scholarly journals The Impact of Vegan and Vegetarian Diets on Physical Performance and Molecular Signaling in Skeletal Muscle

Nutrients ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 3884
Author(s):  
Alexander Pohl ◽  
Frederik Schünemann ◽  
Käthe Bersiner ◽  
Sebastian Gehlert
Keyword(s):  
Skeletal Muscle ◽  
Physical Performance ◽  
Muscle Protein ◽  
Endurance Performance ◽  
Vegetarian Diet ◽  
Molecular Signaling ◽  
Dietary Regimen ◽  
Strength Performance ◽  
Vegetarian Diets ◽  
The Impact

Muscular adaptations can be triggered by exercise and diet. As vegan and vegetarian diets differ in nutrient composition compared to an omnivorous diet, a change in dietary regimen might alter physiological responses to physical exercise and influence physical performance. Mitochondria abundance, muscle capillary density, hemoglobin concentration, endothelial function, functional heart morphology and availability of carbohydrates affect endurance performance and can be influenced by diet. Based on these factors, a vegan and vegetarian diet possesses potentially advantageous properties for endurance performance. Properties of the contractile elements, muscle protein synthesis, the neuromuscular system and phosphagen availability affect strength performance and can also be influenced by diet. However, a vegan and vegetarian diet possesses potentially disadvantageous properties for strength performance. Current research has failed to demonstrate consistent differences of performance between diets but a trend towards improved performance after vegetarian and vegan diets for both endurance and strength exercise has been shown. Importantly, diet alters molecular signaling via leucine, creatine, DHA and EPA that directly modulates skeletal muscle adaptation. By changing the gut microbiome, diet can modulate signaling through the production of SFCA.

scholarly journals Efficacy of Popular Diets Applied by Endurance Athletes on Sports Performance: Beneficial or Detrimental? A Narrative Review

Nutrients ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 491
Author(s):  
Aslı Devrim-Lanpir ◽  
Lee Hill ◽  
Beat Knechtle
Keyword(s):  
Gastrointestinal Symptoms ◽  
Endurance Performance ◽  
Endurance Athletes ◽  
Intermittent Fasting ◽  
Nutritional Strategy ◽  
Current Perspective ◽  
Vegetarian Diets ◽  
Fat Diets ◽  
The Impact ◽  
Harsh Conditions

Endurance athletes need a regular and well-detailed nutrition program in order to fill their energy stores before training/racing, to provide nutritional support that will allow them to endure the harsh conditions during training/race, and to provide effective recovery after training/racing. Since exercise-related gastrointestinal symptoms can significantly affect performance, they also need to develop strategies to address these issues. All these factors force endurance athletes to constantly seek a better nutritional strategy. Therefore, several new dietary approaches have gained interest among endurance athletes in recent decades. This review provides a current perspective to five popular diet approaches: (a) vegetarian diets, (b) high-fat diets, (c) intermittent fasting diets, (d) gluten-free diet, and (e) low fermentable oligosaccharides, disaccharides, monosaccharides and polyols (FODMAP) diets. We reviewed scientific studies published from 1983 to January 2021 investigating the impact of these popular diets on the endurance performance and health aspects of endurance athletes. We also discuss all the beneficial and harmful aspects of these diets, and offer key suggestions for endurance athletes to consider when following these diets.

scholarly journals Knockdown of the E3 ubiquitin ligase UBR5 and its role in skeletal muscle anabolism

2021 ◽  
Vol 320 (1) ◽  
pp. C45-C56
Author(s):  
David C. Hughes ◽  
Daniel C. Turner ◽  
Leslie M. Baehr ◽  
Robert A. Seaborne ◽  
Mark Viggars ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Mass ◽  
Ubiquitin Ligase ◽  
Fluorescent Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Tibialis Anterior Muscle ◽  
E3 Ubiquitin Ligase ◽  
Skeletal Muscle Atrophy ◽  
The Impact

UBR5 is an E3 ubiquitin ligase positively associated with anabolism, hypertrophy, and recovery from atrophy in skeletal muscle. The precise mechanisms underpinning UBR5’s role in the regulation of skeletal muscle mass remain unknown. The present study aimed to elucidate these mechanisms by silencing the UBR5 gene in vivo. To achieve this aim, we electroporated a UBR5-RNAi plasmid into mouse tibialis anterior muscle to investigate the impact of reduced UBR5 on anabolic signaling MEK/ERK/p90RSK and Akt/GSK3β/p70S6K/4E-BP1/rpS6 pathways. Seven days after UBR5 RNAi electroporation, although reductions in overall muscle mass were not detected, the mean cross-sectional area (CSA) of green fluorescent protein (GFP)-positive fibers were reduced (−9.5%) and the number of large fibers were lower versus the control. Importantly, UBR5-RNAi significantly reduced total RNA, muscle protein synthesis, ERK1/2, Akt, and GSK3β activity. Although p90RSK phosphorylation significantly increased, total p90RSK protein levels demonstrated a 45% reduction with UBR5-RNAi. Finally, these early events after 7 days of UBR5 knockdown culminated in significant reductions in muscle mass (−4.6%) and larger reductions in fiber CSA (−18.5%) after 30 days. This was associated with increased levels of phosphatase PP2Ac and inappropriate chronic elevation of p70S6K and rpS6 between 7 and 30 days, as well as corresponding reductions in eIF4e. This study demonstrates that UBR5 plays an important role in anabolism/hypertrophy, whereby knockdown of UBR5 culminates in skeletal muscle atrophy.

scholarly journals Sarcopenia in chronic kidney disease – A brief review

2021 ◽  
Vol 35 (2) ◽  
Author(s):  
Beatriz Donato ◽  
◽  
Catarina Teixeira ◽  
Sónia Velho ◽  
Edgar Almeida ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Chronic Kidney Disease ◽  
Kidney Disease ◽  
Muscle Mass ◽  
Physical Performance ◽  
Functional Independence ◽  
Muscle Dysfunction ◽  
Skeletal Muscle Dysfunction ◽  
Age Related ◽  
The Impact

Sarcopenia is a progressive age -related loss of muscle mass associated with a decline in muscle function and physical performance. Patients with chronic kidney disease experience substantial loss of muscle mass, weakness, and poor physical performance. Indeed, with the progression of chronic kidney disease, skeletal muscle dysfunction contributes to mobility limitation, loss of functional independence, and vulnerability to disease complications. There is a lack of robust data on the negative effect of the impact of kidney disease on skeletal muscle dysfunction, as well as on screening and treatment strategies that can be used in clinical practice to prevent functional decline and disability. Therefore, sarcopenia may be an underestimated condition with major implications for people with chronic kidney disease, even before the start of dialysis, which makes research into this topic necessary. The purpose of this review is to expand on some fundamental topics of sarcopenia, with an emphasis on the setting of chronic kidney disease patients.

P7 THE IMPACT OF PREHABILITATION ON PARAMETERS OF BODY COMPOSITION IN PATIENTS UNDERGOING MULTIMODAL THERAPY FOR OESOPHAGO-GASTRIC (OG) CANCER

2019 ◽  
Vol 32 (Supplement_2) ◽  
Author(s):  
Doganay Emre ◽  
R Boshier Piers ◽  
J Halliday Laura ◽  
Thomas Rob ◽  
E Low Donald ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Body Composition ◽  
Neoadjuvant Therapy ◽  
Physical Performance ◽  
Skeletal Muscle Index ◽  
Significant Difference ◽  
Axial Ct ◽  
Gastric Cancer Patients ◽  
Subcutaneous Adipose ◽  
The Impact

Abstract Aims This study characterises changes in body composition and physical performance during neoadjuvant therapy in the context of prehabilitation before oesophago-gastric resection. Background & Methods Neoadjuvant therapy has deleterious effects on functional capacity and may lead to a decline in physical fitness and skeletal muscle mass. This is a retrospective review of oesophago-gastric cancer patients undergoing prehabilitation. Assessment of body composition (skeletal muscle, visceral and subcutaneous adipose tissue) was performed from L3 axial CT images acquired at the time of diagnosis and after neoadjuvant therapy. Results 42 patients (33M, 65.7±11.1) met the inclusion criteria. Patients body weight (81.8±21.3 kg vs. 81.3±21 kg, p=0.668) and BMI (27.9±7.2 kg/m2 vs. 27.8±7.0 kg/m2, p=0.648) did not change significantly between the study time points. There was no significant difference between estimated lean body mass (39.2±13.2 vs. 38.3±10.1; 95%CI -2.5 to 4.3 p=0.592) and fat mass (30.6±15.4 vs. 28.6±14.0; 95%CI -1.7 to 5.7, p=0.284). Skeletal muscle index significantly decreased (46.5±9.9 to 43.1±9.8; 95%CI 2.1 to 4.6, p<0.001). Patients who were adherent to the prehabilitation programme had a significantly higher skeletal muscle index compared to noncompliant patients (47.4±10.4 vs. 40.2±8.9; 95%CI 1.5 to 13.5, p=0.016). Patients who achieved a higher MET-minutes were less likely to be sarcopenic (F(1,40 = 6.1, p = 0.018)).There was no decline in physical performance (Median IQR; VO2max ml kg−1min−1) during neoadjuvant therapy (17.5 [14-19.3] vs. 17.5 [13.3-19.3]; p=0.164). Conclusion this is the first study to report variations in parameters of body composition in patients undergoing a prehabilitation programme. Findings suggest that prehabilitation may be a useful adjunct in limiting the extent of sarcopenia and patient deconditioning during neoadjuvant therapy.

Role of Amino Acids and Peptides in the Molecular Signaling in Skeletal Muscle after Resistance Exercise

2007 ◽  
Vol 17 (s1) ◽  
pp. S47-S57 ◽  
Author(s):  
René Koopman
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Resistance Exercise ◽  
Translation Initiation ◽  
Intracellular Signaling ◽  
Muscle Protein ◽  
Mrna Translation ◽  
Molecular Signaling ◽  
Stimulation Of

Resistance exercise can effectively result in an increase in muscle mass, or hypertrophy, which generally becomes apparent after several weeks of training. Muscle hypertrophy requires muscle protein synthesis to exceed protein breakdown during an extended time period. It has been firmly established that the interaction between exercise and nutrition (i.e., protein intake) is necessary to attain net protein accretion in skeletal muscle. The stimulation of protein synthesis is caused in part by stimulation of mRNA translation initiation. There is relatively little information on the response of intracellular signaling controlling mRNA translation to exercise and nutrition, especially in humans, but the available data in humans seem to suggest that a single bout of resistance exercise does not substantially enhance PI-3 kinase/mTOR signaling during the first 2 h after exercise. Moreover, it is demonstrated that the ingestion of protein or amino acids after exercise is crucial to further stimulate molecular signaling that controls translation initiation. The aim of this review is to provide an overview of the intracellular signaling related to translational control and to provide a summary of the current knowledge about the response of the signaling pathways controlling the anabolic response to exercise and nutrient intake in vivo in humans.

scholarly journals Continuous Feeding Does Not Blunt Skeletal Muscle Protein Synthesis and Lean Growth Compared to Intermittent Bolus Feeding in the Preterm Piglet (OR26-06-19)

2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Marko Rudar ◽  
Jane Naberhuis ◽  
Hanh Nguyen ◽  
Agus Suryawan ◽  
Candace Style ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Body Weight ◽  
Protein Synthesis ◽  
Translation Initiation ◽  
Muscle Protein ◽  
Feeding Strategies ◽  
Intermittent Bolus ◽  
Lean Growth ◽  
Continuous Feeding ◽  
The Impact

Abstract Objectives Refining early feeding strategies for premature infants is essential for mitigating adverse outcomes of prematurity. In neonatal term piglets, continuous feeding blunts growth compared to intermittent bolus feeding. Our objective was to determine the impact of feeding modality on lean growth in preterm pigs. We hypothesized that intermittent bolus feeding can mitigate low lean growth rates in preterm neonates compared to continuous feeding. Methods Pigs obtained by C-section (105 d gestation; 952 ± 205 g body weight) were fitted with an umbilical artery catheter (later replaced with jugular vein catheter) and an orogastric tube for parenteral and enteral nutrition, respectively. Pigs were assigned to continuous (CONT; 7.5 mL/[kg·h]) or intermittent bolus (INT; 30 mL/kg every 4 h over 15 min) feeding for 21 d. Pigs initially received parenteral nutrition and were advanced to full oral feeds over 6 d (220 kcal/kg and 16 g/kg protein per day). Body composition (by DXA), plasma insulin, and skeletal muscle anabolic signaling and fractional protein synthesis rates (PS; L-[ring-2H5]phenylalanine) were determined in INT pigs in the postabsorptive (before a meal, INT-PA; n = 13) and postprandial (after a meal, INT-PP; n = 16) states and in CONT pigs (n = 14). Results Body weight gain, lean mass, and fat mass did not differ between INT and CONT pigs. Insulin was lower before feeding for INT pigs than CONT pigs (P < 0.05). Insulin increased with feeding for INT pigs and exceeded that of CONT pigs at 30 and 60 min (P < 0.01) before returning to baseline levels at 240 min. In the longissimus dorsi (LD), gastrocnemius, and soleus muscles, the abundance of the eIF4E·eIF4G complex, which is required for translation initiation, was greater in INT-PP and CONT pigs than INT-PA pigs (P < 0.01), but did not differ between INT-PP and CONT pigs. PS in the LD muscle was greater in INT-PP pigs than INT-PA pigs (P < 0.01), but did not differ between INT-PP and CONT pigs. Conclusions Continuous feeding does not blunt translation initiation and protein synthesis in skeletal muscle compared to intermittent bolus feeding in preterm piglets. The resulting absence of enhanced lean growth with intermittent bolus compared to continuous feeding contrasts with term piglets and may be a consequence of prematurity. Funding Sources USDA CRIS 6250-51000-055, NIH HD072891, and USDA NIFA 2013-67015-20438.

scholarly journals Endurance-Type Exercise Increases Bulk and Individual Mitochondrial Protein Synthesis Rates in Rats

2020 ◽  
Vol 30 (2) ◽  
pp. 153-164 ◽  
Author(s):  
Andrew M. Holwerda ◽  
Freek G. Bouwman ◽  
Miranda Nabben ◽  
Ping Wang ◽  
Janneau van Kranenburg ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Atp Synthase ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Mitochondrial Protein ◽  
Experimental Period ◽  
Mitochondrial Protein Synthesis ◽  
The Impact

Physical activity increases muscle protein synthesis rates. However, the impact of exercise on the coordinated up- and/or downregulation of individual protein synthesis rates in skeletal muscle tissue remains unclear. The authors assessed the impact of exercise on mixed muscle, myofibrillar, and mitochondrial protein synthesis rates as well as individual protein synthesis rates in vivo in rats. Adult Lewis rats either remained sedentary (n = 3) or had access to a running wheel (n = 3) for the last 2 weeks of a 3-week experimental period. Deuterated water was injected and subsequently administered in drinking water over the experimental period. Blood and soleus muscle were collected and used to assess bulk mixed muscle, myofibrillar, and mitochondrial protein synthesis rates using gas chromatography–mass spectrometry and individual muscle protein synthesis rates using liquid chromatography–mass spectrometry (i.e., dynamic proteomic profiling). Wheel running resulted in greater myofibrillar (3.94 ± 0.26 vs. 3.03 ± 0.15%/day; p < .01) and mitochondrial (4.64 ± 0.24 vs. 3.97 ± 0.26%/day; p < .05), but not mixed muscle (2.64 ± 0.96 vs. 2.38 ± 0.62%/day; p = .71) protein synthesis rates, when compared with the sedentary condition. Exercise impacted the synthesis rates of 80 proteins, with the difference from the sedentary condition ranging between −64% and +420%. Significantly greater synthesis rates were detected for F1-ATP synthase, ATP synthase subunit alpha, hemoglobin, myosin light chain-6, and synaptopodin-2 (p < .05). The skeletal muscle protein adaptive response to endurance-type exercise involves upregulation of mitochondrial protein synthesis rates, but it is highly coordinated as reflected by the up- and downregulation of various individual proteins across different bulk subcellular protein fractions.

scholarly journals The impact of delivery profile of essential amino acids upon skeletal muscle protein synthesis in older men: clinical efficacy of pulse vs. bolus supply

2015 ◽  
Vol 309 (5) ◽  
pp. E450-E457 ◽  
Author(s):  
W. Kyle Mitchell ◽  
Bethan E. Phillips ◽  
John P. Williams ◽  
Debbie Rankin ◽  
Jonathan N. Lund ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Blood Flow ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Older Men ◽  
Essential Amino Acids ◽  
Low Amplitude ◽  
The Impact

Essential amino acids (EAA) are responsible for skeletal muscle anabolic effects after nutrient intake. The pattern of appearance of EAA in blood, e.g., after intake of “slow” or “fast” protein sources or in response to grazing vs. bolus feeding patterns, may impact anabolism. However, the influence of this on muscle anabolism is poorly understood, particularly in older individuals. We determined the effects of divergent feeding profiles of EAA on blood flow, anabolic signaling, and muscle protein synthesis (MPS) in older men. Sixteen men (∼70 yr) consumed EAA either as a single dose (bolus, 15 g; n = 8) or as small repeated fractions (pulse, 4 × 3.75 g every 45 min; n = 8) during 13C6 phenylalanine infusion. Repeated blood samples and muscle biopsies permitted measurement of fasting and postprandial plasma EAA, insulin, anabolic signaling, and MPS. Muscle blood flow was assessed by contrast-enhanced ultrasound (Sonovue). Bolus achieved rapid insulinemia (12.7 μiU/ml 25-min postfeed), essential aminoacidemia (∼3,000 μM, 45–65 min postfeed), and mTORC1 activity; pulse achieved attenuated insulin responses, gradual low-amplitude aminoacidemia (∼1,800 μM 80–195 min after feeding), and undetectable mTORC1 signaling. Despite this, equivalent anabolic responses were observed: fasting FSRs of 0.051 and 0.047%/h (bolus and pulse, respectively) increased to 0.084 and 0.073%/h, respectively. Moreover, pulse led to sustainment of MPS beyond 180 min, when bolus MPS had returned to basal rates. We detected no benefit of rapid aminoacidemia in this older population despite enhanced anabolic signaling and greater overall EAA exposure. Rather, apparent delayed onset of the “muscle-full” effect permitted identical MPS following low-amplitude-sustained EAA exposure.

The molecular basis of skeletal muscle atrophy

2004 ◽  
Vol 287 (4) ◽  
pp. C834-C843 ◽  
Author(s):  
Robert W. Jackman ◽  
Susan C. Kandarian
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Muscle Protein ◽  
Muscle Tension ◽  
Good Deal ◽  
Skeletal Muscle Atrophy ◽  
Molecular Signaling ◽  
Disuse Atrophy ◽  
Protein Loss ◽  
Ongoing Work

Skeletal muscle atrophy attributable to muscular inactivity has significant adverse functional consequences. While the initiating physiological event leading to atrophy seems to be the loss of muscle tension and a good deal of the physiology of muscle atrophy has been characterized, little is known about the triggers or the molecular signaling events underlying this process. Decreases in protein synthesis and increases in protein degradation both have been shown to contribute to muscle protein loss due to disuse, and recent work has delineated elements of both synthetic and proteolytic processes underlying muscle atrophy. It is also becoming evident that interactions among known proteolytic pathways (ubiquitin-proteasome, lysosomal, and calpain) are involved in muscle proteolysis during atrophy. Factors such as TNF-α, glucocorticoids, myostatin, and reactive oxygen species can induce muscle protein loss under specified conditions. Also, it is now apparent that the transcription factor NF-κB is a key intracellular signal transducer in disuse atrophy. Transcriptional profiles of atrophying muscle show both up- and downregulation of various genes over time, thus providing further evidence that there are multiple concurrent processes involved in muscle atrophy. The purpose of this review is to synthesize our current understanding of the molecular regulation of muscle atrophy. We also discuss how ongoing work should uncover more about the molecular underpinnings of muscle wasting, particularly that due to disuse.

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