell lung carcinoma.

Cancer Metab 2021 Jun 11;9(1):26. Epub 2021 Jun 11.

Maastricht MultiModal Molecular Imaging institute (M4I), Maastricht University, Universiteitssingel 50, 6229 ER, Maastricht, The Netherlands.

Background: Metabolic reprogramming is a common phenomenon in tumorigenesis and tumor progression. Amino acids are important mediators in cancer metabolism, and their kinetics in tumor tissue are far from being understood completely. Mass spectrometry imaging is capable to spatiotemporally trace important endogenous metabolites in biological tissue specimens. In this research, we studied L-[ring-C]-labeled phenylalanine and tyrosine kinetics in a human non-small cell lung carcinoma (NSCLC) xenografted mouse model using matrix-assisted laser desorption/ionization Fourier-transform ion cyclotron resonance mass spectrometry imaging (MALDI-FTICR-MSI).

Methods: We investigated the L-[ring-C]-Phenylalanine (C-Phe) and L-[ring-C]-Tyrosine (C-Tyr) kinetics at 10 min (n = 4), 30 min (n = 3), and 60 min (n = 4) after tracer injection and sham-treated group (n = 3) at 10 min in mouse-xenograft lung tumor tissues by MALDI-FTICR-MSI.

Results: The dynamic changes in the spatial distributions of 19 out of 20 standard amino acids are observed in the tumor tissue. The highest abundance of C-Phe was detected in tumor tissue at 10 min after tracer injection and decreased progressively over time. The overall enrichment of C-Tyr showed a delayed temporal trend compared to C-Phe in tumor caused by the Phe-to-Tyr conversion process. Specifically, C-Phe and C-Tyr showed higher abundances in viable tumor regions compared to non-viable regions.

Conclusions: We demonstrated the spatiotemporal intra-tumoral distribution of the essential aromatic amino acid C-Phe and its de-novo synthesized metabolite C-Tyr by MALDI-FTICR-MSI. Our results explore for the first time local phenylalanine metabolism in the context of cancer tissue morphology. This opens a new way to understand amino acid metabolism within the tumor and its microenvironment.
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http://dx.doi.org/10.1186/s40170-021-00262-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8193875PMC
June 2021

Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial.

Am J Clin Nutr 2021 09;114(3):934-944

Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+, Maastricht, The Netherlands.

Background: Insects have recently been identified as a more sustainable protein-dense food source and may represent a viable alternative to conventional animal-derived proteins.

Objectives: We aimed to compare the impacts of ingesting lesser mealworm- and milk-derived protein on protein digestion and amino acid absorption kinetics, postprandial skeletal muscle protein synthesis rates, and the incorporation of dietary protein-derived amino acids into de novo muscle protein at rest and during recovery from exercise in vivo in humans.

Methods: In this double-blind randomized controlled trial, 24 healthy, young men ingested 30 g specifically produced, intrinsically l-[1-13C]-phenylalanine and l-[1-13C]-leucine labeled lesser mealworm- or milk-derived protein after a unilateral bout of resistance-type exercise. Primed continuous l-[ring-2H5]-phenylalanine, l-[ring-3,5-2H2]-tyrosine, and l-[1-13C]-leucine infusions were applied, with frequent collection of blood and muscle tissue samples.

Results: A total of 73% ± 7% and 77% ± 7% of the lesser mealworm and milk protein-derived phenylalanine was released into the circulation during the 5 h postprandial period, respectively, with no significant differences between groups (P < 0.05). Muscle protein synthesis rates increased after both lesser mealworm and milk protein concentrate ingestion from 0.025 ± 0.008%/h to 0.045 ± 0.017%/h and 0.028 ± 0.010%/h to 0.056 ± 0.012%/h at rest and from 0.025 ± 0.012%/h to 0.059 ± 0.015%/h and 0.026 ± 0.009%/h to 0.073 ± 0.020%/h after exercise, respectively (all P < 0.05), with no differences between groups (both P > 0.05). Incorporation of mealworm and milk protein-derived l-[1-13C]-phenylalanine into de novo muscle protein was greater after exercise than at rest (P < 0.05), with no differences between groups (P > 0.05).

Conclusions: Ingestion of a meal-like amount of lesser mealworm-derived protein is followed by rapid protein digestion and amino acid absorption and increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial protein handling of lesser mealworm does not differ from ingesting an equivalent amount of milk protein concentrate in vivo in humans.This trial was registered at www.trialregister.nl as NL6897.
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http://dx.doi.org/10.1093/ajcn/nqab115DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8408844PMC
September 2021

Basal protein synthesis rates differ between vastus lateralis and rectus abdominis muscle.

J Cachexia Sarcopenia Muscle 2021 06 5;12(3):769-778. Epub 2021 May 5.

Department of Human Biology, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+, Maastricht, The Netherlands.

Background: In vivo muscle protein synthesis rates are typically assessed by measuring the incorporation rate of stable isotope labelled amino acids in skeletal muscle tissue collected from vastus lateralis muscle. It remains to be established whether muscle protein synthesis rates in the vastus lateralis are representative of muscle protein synthesis rates of other muscle groups. We hypothesized that post-absorptive muscle protein synthesis rates differ between vastus lateralis and rectus abdominis, pectoralis major, or temporalis muscle in vivo in humans.

Methods: Twenty-four patients (62 ± 3 years, 42% female), scheduled to undergo surgery, participated in this study and underwent primed continuous intravenous infusions with l-[ring- C ]-phenylalanine. During the surgical procedures, serum samples were collected, and muscle tissue was obtained from the vastus lateralis as well as from the rectus abdominis, pectoralis major, or temporalis muscle. Fractional mixed muscle protein synthesis rates (%/h) were assessed by measuring the incorporation of l-[ring- C ]-phenylalanine into muscle tissue protein.

Results: Serum l-[ring- C ]-phenylalanine enrichments did not change throughout the infusion period. Post-absorptive muscle protein synthesis rates calculated based upon serum l-[ring- C ]-phenylalanine enrichments did not differ between vastus lateralis and rectus abdominis (0.032 ± 0.004 vs. 0.038 ± 0.003%/h), vastus lateralis and pectoralis major, (0.025 ± 0.003 vs. 0.022 ± 0.005%/h) or vastus lateralis and temporalis (0.047 ± 0.005 vs. 0.043 ± 0.005%/h) muscle, respectively (P > 0.05). When fractional muscle protein synthesis rates were calculated based upon tissue-free l-[ring- C ]-phenylalanine enrichments as the preferred precursor pool, muscle protein synthesis rates were significantly higher in rectus abdominis (0.089 ± 0.008%/h) compared with vastus lateralis (0.054 ± 0.005%/h) muscle (P < 0.01). No differences were observed between fractional muscle protein synthesis rates in vastus lateralis and pectoralis major (0.046 ± 0.003 vs. 0.041 ± 0.008%/h) or vastus lateralis and temporalis (0.073 ± 0.008 vs. 0.083 ± 0.011%/h) muscle, respectively.

Conclusions: Post-absorptive muscle protein synthesis rates are higher in rectus abdominis when compared with vastus lateralis muscle. Post-absorptive muscle protein synthesis rates do not differ between vastus lateralis and pectoralis major or temporalis muscle. Protein synthesis rates in muscle tissue samples obtained during surgery do not necessarily represent a good proxy for appendicular skeletal muscle protein synthesis rates.
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http://dx.doi.org/10.1002/jcsm.12701DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8200451PMC
June 2021

Does supplementation with leucine-enriched protein alone and in combination with fish-oil-derived n-3 PUFA affect muscle mass, strength, physical performance, and muscle protein synthesis in well-nourished older adults? A randomized, double-blind, placebo-controlled trial.

Am J Clin Nutr 2021 06;113(6):1411-1427

School of Public Health, Physiotherapy and Sport Science, University College Dublin, Dublin, Ireland.

Background: Leucine-enriched protein (LEU-PRO) and long-chain (LC) n-3 (ω-3) PUFAs have each been proposed to improve muscle mass and function in older adults, whereas their combination may be more effective than either alone.

Objective: The impact of LEU-PRO supplementation alone and combined with LC n-3 PUFAs on appendicular lean mass, strength, physical performance and myofibrillar protein synthesis (MyoPS) was investigated in older adults at risk of sarcopenia.

Methods: This 24-wk, 3-arm parallel, randomized, double-blind, placebo-controlled trial was conducted in 107 men and women aged ≥65 y with low muscle mass and/or strength. Twice daily, participants consumed a supplement containing either LEU-PRO (3 g leucine, 10 g protein; n = 38), LEU-PRO plus LC n-3 PUFAs (0.8 g EPA, 1.1 g DHA; LEU-PRO+n-3; n = 38), or an isoenergetic control (CON; n = 31). Appendicular lean mass, handgrip strength, leg strength, physical performance, and circulating metabolic and renal function markers were measured pre-, mid-, and postintervention. Integrated rates of MyoPS were assessed in a subcohort (n = 28).

Results: Neither LEU-PRO nor LEU-PRO+n-3 supplementation affected appendicular lean mass, handgrip strength, knee extension strength, physical performance or MyoPS. However, isometric knee flexion peak torque (treatment effect: -7.1 Nm; 95% CI: -12.5, -1.8 Nm; P < 0.01) was lower postsupplementation in LEU-PRO+n-3 compared with CON. Serum triacylglycerol and total adiponectin concentrations were lower, and HOMA-IR was higher, in LEU-PRO+n-3 compared with CON postsupplementation (all P < 0.05). Estimated glomerular filtration rate was higher and cystatin c was lower in LEU-PRO and LEU-PRO+n-3 postsupplementation compared with CON (all P < 0.05).

Conclusions: Contrary to our hypothesis, we did not observe a beneficial effect of LEU-PRO supplementation alone or combined with LC n-3 PUFA supplementation on appendicular lean mass, strength, physical performance or MyoPS in older adults at risk of sarcopenia. This trial was registered at clinicaltrials.gov as NCT03429491.
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http://dx.doi.org/10.1093/ajcn/nqaa449DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8168361PMC
June 2021

Fragile bones of elite cyclists: to treat or not to treat?

J Appl Physiol (1985) 2021 Mar 11. Epub 2021 Mar 11.

School of Sport and Exercise, HAN University of Applied Sciences, Netherlands.

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http://dx.doi.org/10.1152/japplphysiol.01034.2020DOI Listing
March 2021

Daily Myofibrillar Protein Synthesis Rates in Response to Low- and High-Frequency Resistance Exercise Training in Healthy, Young Men.

Int J Sport Nutr Exerc Metab 2021 Feb 17;31(3):209-216. Epub 2021 Feb 17.

University of Birmingham.

The impact of resistance exercise frequency on muscle protein synthesis rates remains unknown. The aim of this study was to compare daily myofibrillar protein synthesis rates over a 7-day period of low-frequency (LF) versus high-frequency (HF) resistance exercise training. Nine young men (21 ± 2 years) completed a 7-day period of habitual physical activity (BASAL). This was followed by a 7-day exercise period of volume-matched, LF (10 × 10 repetitions at 70% one-repetition maximum, once per week) or HF (2 × 10 repetitions at ∼70% one-repetition maximum, five times per week) resistance exercise training. The participants had one leg randomly allocated to LF and the other to HF. Skeletal muscle biopsies and daily saliva samples were collected to determine myofibrillar protein synthesis rates using 2H2O, with intracellular signaling determined using Western blotting. The myofibrillar protein synthesis rates did not differ between the LF (1.46 ± 0.26%/day) and HF (1.48 ± 0.33%/day) conditions over the 7-day exercise training period (p > .05). There were no significant differences between the LF and HF conditions over the first 2 days (1.45 ± 0.41%/day vs. 1.25 ± 0.46%/day) or last 5 days (1.47 ± 0.30%/day vs. 1.50 ± 0.41%/day) of the exercise training period (p > .05). Daily myofibrillar protein synthesis rates were not different from BASAL at any time point during LF or HF (p > .05). The phosphorylation status and total protein content of selected proteins implicated in skeletal muscle ribosomal biogenesis were not different between conditions (p > .05). Under the conditions of the present study, resistance exercise training frequency did not modulate daily myofibrillar protein synthesis rates in young men.
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http://dx.doi.org/10.1123/ijsnem.2020-0274DOI Listing
February 2021

No differences in muscle protein synthesis rates following ingestion of wheat protein, milk protein, and their protein blend in healthy, young males.

Br J Nutr 2021 Dec 18;126(12):1832-1842. Epub 2021 Feb 18.

TiFN, Wageningen, The Netherlands.

Plant-derived proteins have been suggested to have less anabolic properties when compared with animal-derived proteins. Whether blends of plant- and animal-derived proteins can compensate for their lesser anabolic potential has not been assessed. The present study compares post-prandial muscle protein synthesis rates following the ingestion of milk protein with wheat protein or a blend of wheat plus milk protein in healthy, young males. In a randomised, double-blind, parallel-group design, 36 males (23 (sd 3) years) received a primed continuous L-[ring-13C6]-phenylalanine infusion after which they ingested 30 g milk protein (MILK), 30 g wheat protein (WHEAT) or a 30 g blend combining 15 g wheat plus 15 g milk protein (WHEAT+MILK). Blood and muscle biopsies were collected frequently for 5 h to assess post-prandial plasma amino acid profiles and subsequent myofibrillar protein synthesis rates. Ingestion of protein increased myofibrillar protein synthesis rates in all treatments (P < 0·001). Post-prandial myofibrillar protein synthesis rates did not differ between MILK v. WHEAT (0·053 (sd 0·013) v. 0·056 (sd 0·012) %·h-1, respectively; t test P = 0·56) or between MILK v. WHEAT+MILK (0·053 (sd 0·013) v. 0·059 (sd 0·025) %·h-1, respectively; t test P = 0·46). In conclusion, ingestion of 30 g milk protein, 30 g wheat protein or a blend of 15 g wheat plus 15 g milk protein increases muscle protein synthesis rates in young males. Furthermore, muscle protein synthesis rates following the ingestion of 30 g milk protein do not differ from rates observed after ingesting 30 g wheat protein or a blend with 15 g milk plus 15 g wheat protein in healthy, young males.
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http://dx.doi.org/10.1017/S0007114521000635DOI Listing
December 2021

Exercise Plus Presleep Protein Ingestion Increases Overnight Muscle Connective Tissue Protein Synthesis Rates in Healthy Older Men.

Int J Sport Nutr Exerc Metab 2021 Feb 14;31(3):217-226. Epub 2021 Feb 14.

Maastricht University Medical Centre.

Protein ingestion and exercise stimulate myofibrillar protein synthesis rates. When combined, exercise further increases the postprandial rise in myofibrillar protein synthesis rates. It remains unclear whether protein ingestion with or without exercise also stimulates muscle connective tissue protein synthesis rates. The authors assessed the impact of presleep protein ingestion on overnight muscle connective tissue protein synthesis rates at rest and during recovery from resistance-type exercise in older men. Thirty-six healthy, older men were randomly assigned to ingest 40 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine-labeled casein protein (PRO, n = 12) or a nonprotein placebo (PLA, n = 12) before going to sleep. A third group performed a single bout of resistance-type exercise in the evening before ingesting 40 g intrinsically-labeled casein protein prior to sleep (EX+PRO, n = 12). Continuous intravenous infusions of L-[ring-2H5]-phenylalanine and L-[1-13C]-leucine were applied with blood and muscle tissue samples collected throughout overnight sleep. Presleep protein ingestion did not increase muscle connective tissue protein synthesis rates (0.049 ± 0.013 vs. 0.060 ± 0.024%/hr in PLA and PRO, respectively; p = .73). Exercise plus protein ingestion resulted in greater overnight muscle connective tissue protein synthesis rates (0.095 ± 0.022%/hr) when compared with PLA and PRO (p < .01). Exercise increased the incorporation of dietary protein-derived amino acids into muscle connective tissue protein (0.036 ± 0.013 vs. 0.054 ± 0.009 mole percent excess in PRO vs. EX+PRO, respectively; p < .01). In conclusion, resistance-type exercise plus presleep protein ingestion increases overnight muscle connective tissue protein synthesis rates in older men. Exercise enhances the utilization of dietary protein-derived amino acids as precursors for de novo muscle connective tissue protein synthesis during overnight sleep.
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http://dx.doi.org/10.1123/ijsnem.2020-0222DOI Listing
February 2021

Comprehensive assessment of post-prandial protein handling by the application of intrinsically labelled protein in human subjects.

Proc Nutr Soc 2021 05 25;80(2):221-229. Epub 2021 Jan 25.

NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre, Maastricht, the Netherlands.

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.
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http://dx.doi.org/10.1017/S0029665120008034DOI Listing
May 2021

Assessing the whole-body protein synthetic response to feeding in human subjects.

Proc Nutr Soc 2021 05 5;80(2):139-147. Epub 2021 Jan 5.

NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre, Maastricht, the Netherlands.

All tissues are in a constant state of turnover, with a tightly controlled regulation of protein synthesis and breakdown rates. Due to the relative ease of sampling skeletal muscle tissue, basal muscle protein synthesis rates and the protein synthetic responses to various anabolic stimuli have been well defined in human subjects. In contrast, only limited data are available on tissue protein synthesis rates in other organs. Several organs such as the brain, liver and pancreas, show substantially higher (basal) protein synthesis rates when compared to skeletal muscle tissue. Such data suggest that these tissues may also possess a high level of plasticity. It remains to be determined whether protein synthesis rates in these tissues can be modulated by external stimuli. Whole-body protein synthesis rates are highly responsive to protein intake. As the contribution of muscle protein synthesis rates to whole-body protein synthesis rates is relatively small considering the large amount of muscle mass, this suggests that other organ tissues may also be responsive to (protein) feeding. Whole-body protein synthesis rates in the fasted or fed state can be quantified by measuring plasma amino acid kinetics, although this requires the production of intrinsically labelled protein. Protein intake requirements to maximise whole-body protein synthesis may also be determined by the indicator amino acid oxidation technique, but the technique does not allow the assessment of actual protein synthesis and breakdown rates. Both approaches have several other methodological and inferential limitations that will be discussed in detail in this paper.
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http://dx.doi.org/10.1017/S0029665120008009DOI Listing
May 2021

Myonuclear content and domain size in small versus larger muscle fibres in response to 12 weeks of resistance exercise training in older adults.

Acta Physiol (Oxf) 2021 04 20;231(4):e13599. Epub 2020 Dec 20.

Human Biology, School of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University, Maastricht, The Netherlands.

Aim: To assess the relation between muscle fibre hypertrophy and myonuclear accretion in relatively small and large muscle fibre size clusters following prolonged resistance exercise training in older adults.

Methods: Muscle biopsies were collected before and after 12 weeks of resistance exercise training in 40 healthy, older men (70 ± 3 years). All muscle fibres were ordered by size and categorized in four muscle fibre size clusters: 'Small': 2000-3999 µm , 'Moderate': 4000-5999 µm , 'Large': 6000-7999 µm and 'Largest': 8000-9999 µm . Changes in muscle fibre size cluster distribution were related to changes in muscle fibre size, myonuclear content and myonuclear domain size.

Results: With training, the percentage of muscle fibres decreased in the Small (from 23 ± 12 to 17 ± 14%, P < .01) and increased in the Largest (from 11 ± 8 to 15 ± 10%, P < .01) muscle fibre size clusters. The decline in the percentage of Small muscle fibres was accompanied by an increase in overall myonuclear domain size (r = -.466, P = .002) and myonuclear content (r = -.390, P = .013). In contrast, the increase in the percentage of the Largest muscle fibres was accompanied by an overall increase in myonuclear content (r = .616, P < .001), but not in domain size.

Conclusion: Prolonged resistance-type exercise training induces a decline in the percentage of small as well as an increase in the percentage of the largest muscle fibres in older adults. Whereas the change in the percentage of small fibres is best predicted by an increase in overall myonuclear domain size, the change in the percentage of the largest fibres is associated with an overall increase in myonuclear content.
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http://dx.doi.org/10.1111/apha.13599DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8047909PMC
April 2021

Dietary protein interventions to improve nutritional status in end-stage renal disease patients undergoing hemodialysis.

Curr Opin Clin Nutr Metab Care 2021 01;24(1):79-87

Department of Human Biology.

Purpose Of Review: Poor nutritional status is prevalent among end-stage renal disease patients undergoing hemodialysis. Chronic hemodialysis patients show an accelerated decline in skeletal muscle mass and strength, which is associated with higher mortality rates and a reduced quality of life. The current review aims to summarize recent advances regarding underlying causes of muscle loss and interventions that support muscle mass maintenance in patients with chronic hemodialysis.

Recent Findings: Muscle maintenance in chronic hemodialysis patients is compromised by low dietary protein intake levels, anabolic resistance of skeletal muscle tissue, sedentary behavior, and amino acid removal during hemodialysis. Studies assessing the effect of increased protein intake on nutritional status generally show beneficial results, especially in hypoalbuminemic chronic hemodialysis patients. The muscle protein synthetic response following protein ingestion in chronic hemodialysis patients may be enhanced through incorporation of structured physical activity and/or concurrent ketoacid ingestion.

Summary: A coordinated program that combines nutritional and physical activity interventions is likely required to attenuate the decline in muscle mass and strength of chronic hemodialysis patients. Nephrologists, dieticians, and exercise specialists should collaborate closely to establish guidelines regarding the appropriate quantity and timing of protein ingestion. In addition, they should provide tailored nutritional and physical activity interventions for chronic hemodialysis patients (see video, Supplemental Digital Content 1, Video abstract, http://links.lww.com/COCN/A14).
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http://dx.doi.org/10.1097/MCO.0000000000000703DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7752218PMC
January 2021

Whey protein supplementation does not accelerate recovery from a single bout of eccentric exercise.

J Sports Sci 2021 Feb 5;39(3):322-331. Epub 2020 Oct 5.

Institute of Sports and Exercise Studies, HAN University of Applied Sciences , Nijmegen, The Netherlands.

The current double blind, randomized, placebo-controlled trial with two parallel groups aimed to assess the impact of whey protein supplementation on recovery of muscle function and muscle soreness following eccentric exercise. During a 9-day period, forty recreationally active males received twice daily supplementation with either whey protein (PRO; 60 g/day) or an iso-energetic amount of carbohydrate (CON). Muscle function and soreness were assessed before, and 0, 3, 24, 48, and 72 h after performing 100 drop jumps. Recovery of isometric maximal voluntary contraction (MVC) did not significantly differ between groups (timextreatment, = 0.56). In contrast, the recovery of isokinetic MVC at 90°·s was faster in CON as opposed to PRO (timextreatment interaction, = 0.044). Recovery of isokinetic MVC at 180°·s was also faster in CON as opposed to PRO (timextreatment interaction, = 0.011). Recovery of countermovement jump performance did not differ between groups (timextreatment interaction, = 0.52). Muscle soreness, CK and CRP showed a transient increase over time ( < 0.001), with no differences between groups. In conclusion, whey protein supplementation does not accelerate recovery of muscle function or attenuate muscle soreness and inflammation during 3 days of recovery from a single bout of eccentric exercise.
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http://dx.doi.org/10.1080/02640414.2020.1820184DOI Listing
February 2021

Primary, Secondary, and Tertiary Effects of Carbohydrate Ingestion During Exercise.

Sports Med 2020 11;50(11):1863-1871

School of Sports Exercise and Health Sciences, Loughborough University, Loughborough, UK.

The purpose of this current opinion paper is to describe the journey of ingested carbohydrate from 'mouth to mitochondria' culminating in energy production in skeletal muscles during exercise. This journey is conveniently described as primary, secondary, and tertiary events. The primary stage is detection of ingested carbohydrate by receptors in the oral cavity and on the tongue that activate reward and other centers in the brain leading to insulin secretion. After digestion, the secondary stage is the transport of monosaccharides from the small intestine into the systemic circulation. The passage of these monosaccharides is facilitated by the presence of various transport proteins. The intestinal mucosa has carbohydrate sensors that stimulate the release of two 'incretin' hormones (GIP and GLP-1) whose actions range from the secretion of insulin to appetite regulation. Most of the ingested carbohydrate is taken up by the liver resulting in a transient inhibition of hepatic glucose release in a dose-dependent manner. Nonetheless, the subsequent increased hepatic glucose (and lactate) output can increase exogenous carbohydrate oxidation rates by 40-50%. The recognition and successful distribution of carbohydrate to the brain and skeletal muscles to maintain carbohydrate oxidation as well as prevent hypoglycaemia underpins the mechanisms to improve exercise performance.
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http://dx.doi.org/10.1007/s40279-020-01343-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8159838PMC
November 2020

Casein Protein Processing Strongly Modulates Post-Prandial Plasma Amino Acid Responses In Vivo in Humans.

Nutrients 2020 Jul 31;12(8). Epub 2020 Jul 31.

NUTRIM School of Nutrition and Translation Research in Metabolism, Maastricht University Medical Centre, P.O. Box 616, 6200 MD Maastricht, The Netherlands.

Micellar casein is characterized as a slowly digestible protein source, and its structure can be modulated by various food processing techniques to modify its functional properties. However, little is known about the impact of such modifications on casein protein digestion and amino acid absorption kinetics and the subsequent post-prandial plasma amino acid responses. In the present study, we determined post-prandial aminoacidemia following ingestion of isonitrogenous amounts of casein protein (40 g) provided as micellar casein (Mi-CAS), calcium caseinate (Ca-CAS), or cross-linked sodium caseinate (XL-CAS). Fifteen healthy, young men (age: 26 ± 4 years, BMI: 23 ± 1 kg·m) participated in this randomized cross-over study and ingested 40 g Mi-Cas, Ca-CAS, and XL-CAS protein, with a ~1 week washout between treatments. On each trial day, arterialized 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 amino acid concentrations were higher following the ingestion of XL-CAS when compared to Mi-CAS and Ca-CAS from t = 15 to 90 min (all < 0.05). Plasma amino acid concentrations were higher following ingestion of Mi-CAS compared to Ca-CAS from t = 30 to 45 min (both < 0.05). Plasma total amino acids iAUC were higher following the ingestion of XL-CAS when compared to Ca-CAS (294 ± 63 vs. 260 ± 75 mmol·L, = 0.006), with intermediate values following Mi-CAS ingestion (270 ± 63 mmol·L, > 0.05). In conclusion, cross-linked sodium caseinate is more rapidly digested when compared to micellar casein and calcium caseinate. Protein processing can strongly modulate the post-prandial rise in plasma amino acid bioavailability in vivo in humans.
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http://dx.doi.org/10.3390/nu12082299DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7468913PMC
July 2020

In vitro ketone-supported mitochondrial respiration is minimal when other substrates are readily available in cardiac and skeletal muscle.

J Physiol 2020 11 19;598(21):4869-4885. Epub 2020 Aug 19.

Department of Human Health and Nutritional Science, University of Guelph, Guelph, Ontario, Canada.

Key Points: Ketone bodies are proposed to represent an alternative fuel source driving energy production, particularly during exercise. Biologically, the extent to which mitochondria utilize ketone bodies compared to other substrates remains unknown. We demonstrate in vitro that maximal mitochondrial respiration supported by ketone bodies is low when compared to carbohydrate-derived substrates in the left ventricle and red gastrocnemius muscle from rodents, and in human skeletal muscle. When considering intramuscular concentrations of ketone bodies and the presence of other carbohydrate and lipid substrates, biological rates of mitochondrial respiration supported by ketone bodies are predicted to be minimal. At the mitochondrial level, it is therefore unlikely that ketone bodies are an important source for energy production in cardiac and skeletal muscle, particularly when other substrates are readily available.

Abstract: Ketone bodies (KB) have recently gained popularity as an alternative fuel source to support mitochondrial oxidative phosphorylation and enhance exercise performance. However, given the low activity of ketolytic enzymes and potential inhibition from carbohydrate oxidation, it remains unknown if KBs can contribute to energy production. We therefore determined the ability of KBs (sodium dl-β-hydroxybutyrate, β-HB; lithium acetoacetate, AcAc) to stimulate in vitro mitochondrial respiration in the left ventricle (LV) and red gastrocnemius (RG) of rats, and in human vastus lateralis. Compared to pyruvate, the ability of KBs to maximally drive respiration was low in isolated mitochondria and permeabilized fibres (PmFb) from the LV (∼30-35% of pyruvate), RG (∼10-30%), and human vastus lateralis (∼2-10%). In PmFb, the concentration of KBs required to half-maximally drive respiration (LV: 889 µm β-HB, 801 µm AcAc; RG: 782 µm β-HB, 267 µm AcAc) were greater than KB content representative of the muscle microenvironment (∼100 µm). This would predict low rates (∼1-4% of pyruvate) of biological KB-supported respiration in the LV (8-14 pmol s mg ) and RG (3-6 pmol s mg ) at rest and following exercise. Moreover, KBs did not increase respiration in the presence of saturating pyruvate, submaximal pyruvate (100 µm) reduced the ability of physiological β-HB to drive respiration, and addition of other intracellular substrates (succinate + palmitoylcarnitine) decreased maximal KB-supported respiration. As a result, product inhibition is likely to limit KB oxidation. Altogether, the ability of KBs to drive mitochondrial respiration is minimal and they are likely to be outcompeted by other substrates, compromising their use as an important energy source.
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http://dx.doi.org/10.1113/JP280032DOI Listing
November 2020
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