Coingestion of Collagen With Whey Protein Prevents Postexercise Decline in Plasma Glycine Availability in Recreationally Active Men.

Whey protein ingestion during recovery from exercise increases myofibrillar but not muscle connective protein synthesis rates. It has been speculated that whey protein does not provide sufficient glycine to maximize postexercise muscle connective protein synthesis rates. In the present study, we assessed the impact of coingesting different amounts of collagen with whey protein as a nutritional strategy to increase plasma glycine availability during recovery from exercise. In a randomized, double-blind, crossover design, 14 recreationally active men (age: 26 ± 5 years; body mass index: 23.8 ± 2.1 kg·m-2) ingested in total 30 g protein, provided as whey protein with 0 g (WHEY), 5 g (WC05); 10 g (WC10), and 15 g (WC15) of collagen protein immediately after a single bout of resistance exercise. Blood samples were collected frequently over 6 hr of postexercise recovery to assess postprandial plasma amino acid kinetics and availability. Protein ingestion strongly increased plasma amino acid concentrations (p < .001) with no differences in plasma total amino acid availability between treatments (p > .05). The postprandial rise in plasma leucine and essential amino acid availability was greater in WHEY compared with the WC10 and WC15 treatments (p < .05). Plasma glycine and nonessential amino acid concentrations declined following whey protein ingestion but increased following collagen coingestion (p < .05). Postprandial plasma glycine availability averaged -8.9 ± 5.8, 9.2 ± 3.7, 23.1 ± 6.5, and 39.8 ± 11.0 mmol·360 min/L in WHEY, WC05, WC10, and WC15, respectively (incremental area under curve values, p < .05). Coingestion of a small amount of collagen (5 g) with whey protein (25 g) is sufficient to prevent the decline in plasma glycine availability during recovery from lower body resistance-type exercise in recreationally active men.

Access to a pre-sleep protein snack increases daily energy and protein intake in surgical hospitalized patients.

BACKGROUND & AIM: In hospitalized patients, daily protein intake remains far below WHO requirements for healthy adults (0.8 g·kg-1·d-1) as well as ESPEN guidelines for patients (1.2-1.5 g·kg-1·d-1). Providing access to a pre-sleep protein dense snack between dinner and going to bed may serve as a great opportunity to increase daily energy and protein intake in hospitalized patients. However, it remains to be assessed whether protein provision prior to sleep effectively increases protein intake, or may reduce food intake throughout the remainder of the day(s). The present study evaluated the impact of giving access to a pre-sleep snack on daily energy and protein intake in patients throughout their hospitalization. METHODS: Patients admitted to the surgical wards of the Maastricht University Medical Centre+ were randomly allocated to usual care (n = 51) or given access to a pre-sleep snack (n = 50). The pre-sleep snack consisted of 103 g cheese cubes (30 g protein) provided between 7:30 and 9:30 PM, prior to sleep. All food provided and all food consumed was weighed and recorded throughout (2-7 days) hospitalization. Daily energy and protein intake and distribution were calculated. Data were analyzed by independent T-Tests with P < 0.05 considered as statistically significant. RESULTS: Daily energy intake was higher in the pre-sleep group (1353 ± 424 kcal d-1) when compared to the usual care group (1190 ± 402 kcal·d-1; P = 0.049). Providing patients access to a pre-sleep snack resulted in a 17% (11 ± 9 g) higher daily protein intake (0.81 ± 0.29 g·kg-1·d-1) when compared to the usual care group (0.69 ± 0.28 g·kg-1·d-1; P = 0.045). Protein intake at breakfast, lunch, and dinner did not differ between the pre-sleep and usual care groups (all P > 0.05). CONCLUSION: Providing access to a pre-sleep protein snack, in the form of protein dense food items such as cheese, represents an effective dietary strategy to increase daily energy and protein intake in hospitalized patients. Patients consuming pre-sleep protein snacks do not compensate by lowering energy or protein intake throughout the remainder of the days. Pre-sleep protein dense food provision should be implemented in hospital food logistics to improve the nutritional intake of patients. TRIAL REGISTER NO: NL8507 (https://trialsearch.who.int/).

Becoming a World Champion Powerlifter at 71 Years of Age: It Is Never Too Late to Start Exercising.

This case study assessed body composition, muscle strength, cardiorespiratory fitness, and metabolic health of the present female world champion powerlifter in the 70+ age category who started resistance exercise training at 63 years of age with no prior experience with structured exercise training. Measures of body composition (magnetic resonance imaging, computed tomography, and dual-energy X-ray absorptiometry scanning, leg volume); strength (one-repetition maximum leg press and extension, maximum voluntary contraction, and handgrip strength); physical function (short physical performance battery); cardiorespiratory fitness (peak oxygen consumption); and metabolic health (oral glucose tolerance test) were assessed. In addition, a muscle biopsy was collected to assess muscle fiber type distribution and cross-sectional area (CSA). Where possible, data were compared with previously (un)published sex- and age-matched data using z scores. Skeletal muscle mass index was calculated by dividing limb muscle mass by height squared. Data from the control groups are expressed as mean ± 95% confidence interval. Our participant (age: 71 years; body mass: 64.5 kg; body mass index: 27.6 kg/m2) reported a good bone mineral density of 1.09 g/cm2 (T score between -1 and +1) and very low values of abdominal and organ body fat (i.e., between 20% and 70% lower compared with a reference group of postmenopausal women). In addition, she showed a 33% greater skeletal muscle mass index when compared with healthy, older female control subjects (7.9 vs. 5.9 [5.7-6.2] kg/m2; n = 61) as well as 37% greater muscle quadriceps CSA (63.8 vs. 46.6 [44.5-48.7] cm2; n = 48) and 46% greater Type II muscle fiber CSA (4,536 vs. 3,097 [2,707-3,488] µm2; n = 19). Absolute leg press muscle strength was 36% greater (190 vs. 140 [132-147] kg; n = 30) and handgrip strength was 33% greater (33 vs. 25 [23-26] kg; n = 48) when compared with healthy, age-matched controls. In conclusion, even for resistance exercise naïve individuals, starting exercise at an advanced age can lead to improvements in body composition and muscle strength allowing older adults to reduce the risk for developing metabolic syndrome, live independently, and even compete at a world class level.

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

Plant-derived proteins are generally believed to possess lesser anabolic properties when compared with animal-derived proteins. This is, at least partly, attributed to the lower leucine content of most plant-derived proteins. Corn protein has a leucine content that is highest among most plant-derived proteins and it even exceeds the levels observed in animal-derived proteins such as whey protein. Therefore, this study aimed to compare muscle protein synthesis rates following the ingestion of 30 g corn protein and a 30 g blend of corn plus milk protein with 30 g milk protein. In a randomized, double blind, parallel-group design, 36 healthy young males (26 ± 4 y) received primed continuous L-[ring-13C6]-phenylalanine infusions and ingested 30 g corn protein (CORN), 30 g milk protein (MILK), or a 30 g proteinblend with 15 g corn plus 15 g milk protein (CORN + MILK). Blood and muscle biopsies were collected for 5 h following protein ingestion to assess post-prandial plasma amino acid profiles and myofibrillar protein synthesis rates. The results show that Ingestion of protein increased myofibrillar protein synthesis rates from basal post-absorptive values in all treatments(P < 0.001). Post-prandial myofibrillar protein synthesis rates did not differ between CORN vs MILK (0.053 ± 0.013 vs 0.053 ± 0.013%∙h-1, respectively; t-test P = 0.90), or between CORN + MILK vs MILK (0.052 ± 0.024 vs 0.053 ± 0.013%∙h-1, respectively; t-test P = 0.92). Ingestion of 30 g corn protein, 30 g milk protein, or a blend of 15 g corn plus 15 g milk protein robustly increases muscle protein synthesis rates in young males. The muscle protein synthetic response to the ingestion of 30 g corn-derived protein does not differ from the ingestion of an equivalent amount of milk protein in healthy, young males. Clinical Trial Registry number. NTR6548 (registration date: 27-06-2017) https://www.trialregister.nl/ .

Daily blood flow restriction does not preserve muscle mass and strength during 2 weeks of bed rest.

We measured the impact of blood flow restriction on muscle protein synthesis rates, muscle mass and strength during 2 weeks of strict bed rest. Twelve healthy, male adults (age: 24 ± 3 years, body mass index: 23.7 ± 3.1 kg/m2 ) were subjected to 14 days of strict bed rest with unilateral blood flow restriction performed three times daily in three 5 min cycles (200 mmHg). Participants consumed deuterium oxide and we collected blood and saliva samples throughout 2 weeks of bed rest. Before and immediately after bed rest, lean body mass (dual-energy X-ray absorptiometry scan) and thigh muscle volume (magnetic resonance imaging scan) were assessed in both the blood flow restricted (BFR) and control (CON) leg. Muscle biopsies were collected and unilateral muscle strength (one-repetition maximum; 1RM) was assessed for both legs before and after the bed rest period. Bed rest resulted in 1.8 ± 1.0 kg lean body mass loss (P < 0.001). Thigh muscle volume declined from 7.1 ± 1.1 to 6.7 ± 1.0 L in CON and from 7.0 ± 1.1 to 6.7 ± 1.0 L in BFR (P < 0.001), with no differences between treatments (P = 0.497). In addition, 1RM leg extension strength decreased from 60.2 ± 10.6 to 54.8 ± 10.9 kg in CON and from 59.2 ± 12.1 to 52.9 ± 12.0 kg in BFR (P = 0.014), with no differences between treatments (P = 0.594). Muscle protein synthesis rates during bed rest did not differ between the BFR and CON leg (1.11 ± 0.12 vs. 1.08 ± 0.13%/day, respectively; P = 0.302). Two weeks of bed rest substantially reduces skeletal muscle mass and strength. Blood flow restriction during bed rest does not modulate daily muscle protein synthesis rates and does not preserve muscle mass or strength. KEY POINTS: Bed rest, often necessary for recovery from illness or injury, leads to the loss of muscle mass and strength. It has been postulated that blood flow restriction may attenuate the loss of muscle mass and strength during bed rest. We investigated the effect of blood flow restriction on muscle protein synthesis rates, muscle mass and strength during 2 weeks of strict bed rest. Blood flow restriction applied during bed rest does not modulate daily muscle protein synthesis rates and does not preserve muscle mass or strength. Blood flow restriction is not effective in preventing muscle atrophy during a prolonged period of bed rest.

Energy Requirements of Paralympic Athletes: Insights from the Doubly Labeled Water Approach.

PURPOSE: Advanced insight in energy requirements of Paralympic athletes is imperative for optimizing their nutritional counseling. Given the lack of accurate data on total daily energy expenditure (TDEE) of Paralympic athletes, this study aimed to assess energy expenditure and nutritional intake of a large cohort of Paralympic athletes, across different sports and disabilities. METHODS: In this cross-sectional study, 48 Dutch and Norwegian Paralympic athletes (19 male/29 female) with various disabilities, competing in Para cycling, wheelchair tennis, wheelchair basketball, Para Nordic skiing, and alpine skiing participated. TDEE was assessed by the gold standard doubly labeled water method over a 14-d period, resting metabolic rate by ventilated hood indirect calorimetry, energy intake by three unannounced 24-h dietary recalls, body composition by dual-energy x-ray absorptiometry, and exercise training duration by a training log. RESULTS: Mean TDEE was 2908 ± 797 kcal·d -1 , ranging from 2322 ± 340 kcal·d -1 for wheelchair basketball players to 3607 ± 1001 kcal·d -1 for Para cyclists. Regression analysis identified fat-free mass, exercise duration, and the presence of a spinal cord disorder as the primary predictors of TDEE, explaining up to 73% of the variance in TDEE. Athletes' energy intake (2363 ± 905 kcal·d -1 ) was below their TDEE, whereas their body mass remained constant, indicating underreporting. Carbohydrate intake (4.1 ± 1.9 g·kg -1 body mass) was low, even when considering underreporting, whereas protein intake (1.8 ± 0.6 g·kg -1 body mass) was relatively high. CONCLUSIONS: Paralympic athletes display moderate- to high-energy expenditure, varying across sports and individuals. Much of the variation in TDEE can be attributed to individual differences in fat-free mass and exercise duration. This study establishes the benchmarks for energy requirements of Paralympic athletes, serving as the foundation for future dietary guidelines within this population.

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.

PURPOSE: Plant-derived proteins have received considerable attention as an alternative to animal-derived proteins. However, plant-derived proteins are considered to have less anabolic properties when compared with animal-derived proteins. The lower muscle protein synthesis rates following ingestion of plant- compared with animal-derived protein have been attributed to the lower essential amino acid content of plant-derived proteins and/or their specific amino acid deficiencies. This study aimed to compare post-prandial muscle protein synthesis rates following the ingestion of 30 g pea-derived protein with 30 g milk-derived protein in healthy, young males. METHODS: In a randomized, double-blind, parallel-group design, 24 young males (24 ± 3 y) received a primed continuous L-[ring-13C6]-phenylalanine infusion after which they ingested 30 g pea (PEA) or 30 g milk-derived protein (MILK). Blood and muscle biopsies were collected frequently for 5 h to assess post-prandial plasma amino acid profiles and subsequent post-prandial muscle protein synthesis rates. RESULTS: MILK increased plasma essential amino acid concentrations more than PEA over the 5 h post-prandial period (incremental area under curve 151 ± 31 vs 102 ± 15 mmol∙300 min∙L-1, respectively; P < 0.001). Ingestion of both MILK and PEA showed a robust muscle protein synthetic response with no significant differences between treatments (0.053 ± 0.013 and 0.053 ± 0.017%∙h-1, respectively; P = 0.96). CONCLUSION: Post-prandial muscle protein synthesis rates following the ingestion of 30 g pea-derived protein do not differ from the response following ingestion of an equivalent amount of milk-derived protein. International Clinical Trials Registry Platform (NTR6548; 27-06-2017).

Resistance Exercise Training, a Simple Intervention to Preserve Muscle Mass and Strength in Prostate Cancer Patients on Androgen Deprivation Therapy.

Androgen deprivation therapy (ADT) forms the cornerstone in the treatment of advanced prostate cancer. However, by suppressing testosterone ADT results in a decrease of skeletal muscle mass. In this narrative review, we explore the magnitude and mechanisms of ADT-induced muscle mass loss and the consequences for muscle strength and physical performance. Subsequently, we elucidate the effectiveness of supervised resistance exercise training as a means to mitigate these adverse effects. Literature shows that resistance exercise training can effectively counteract ADT-induced loss of appendicular lean body mass and decline in muscle strength, while the effect on physical performances is inconclusive. As resistance exercise training is feasible and can be safely implemented during ADT (with special attention for patients with bone metastases), it should be incorporated in standard clinical care for prostate cancer patients (starting) with ADT.

Muscle Mass and Strength Gains Following Resistance Exercise Training in Older Adults 65-75 Years and Older Adults Above 85 Years.

Resistance exercise training (RET) can be applied effectively to increase muscle mass and function in older adults (65-75 years). However, it has been speculated that older adults above 85 years are less responsive to the benefits of RET. This study compares the impact of RET on muscle mass and function in healthy older adults 65-75 years versus older adults above 85 years. We subjected 17 healthy older adults 65-75 years (OLDER 65-75, n = 13/4 [female/male]; 68 ± 2 years; 26.9 ± 2.3 kg/m2) and 12 healthy older adults above 85 years (OLDER 85+, n = 7/5 [female/male]; 87 ± 3 years; 26.0 ± 3.6 kg/m2) to 12 weeks of whole-body RET (three times per week). Prior to, and after 6 and 12 weeks of training, quadriceps and lumbar spine vertebra 3 muscle cross-sectional area (computed tomography scan), whole-body lean mass (dual-energy X-ray absorptiometry scan), strength (one-repetition maximum test), and physical performance (timed up and go and short physical performance battery) were assessed. Twelve weeks of RET resulted in a 10% ± 4% and 11% ± 5% increase in quadriceps cross-sectional area (from 46.5 ± 10.7 to 51.1 ± 12.1 cm2, and from 38.9 ± 6.1 to 43.1 ± 8.0 cm2, respectively; p < .001; η2 = .67); a 2% ± 3% and 2% ± 3% increase in whole-body lean mass (p = .001; η2 = .22); and a 38% ± 20% and 46% ± 14% increase in one-repetition maximum leg extension strength (p < .001; η2 = .77) in the OLDER 65-75 and OLDER 85+ groups, respectively. No differences in the responses to RET were observed between groups (Time × Group, all p > .60; all η2 ≤ .012). Physical performance on the short physical performance battery and timed up and go improved (both p < .01; η2 ≥ .22), with no differences between groups (Time × Group, p > .015; η2 ≤ .07). Prolonged RET increases muscle mass, strength, and physical performance in the aging population, with no differences between 65-75 years and 85+ years older adults.

Jumping Exercise Combined With Collagen Supplementation Preserves Bone Mineral Density in Elite Cyclists.

This study assessed the effect of combined jump training and collagen supplementation on bone mineral density (BMD) in elite road-race cyclists. In this open-label, randomized study with two parallel groups, 36 young (21 ± 3 years) male (n = 8) and female (n = 28) elite road-race cyclists were allocated to either an intervention (INT: n = 18) or a no-treatment control (CON: n = 18) group. The 18-week intervention period, conducted during the off-season, comprised five 5-min bouts of jumping exercise per week, with each bout preceded by the ingestion of 15 g hydrolyzed collagen. Before and after the intervention, BMD of various skeletal sites and trabecular bone score of the lumbar spine were assessed by dual-energy X-ray absorptiometry, along with serum bone turnover markers procollagen Type I N propeptide and carboxy-terminal cross-linking telopeptide of Type I collagen. BMD of the femoral neck decreased in CON (from 0.789 ± 0.104 to 0.774 ± 0.095 g/cm2), while being preserved in INT (from 0.803 ± 0.058 to 0.809 ± 0.066 g/cm2; Time × Treatment, p < .01). No differences between treatments were observed for changes in BMD at the total hip, lumbar spine, and whole body (Time × Treatment, p > .05 for all). Trabecular bone score increased from 1.38 ± 0.08 to 1.40 ± 0.09 in CON and from 1.46 ± 0.08 to 1.47 ± 0.08 in INT, respectively (time effect: p < .01), with no differences between treatments (Time × Treatment: p = .33). Serum procollagen Type I N propeptide concentrations decreased to a similar extent in CON (83.6 ± 24.8 to 71.4 ± 23.1 ng/ml) and INT (82.8 ± 30.7 to 66.3 ± 30.6; time effect, p < .001; Time × Treatment, p = .22). Serum carboxy-terminal cross-linking telopeptide of Type I collagen concentrations did not change over time, with no differences between treatments (time effect, p = .08; Time × Treatment, p = .58). In conclusion, frequent short bouts of jumping exercise combined with collagen supplementation beneficially affects femoral neck BMD in elite road-race cyclists.

Type II Muscle Fiber Capillarization Is an Important Determinant of Post-Exercise Microvascular Perfusion in Older Adults.

INTRODUCTION: Microvascular perfusion is essential for post-exercise skeletal muscle recovery to ensure adequate delivery of nutrients and growth factors. This study assessed the relationship between various indices of muscle fiber capillarization and microvascular perfusion assessed by contrast-enhanced ultrasound (CEUS) at rest and during recovery from a bout of resistance exercise in older adults. METHODS: Sixteen older adults (72 ± 6 y, 5/11 male/female) participated in an experimental test day during which a muscle biopsy was collected from the vastus lateralis and microvascular perfusion was determined by CEUS at rest and at 10 and 40 min following a bout of resistance exercise. Immunohistochemistry was performed on muscle tissue samples to determine various indices of both mixed and fiber-type-specific muscle fiber capillarization. RESULTS: Microvascular blood volume at t = 10 min was higher compared with rest and t = 40 min (27.2 ± 4.7 vs. 3.9 ± 4.0 and 7.0 ± 4.9 AU, respectively, both p < 0.001). Microvascular blood volume at t = 40 min was higher compared with rest (p < 0.001). No associations were observed between different indices of mixed muscle fiber capillarization and microvascular blood volume at rest and following exercise. A moderate (r = 0.59, p < 0.05) and strong (r = 0.81, p < 0.001) correlation was observed between type II muscle fiber capillary-to-fiber ratio and the microvascular blood volume increase from rest to t = 10 and t = 40 min, respectively. In addition, type II muscle fiber capillary contacts and capillary-to-fiber perimeter exchange index were strongly correlated with the microvascular blood volume increase from rest to t = 40 min (r = 0.66, p < 0.01 and r = 0.64, p < 0.01, respectively). CONCLUSION: Resistance exercise strongly increases microvascular blood volume for at least 40 min after exercise cessation in older adults. This resistance exercise-induced increase in microvascular blood volume is strongly associated with type II muscle fiber capillarization in older adults.

A Low or High Physical Activity Level Does Not Modulate Prostate Tumor Tissue Protein Synthesis Rates.

INTRODUCTION: Physical activity level has been identified as an important factor in the development and progression of various types of cancer. In this study, we determined the impact of a low versus high physical activity level on skeletal muscle, healthy prostate, and prostate tumor protein synthesis rates in vivo in prostate cancer patients. METHODS: Thirty prostate cancer patients (age: 66 ± 5 y, BMI: 27.4 ± 2.9 kg per m2) were randomized to a low (<4000 steps per day, n = 15) or high (>14000 steps per day, n = 15) physical activity level for seven days prior to their scheduled radical prostatectomy. Daily deuterium oxide administration was combined with the collection of plasma, skeletal muscle, non-tumorous prostate, and prostate tumor tissue during the surgical procedure to determine tissue protein synthesis rates throughout the intervention period. RESULTS: Daily step counts averaged 3610 ± 878 and 17589 ± 4680 steps in patients subjected to the low and high physical activity level, respectively (P < 0.001). No differences were observed between tissue protein synthesis rates of skeletal muscle, healthy prostate, or prostate tumor between the low (1.47 ± 0.21, 2.74 ± 0.70, and 4.76 ± 1.23 % per day, respectively) and high (1.42 ± 0.16, 2.64 ± 0.58, and 4.72 ± 0.80 % per day, respectively) physical activity group (all P > 0.4). Tissue protein synthesis rates were nearly twofold higher in prostate tumor compared with non-tumorous prostate tissue. CONCLUSIONS: A short-term high or low physical activity level does not modulate prostate or prostate tumor protein synthesis rates in vivo in prostate cancer patients. More studies on the impact of physical activity level on tumor protein synthesis rates and tumor progression are warranted to understand the potential impact of lifestyle interventions in the prevention and treatment of cancer.

The anabolic response to protein ingestion during recovery from exercise has no upper limit in magnitude and duration in vivo in humans.

The belief that the anabolic response to feeding during postexercise recovery is transient and has an upper limit and that excess amino acids are being oxidized lacks scientific proof. Using a comprehensive quadruple isotope tracer feeding-infusion approach, we show that the ingestion of 100 g protein results in a greater and more prolonged (>12 h) anabolic response when compared to the ingestion of 25 g protein. We demonstrate a dose-response increase in dietary-protein-derived plasma amino acid availability and subsequent incorporation into muscle protein. Ingestion of a large bolus of protein further increases whole-body protein net balance, mixed-muscle, myofibrillar, muscle connective, and plasma protein synthesis rates. Protein ingestion has a negligible impact on whole-body protein breakdown rates or amino acid oxidation rates. These findings demonstrate that the magnitude and duration of the anabolic response to protein ingestion is not restricted and has previously been underestimated in vivo in humans.

One Week of Single Leg Immobilization Lowers Muscle Connective Protein Synthesis Rates in Healthy, Young Adults.

PURPOSE: Short periods of limb immobilization lower myofibrillar protein synthesis rates. Within skeletal muscle, the extracellular matrix of connective proteins is recognized as an important factor determining the capacity to transmit contractile force. Little is known regarding the impact of immobilization and subsequent recovery on muscle connective protein synthesis rates. This study examined the impact of one week of leg immobilization and two weeks of subsequent ambulant recovery on daily muscle connective protein synthesis rates. METHODS: Thirty healthy, young (24 ± 5 y) men were subjected to 7 days of one-legged knee immobilization followed by 14 days of ambulant recovery. Deuterium oxide ingestion was applied over the entire period and muscle biopsy samples were collected before immobilization, after immobilization, and after recovery to measure muscle connective protein synthesis rates and mRNA expression of key extracellular matrix proteins (collagen I, collagen III), glycoproteins (fibronectin, tenascin-C), and proteoglycans (fibromodulin, and decorin). A two-way repeated measures (time x leg) ANOVA was used to compare changes in muscle connective protein synthesis rates during immobilization and recovery. RESULTS: During immobilization, muscle connective protein synthesis rates were lower in the immobilized (1.07 ± 0.30 %/d) compared with the non-immobilized (1.48 ± 0.44 %/d; P < 0.01) leg. When compared to the immobilization period, connective protein synthesis rates in the immobilized leg increased during subsequent recovery (1.48 ± 0.64 %/d; P < 0.01). Following recovery, skeletal muscle collagen I, collagen III, fibronectin, fibromodulin, and decorin mRNA expression increased when compared to the post-immobilization timepoint (all P < 0.001). CONCLUSIONS: One week of leg immobilization lowers muscle connective protein synthesis rates. Muscle connective protein synthesis rates increase during subsequent ambulant recovery, which is accompanied by increased mRNA expression of key extracellular matrix proteins.

Trabecular, but not cortical, bone tissue protein synthesis rates are lower in the femoral head when compared to the proximal femur following an intracapsular hip fracture.

BACKGROUND: All musculoskeletal tissues are in a constant state of turnover, with a dynamic equilibrium between tissue protein synthesis and breakdown rates. The synthesis of protein allows musculoskeletal tissues to heal following injury. Yet, impaired tissue healing is observed following certain injuries, such as geriatric hip fractures. It is assumed that the regenerative properties of femoral head bone tissue are compromised following an intracapsular hip fracture and therefore hip replacement surgery is normally performed. However, the actual impact on in vivo bone protein synthesis rates has never been determined. DESIGN: In the present study, 10 patients (age: 79 ± 10 y, BMI: 24 ± 4 kg/m2) with an acute (<24 h) intracapsular hip fracture received a primed continuous intravenous infusion of L-[ring-13C6]-phenylalanine before and throughout their hip replacement surgery. Trabecular and cortical bone tissue from both the femoral head and proximal femur were sampled during surgery to assess protein synthesis rates of affected (femoral head) and unaffected (proximal femur) bone tissue, respectively. In addition, tissue samples of gluteus maximus muscle, synovium, ligamentum teres, and femoral head cartilage were collected. Tissue-specific protein synthesis rates were assessed by measuring L-[ring-13C6]-phenylalanine incorporation in tissue protein. RESULTS: Femoral head trabecular bone protein synthesis rates (0.056 [0.024-0.086] %/h) were lower when compared to proximal femur trabecular bone protein synthesis rates (0.081 [0.056-0.118] %/h; P = 0.043). Cortical bone protein synthesis rates did not differ between the femoral head and proximal femur (0.041 [0.021-0.078] and 0.045 [0.028-0.073] %/h, respectively; P > 0.05). Skeletal muscle, synovium, ligamentum teres, and femoral head cartilage protein synthesis rates averaged 0.080 [0.048-0.089], 0.093 [0.051-0.130], 0.121 [0.110-0.167], and 0.023 [0.015-0.039] %/h, respectively. CONCLUSION: In contrast to the general assumption that the femoral head is avital after an intracapsular displaced hip fracture in the elderly, our data show that bone protein synthesis is still ongoing in femoral head bone tissue during the early stages following an intracapsular hip fracture in older patients. Nonetheless, trabecular bone protein synthesis rates are lower in the femoral head when compared to the proximal femur in older patients following an acute intracapsular hip fracture. Trial register no: NL9036.

Branched-chain ketoacid co-ingestion with protein lowers amino acid oxidation during hemodialysis: A randomized controlled cross-over trial.

BACKGROUND & AIMS: Hemodialysis removes amino acids from the circulation, thereby stimulating muscle proteolysis. Protein ingestion during hemodialysis can compensate for amino acid removal but may also increase uremic toxin production. Branched-chain ketoacid (BCKA) co-ingestion may provide an additional anabolic stimulus without adding to uremic toxin accumulation. In the present study we assessed the impact of BCKA co-ingestion with protein on forearm amino acid balance and amino acid oxidation during hemodialysis. METHODS: Nine patients (age: 73 ± 10 y) on chronic hemodialysis participated in this crossover trial. During two 4-h hemodialysis sessions, patients ingested 18 g protein with (PRO + BCKA) or without (PRO) 9 g BCKAs in a randomized order. Test beverages were labeled with L-[ring-13C6]-phenylalanine and provided throughout the last 3 h of hemodialysis as 18 equal sips consumed with 10-min intervals. Arterial and venous plasma as well as breath samples were collected frequently throughout hemodialysis. RESULTS: Arterial plasma total amino acid (TAA) concentrations during PRO and PRO + BCKA treatments were significantly lower after 1 h of hemodialysis (2.6 ± 0.3 and 2.6 ± 0.3 mmol/L, respectively) when compared to pre-hemodialysis concentrations (4.2 ± 1.0 and 4.0 ± 0.5 mmol/L, respectively; time effect: P < 0.001). Arterial plasma TAA concentrations increased throughout test beverage ingestion (time effect: P = 0.027) without differences between treatments (time∗treatment: P = 0.62). Forearm arteriovenous TAA balance during test beverage ingestion did not differ between timepoints (time effect: P = 0.31) or treatments (time∗treatment: P = 0.34). Whole-body phenylalanine oxidation was 33 ± 16% lower during PRO + BCKA when compared to PRO treatments (P < 0.001). CONCLUSIONS: BCKA co-ingestion with protein during hemodialysis does not improve forearm net protein balance but lowers amino acid oxidation.

Vicia faba Peptide Network Supplementation Does Not Differ From Milk Protein in Modulating Changes in Muscle Size During Short-Term Immobilization and Subsequent Remobilization, but Increases Muscle Protein Synthesis Rates During Remobilization in Healthy Young Men.

BACKGROUND: Muscle mass and strength decrease during short periods of immobilization and slowly recover during remobilization. Recent artificial intelligence applications have identified peptides that appear to possess anabolic properties in in vitro assays and murine models. OBJECTIVES: This study aimed to compare the impact of Vicia faba peptide network compared with milk protein supplementation on muscle mass and strength loss during limb immobilization and regain during remobilization. METHODS: Thirty young (24 ± 5 y) men were subjected to 7 d of one-legged knee immobilization followed by 14 d of ambulant recovery. Participants were randomly allocated to ingest either 10 g of the Vicia faba peptide network (NPN_1; n = 15) or an isonitrogenous control (milk protein concentrate; MPC; n = 15) twice daily throughout the study. Single-slice computed tomography scans were performed to assess quadriceps cross-sectional area (CSA). Deuterium oxide ingestion and muscle biopsy sampling were applied to measure myofibrillar protein synthesis rates. RESULTS: Leg immobilization decreased quadriceps CSA (primary outcome) from 81.9 ± 10.6 to 76.5 ± 9.2 cm2 and from 74.8 ± 10.6 to 71.5 ± 9.8 cm2 in the NPN_1 and MPC groups, respectively (P < 0.001). Remobilization partially recovered quadriceps CSA (77.3 ± 9.3 and 72.6 ± 10.0 cm2, respectively; P = 0.009), with no differences between the groups (P > 0.05). During immobilization, myofibrillar protein synthesis rates (secondary outcome) were lower in the immobilized leg (1.07% ± 0.24% and 1.10% ± 0.24%/d, respectively) than in the non-immobilized leg (1.55% ± 0.27% and 1.52% ± 0.20%/d, respectively; P < 0.001), with no differences between the groups (P > 0.05). During remobilization, myofibrillar protein synthesis rates in the immobilized leg were greater with NPN_1 than those with MPC (1.53% ± 0.38% vs. 1.23% ± 0.36%/d, respectively; P = 0.027). CONCLUSION: NPN_1 supplementation does not differ from milk protein in modulating the loss of muscle size during short-term immobilization and the regain during remobilization in young men. NPN_1 supplementation does not differ from milk protein supplementation in modulating the myofibrillar protein synthesis rates during immobilization but further increases myofibrillar protein synthesis rates during remobilization.

The Postprandial Plasma Amino Acid Response Does Not Differ Following the Ingestion of a Solid Versus a Liquid Milk Protein Product in Healthy Adult Females.

Dietary protein digestion and amino acid absorption rates are modulated by numerous factors such as the food matrix. It has been speculated that protein ingested in liquid form is more rapidly digested and absorbed when compared with ingestion in solid form. Here, we assessed the postprandial plasma amino acid availability following ingestion of a single bolus of protein provided in either liquid or solid form. Twelve healthy, young females were included in this randomized cross-over study. On two separate test days, participants ingested 20-g milk protein concentrate in solid form (protein bar) or in liquid form (protein drink). Products were composed of matched ingredients and, thereby, had the same macro- and micronutrient composition. On both test days, arterialized blood samples were collected at regular time intervals for up to 4 hr following protein ingestion to assess the postprandial rise in plasma amino acid concentrations. Protein ingestion robustly elevated circulating plasma amino acid concentrations (p < .001), with no significant differences between treatments (p = .088). The incremental area under the curve of the postprandial rise in total plasma amino acid concentrations did not differ following bar versus drink consumption (160 ± 73 vs. 160 ± 71 mmol·L-1·240 min-1, respectively; 95% confidence interval [-37, 37]; Cohen's dz = 0.003; p = .992). Ingestion of protein in liquid or solid form does not modulate postprandial amino acid availability in healthy, female adults. Any differences in protein digestion and amino acid absorption due to differences in food matrix are not attributed to the protein being consumed as a bar or as a drink.

Dietary nitrate preserves mitochondrial bioenergetics and mitochondrial protein synthesis rates during short-term immobilization in mice.

Skeletal muscle disuse reduces muscle protein synthesis rates and induces atrophy, events associated with decreased mitochondrial respiration and increased reactive oxygen species. Given that dietary nitrate can improve mitochondrial bioenergetics, we examined whether nitrate supplementation attenuates disuse-induced impairments in mitochondrial function and muscle protein synthesis rates. Female C57Bl/6N mice were subjected to single-limb casting (3 or 7 days) and consumed drinking water with or without 1 mM sodium nitrate. Compared with the contralateral control limb, 3 days of immobilization lowered myofibrillar fractional synthesis rates (FSR, P < 0.0001), resulting in muscle atrophy. Although FSR and mitophagy-related proteins were higher in subsarcolemmal (SS) compared with intermyofibrillar (IMF) mitochondria, immobilization for 3 days decreased FSR in both SS (P = 0.009) and IMF (P = 0.031) mitochondria. Additionally, 3 days of immobilization reduced maximal mitochondrial respiration, decreased mitochondrial protein content, and increased maximal mitochondrial reactive oxygen species emission, without altering mitophagy-related proteins in muscle homogenate or isolated mitochondria (SS and IMF). Although nitrate consumption did not attenuate the decline in muscle mass or myofibrillar FSR, intriguingly, nitrate completely prevented immobilization-induced reductions in SS and IMF mitochondrial FSR. In addition, nitrate prevented alterations in mitochondrial content and bioenergetics after both 3 and 7 days of immobilization. However, in contrast to 3 days of immobilization, nitrate did not prevent the decline in SS and IMF mitochondrial FSR after 7 days of immobilization. Therefore, although nitrate supplementation was not sufficient to prevent muscle atrophy, nitrate may represent a promising therapeutic strategy to maintain mitochondrial bioenergetics and transiently preserve mitochondrial protein synthesis rates during short-term muscle disuse. KEY POINTS: Alterations in mitochondrial bioenergetics (decreased respiration and increased reactive oxygen species) are thought to contribute to muscle atrophy and reduced protein synthesis rates during muscle disuse. Given that dietary nitrate can improve mitochondrial bioenergetics, we examined whether nitrate supplementation could attenuate immobilization-induced skeletal muscle impairments in female mice. Dietary nitrate prevented short-term (3 day) immobilization-induced declines in mitochondrial protein synthesis rates, reductions in markers of mitochondrial content, and alterations in mitochondrial bioenergetics. Despite these benefits and the preservation of mitochondrial content and bioenergetics during more prolonged (7 day) immobilization, nitrate consumption did not preserve skeletal muscle mass or myofibrillar protein synthesis rates. Overall, although dietary nitrate did not prevent atrophy, nitrate supplementation represents a promising nutritional approach to preserve mitochondrial function during muscle disuse.