Resistance exercise and nutrition to counteract muscle wasting

2009 ◽  
Vol 34 (5) ◽  
pp. 817-828 ◽  
Author(s):  
Jonathan P. Little ◽  
Stuart M. Phillips
Keyword(s):  
Protein Synthesis ◽  
Resistance Exercise ◽  
Muscle Mass ◽  
Muscle Wasting ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Effective Means ◽  
Resistance Exercise Training ◽  
Highly Effective

Loss of muscle mass is an unfavourable consequence of aging and many chronic diseases. The debilitating effects of muscle loss include declines in physical function and quality of life and increases in morbidity and mortality. Loss of muscle mass is the result of a decrease in muscle protein synthesis, an increase in muscle protein degradation, or a combination of both. Much research on muscle wasting has tended to focus on preventing muscle protein breakdown, and less attention has been paid to providing adequate stimulation to increase muscle protein synthesis. In this review, we present evidence to suggest that interventions aimed at increasing muscle protein synthesis represent the most effective countermeasure for preventing, delaying, or reversing the loss of skeletal muscle mass experienced in various muscle wasting conditions. Based on results from acute and chronic studies in humans in a wide variety of wasting conditions, we propose that resistance exercise training combined with appropriately timed protein (likely leucine-rich) ingestion represents a highly effective means to promote muscle hypertrophy, and may represent a highly effective treatment strategy to counteract the muscle wasting tassociated with aging and chronic disease.

Muscle Protein Metabolism in the Elderly: Influence of Exercise and Nutrition

2001 ◽  
Vol 26 (6) ◽  
pp. 588-606 ◽  
Author(s):  
Kevin D. Tipton
Keyword(s):  
Protein Synthesis ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Effective Means ◽  
The Elderly ◽  
Protein Breakdown ◽  
Small Magnitude ◽  
Muscle Protein Breakdown ◽  
Metabolic Basis

Although the causes of sarcopenia are multi-factorial, at least some, such as poor nutrition and inactivity, may be preventable. Changes in muscle mass must be a result of net muscle protein breakdown over that particular time period. Stable isotope methodology has been used to examine the metabolic basis of muscle loss. Net muscle protein breakdown may occur due to a decrease in the basal level of muscle protein synthesis. However, changes of this type would likely be of small magnitude and undetectable by current methodology. Hormonal mediators may also be important, especially in association with forced inactivity. Net muscle protein breakdown may be also attributed to alterations in the periods of net muscle protein synthesis and breakdown each day. Reduced activity, combined with ineffectual nutrient intake, could lead to decreased net muscle protein balance. Chronic resistance exercise training clearly is an effective means of increasing muscle mass and strength in elderly individuals. Although sometimes limited, acute metabolic studies provide valuable information for maintenance of muscle mass with age. Key words: sarcopenia, inactivity, strength training, muscle protein synthesis, muscle hypertrophy

scholarly journals The anabolic role of plant-based proteins in response to chronic resistance exercise

2021 ◽  
Vol 11 (3) ◽  
pp. 14-23
Author(s):  
Carina Sousa Santos ◽  
Eudes Souza Oliveira Júnior ◽  
Marcus James Lopes de Sá ◽  
Elizabethe Adriana Esteves
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Resistance Exercise ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
The Elderly ◽  
Food Sources ◽  
Dietary Adequacy ◽  
The Face

Proper maintenance of skeletal muscle mass is essential to prevent sarcopenia and ensure health and quality of life as aging progress. The two determinants of muscle protein synthesis are the increased load on skeletal muscle through resistance exercise and protein intake. For an effective result of maintaining or increasing muscle mass, it is relevant to consider the quantitative and adequate intake of protein, and the dietary source of protein since the plant-based protein has differences in comparison to animals that limit its anabolic capacity. Given the increase in vegetarianism and the elderly population, which consumes fewer food sources of animal protein, the importance of understanding how protein of plant-based protein can sustain muscle protein synthesis in the long term when associated with resistance exercise is justified, as well as the possibilities of dietary adequacy in the face of this demand.

Cumulative responses of muscle protein synthesis are augmented with chronic resistance exercise training

2010 ◽  
Vol 201 (3) ◽  
pp. 381-389 ◽  
Author(s):  
H. G. Gasier ◽  
S. E. Riechman ◽  
M. P. Wiggs ◽  
A. Buentello ◽  
S. F. Previs ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Exercise Training ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Resistance Exercise Training

Gaining Weight: The Scientific Basis of Increasing Skeletal Muscle Mass

1999 ◽  
Vol 24 (4) ◽  
pp. 305-316 ◽  
Author(s):  
Michael E. Houston
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Resistance Exercise ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Recovery Period ◽  
Scientific Basis ◽  
Whole Body ◽  
Anabolic Hormone

Most athletes today tend to have a larger muscle mass than their predecessors. Better training and nutrition practices are responsible for much of this difference, but whatever the mechanism, the balance between muscle protein synthesis and breakdown must be in favor of increased muscle protein. Applying new techniques for measuring whole body and muscle protein synthesis to resistance exercise has led to some interesting results. In the recovery period following resistance exercise, both muscle protein synthesis and breakdown are accelerated in the fasted state. Ingestion of carbohydrate or carbohydrate and protein during recovery further increases muscle protein synthesis, due in part to an improved anabolic hormone environment. In addition, the anabolic effect of a resistance training bout may last well beyond 48 hours. Using information obtained from research studies, better training and dietary practices can optimize the benefits from resistance training, Key words: protein synthesis, protein breakdown, anabolic hormones, nutrition, resistance training

scholarly journals Muscle Protein Synthesis and Muscle/Metabolic Responses To Resistance Exercise Training in South Asian and White European Men

2021 ◽  
Author(s):  
Faris Alkhayl ◽  
Ahmad Ismail ◽  
Carlos Celis-Morales ◽  
John Wilson ◽  
Aleksandra Radjenovic ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Exercise Training ◽  
Resistance Exercise ◽  
South Asian ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
South Asians ◽  
Metabolic Responses ◽  
Resistance Exercise Training ◽  
Free Living

Abstract PurposeThe aims of the current study, therefore, were to compare 1) free-living MPS and 2) muscle and metabolic adaptations to resistance exercise in South Asian and white European adults.MethodsEighteen South Asian and 16 White European men were enrolled in the study. Free-living muscle protein synthesis was measured at baseline. Muscle strength, body composition, resting metabolic rate, VO2max and metabolic responses (insulin sensitivity) to a mixed meal were measured at baseline and following 12 weeks of resistance exercise training. Results Free-living muscle protein synthesis was not different between South Asians (1.48 ± 0.09 %/day) and White Europeans (1.59 ± 0.15 %/day) (p=0.522). In response to resistance exercise training there were no differences, between South Asians and White Europeans, muscle mass, lower body strength or insulin sensitivity. However, there were differences between the ethnicities in response to resistance exercise training in body fat, resting carbohydrate and fat metabolism, blood pressure, VO2max and upper body strength with responses less favourable in South Asians. ConclusionIn this exploratory study there were no differences in muscle protein synthesis or anabolic and metabolic responses to resistance exercise, yet there were less favourable responses in several outcomes. These findings require further investigation.

scholarly journals Methylarginine metabolites are associated with attenuated muscle protein synthesis in cancer-associated muscle wasting

2020 ◽  
Vol 295 (51) ◽  
pp. 17441-17459
Author(s):  
Hawley E. Kunz ◽  
Jessica M. Dorschner ◽  
Taylor E. Berent ◽  
Thomas Meyer ◽  
Xuewei Wang ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Mass ◽  
Cancer Cachexia ◽  
Muscle Wasting ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Mitochondrial Protein ◽  
Coupling Efficiency ◽  
C2c12 Myotubes ◽  
Tumor Bearing

Cancer cachexia is characterized by reductions in peripheral lean muscle mass. Prior studies have primarily focused on increased protein breakdown as the driver of cancer-associated muscle wasting. Therapeutic interventions targeting catabolic pathways have, however, largely failed to preserve muscle mass in cachexia, suggesting that other mechanisms might be involved. In pursuit of novel pathways, we used untargeted metabolomics to search for metabolite signatures that may be linked with muscle atrophy. We injected 7-week–old C57/BL6 mice with LLC1 tumor cells or vehicle. After 21 days, tumor-bearing mice exhibited reduced body and muscle mass and impaired grip strength compared with controls, which was accompanied by lower synthesis rates of mixed muscle protein and the myofibrillar and sarcoplasmic muscle fractions. Reductions in protein synthesis were accompanied by mitochondrial enlargement and reduced coupling efficiency in tumor-bearing mice. To generate mechanistic insights into impaired protein synthesis, we performed untargeted metabolomic analyses of plasma and muscle and found increased concentrations of two methylarginines, asymmetric dimethylarginine (ADMA) and NG-monomethyl-l-arginine, in tumor-bearing mice compared with control mice. Compared with healthy controls, human cancer patients were also found to have higher levels of ADMA in the skeletal muscle. Treatment of C2C12 myotubes with ADMA impaired protein synthesis and reduced mitochondrial protein quality. These results suggest that increased levels of ADMA and mitochondrial changes may contribute to impaired muscle protein synthesis in cancer cachexia and could point to novel therapeutic targets by which to mitigate cancer cachexia.

Insulin facilitation of muscle protein synthesis following resistance exercise in hindlimb-suspended rats is independent of a rapamycin-sensitive pathway

2004 ◽  
Vol 287 (6) ◽  
pp. E1070-E1075 ◽  
Author(s):  
James D. Fluckey ◽  
Esther E. Dupont-Versteegden ◽  
Micheal Knox ◽  
Dana Gaddy ◽  
Per A. Tesch ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Exercise ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Mammalian Target Of Rapamycin ◽  
Exercise Bout ◽  
Hindlimb Suspension ◽  
Sprague Dawley

Hindlimb suspension (HS) results in rapid losses of muscle mass, which may in part be explained by attenuated rates of protein synthesis. Mammalian target of rapamycin (mTOR) regulates protein synthesis and has been implicated as a potential mediator of the muscle mass decrement with HS. This study examined the effect of resistance exercise, a muscle hypertrophy stimulant, on rates of protein synthesis after 4 days of HS in mature male Sprague-Dawley rats. Flywheel resistance exercise (2 sets × 25 repetitions) was conducted on days 2 and 4 of HS (HSRE). Sixteen hours after the last exercise bout, soleus muscles were assessed for in vitro rates of protein synthesis, with and without insulin (signaling agonist) and/or rapamycin (mTOR inhibitor). Results demonstrated that soleus mass was reduced ( P < 0.05) with HS, but this loss of mass was not observed ( P > 0.05) with HSRE. Muscle protein synthesis was diminished ( P < 0.05) with HS, with or without insulin. HSRE also had reduced rates of synthesis without insulin; however, insulin administration yielded higher ( P < 0.05) rates in HSRE compared with HS or control. Rapamycin diminished protein synthesis in all groups ( P < 0.05), but insulin rescued synthesis rates in HS and HSRE to levels similar to insulin alone for each group, suggesting that alternate signaling pathways develop to increase protein synthesis with HS. These results demonstrate that the capacity for an augmented anabolic response to resistance exercise is maintained after 4 days of HS and is independent of a rapamycin-sensitive pathway.

scholarly journals Resistance exercise training increases mixed muscle protein synthesis rate in frail women and men ≥76 yr old

1999 ◽  
Vol 277 (1) ◽  
pp. E118-E125 ◽  
Author(s):  
Kevin E. Yarasheski ◽  
Jina Pak-Loduca ◽  
Debbie L. Hasten ◽  
Kathleen A. Obert ◽  
Mary Beth Brown ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Exercise Training ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Weight Lifting ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Resistance Exercise Training

Muscle atrophy (sarcopenia) in the elderly is associated with a reduced rate of muscle protein synthesis. The purpose of this study was to determine if weight-lifting exercise increases the rate of muscle protein synthesis in physically frail 76- to 92-yr-old women and men. Eight women and 4 men with mild to moderate physical frailty were enrolled in a 3-mo physical therapy program that was followed by 3 mo of supervised weight-lifting exercise. Supervised weight-lifting exercise was performed 3 days/wk at 65–100% of initial 1-repetition maximum on five upper and three lower body exercises. Compared with before resistance training, the in vivo incorporation rate of [13C]leucine into vastus lateralis muscle protein was increased after resistance training in women and men ( P < 0.01), although it was unchanged in five 82 ± 2-yr-old control subjects studied two times in 3 mo. Maximum voluntary knee extensor muscle torque production increased in the supervised resistance exercise group. These findings suggest that muscle contractile protein synthetic pathways in physically frail 76- to 92-yr-old women and men respond and adapt to the increased contractile activity associated with progressive resistance exercise training.

Acute effects of resistance exercise on muscle protein synthesis rate in young and elderly men and women

1993 ◽  
Vol 265 (2) ◽  
pp. E210-E214 ◽  
Author(s):  
K. E. Yarasheski ◽  
J. J. Zachwieja ◽  
D. M. Bier
Keyword(s):  
Protein Synthesis ◽  
Exercise Training ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
The Elderly ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Breakdown ◽  
Resistance Exercise Training

Muscle mass and function are improved in the elderly during resistance exercise training. These improvements must result from alterations in the rates of muscle protein synthesis and breakdown. We determined the rate of quadriceps muscle protein synthesis using the in vivo rate of incorporation of intravenously infused [13C]leucine into mixed-muscle protein in both young (24 yr) and elderly (63-66 yr) men and women before and at the end of 2 wk of resistance exercise training. Before training, the fractional rate of muscle protein synthesis was lower in the elderly than in the young (0.030 +/- 0.003 vs. 0.049 +/- 0.004%/h; P = 0.004) but increased (P < 0.03) to a comparable rate of muscle protein synthesis in both young (0.075 +/- 0.009%/h) and elderly subjects (0.076 +/- 0.011%/h) after 2 wk of exercise. In the elderly, muscle mass, 24-h urinary 3-methylhistidine and creatinine excretion, and whole body protein breakdown rate determined during the [13C]leucine infusion were not changed after 2 wk of exercise. These findings demonstrate that, during the initial phase of a resistance exercise training program, a marked increase in quadriceps muscle protein synthesis rate occurs in elderly and young adults without an increase in the rate of whole body protein breakdown. In the elderly, this was not accompanied by an increase in urinary 3-methylhistidine excretion, an index of myofibrillar protein breakdown.

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