scholarly journals The Role of the Anabolic Properties of Plant- versus Animal-Based Protein Sources in Supporting Muscle Mass Maintenance: A Critical Review

Nutrients ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 1825 ◽  
Author(s):  
Insaf Berrazaga ◽  
Valérie Micard ◽  
Marine Gueugneau ◽  
Stéphane Walrand
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Intake ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Essential Amino Acids ◽  
Protein Sources ◽  
Nutritional Strategies

Plant-sourced proteins offer environmental and health benefits, and research increasingly includes them in study formulas. However, plant-based proteins have less of an anabolic effect than animal proteins due to their lower digestibility, lower essential amino acid content (especially leucine), and deficiency in other essential amino acids, such as sulfur amino acids or lysine. Thus, plant amino acids are directed toward oxidation rather than used for muscle protein synthesis. In this review, we evaluate the ability of plant- versus animal-based proteins to help maintain skeletal muscle mass in healthy and especially older people and examine different nutritional strategies for improving the anabolic properties of plant-based proteins. Among these strategies, increasing protein intake has led to a positive acute postprandial muscle protein synthesis response and even positive long-term improvement in lean mass. Increasing the quality of protein intake by improving amino acid composition could also compensate for the lower anabolic potential of plant-based proteins. We evaluated and discussed four nutritional strategies for improving the amino acid composition of plant-based proteins: fortifying plant-based proteins with specific essential amino acids, selective breeding, blending several plant protein sources, and blending plant with animal-based protein sources. These nutritional approaches need to be profoundly examined in older individuals in order to optimize protein intake for this population who require a high-quality food protein intake to mitigate age-related muscle loss.

scholarly journals Postexercise net protein synthesis in human muscle from orally administered amino acids

1999 ◽  
Vol 276 (4) ◽  
pp. E628-E634 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando ◽  
Stuart M. Phillips ◽  
David Doyle ◽  
Robert R. Wolfe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Random Order ◽  
Essential Amino Acids ◽  
Constant Infusion ◽  
Protein Balance

We examined the response of net muscle protein synthesis to ingestion of amino acids after a bout of resistance exercise. A primed, constant infusion ofl-[ ring-2H5]phenylalanine was used to measure net muscle protein balance in three male and three female volunteers on three occasions. Subjects consumed in random order 1 liter of 1) a mixed amino acid (40 g) solution (MAA), 2) an essential amino acid (40 g) solution (EAA), and 3) a placebo solution (PLA). Arterial amino acid concentrations increased ∼150–640% above baseline during ingestion of MAA and EAA. Net muscle protein balance was significantly increased from negative during PLA ingestion (−50 ± 23 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) to positive during MAA ingestion (17 ± 13 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) and EAA (29 ± 14 nmol ⋅ min−1 ⋅ 100 ml leg volume−1; P < 0.05). Because net balance was similar for MAA and EAA, it does not appear necessary to include nonessential amino acids in a formulation designed to elicit an anabolic response from muscle after exercise. We concluded that ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused.

scholarly journals Role of specific dietary amino acids in clinical conditions

2012 ◽  
Vol 108 (S2) ◽  
pp. S139-S148 ◽  
Author(s):  
Renate Jonker ◽  
Mariëlle P. K. J. Engelen ◽  
Nicolaas E. P. Deutz
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Wasting ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Essential Amino Acids ◽  
Dietary Proteins ◽  
Disease States ◽  
Stimulation Of

In a variety of chronic and acute disease states, alterations in protein synthesis, breakdown and protein turnover rates occur that are related to the loss of body protein and skeletal muscle wasting. A key observation is the stimulation of protein breakdown in muscle and the stimulation of protein synthesis in the splanchnic area; mainly liver. An altered splanchnic extraction of amino acids as well as an anabolic resistance to dietary protein, related to stress, disuse and aging play a key role in the pathogenesis of muscle wasting in these conditions. To overcome these factors, specific dietary protein and amino acid diets have been introduced. The main focus of these diets is the quantity and quality of dietary proteins and whether a balanced mixture or solely dietary essential amino acids are required with or without higher intake levels of specific amino acids. Specifically in cancer patients, stimulated muscle protein synthesis has been obtained by increasing the amount of protein in a meal and by providing additional leucine. Also in other chronic diseases such as chronic obstructive pulmonary disease and cystic fibrosis, meals with specific dietary proteins and specific combinations of dietary essential amino acids are able to stimulate anabolism. In acute diseases, a special role for the amino acid arginine and its precursor citrulline as anabolic drivers has been observed. Thus, there is growing evidence that modifying the dietary amino acid composition of a meal will positively influence the net balance between muscle protein synthesis and breakdown, leading to muscle protein anabolism in a variety of chronic and acute disease states. Specific amino acids with anabolic potential are leucine, arginine and citrulline.

scholarly journals Příjem bílkovin po odporovém tréninku a svalová hypertrofie (přehledová práce)

2015 ◽  
Vol 9 (2) ◽  
pp. 100-106
Author(s):  
Michal Richter ◽  
Michal Kumstát
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Whey Protein ◽  
Protein Intake ◽  
Muscle Hypertrophy ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Essential Amino Acids ◽  
Factors Affecting ◽  
Key Factor

Protein intake and resistance training are factors affecting the rate of muscle protein synthesis. Muscle hypertrophy manifests as a result of a positive protein balance between the rate of muscle protein synthesis and muscle protein breakdown. An intake of protein containing essential amino acids in the period after the resistance exercise is a key prerequisite of an effective adaptation. Postprandial hyperaminoacidemia is a key factor in the effectiveness of proteosynthetic processes. The most common types of protein used in sports nutrition include milk protein, egg and soy protein. There are significant differences among them in the context of digestion and essential amino acids resorptio kinetics. Whey protein represents due to the high content of essential amino acids and leucine a superior source and is considered an important anabolic stimuli. An amount of ~20–25 g of whey protein consumed after restistance exercise optimizes conditions for muscle hypertrophy. Appropriate timing of protein intake in close proximity to the load positively affects an athletes attempt to achieve muscle hypertrophy.

Effects of Amino Acid Intake on Anabolic Processes

2001 ◽  
Vol 26 (S1) ◽  
pp. S220-S227 ◽  
Author(s):  
Robert R. Wolfe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Essential Amino Acids ◽  
Negative Resistance ◽  
Static Concentration ◽  
Amino Acid Intake ◽  
Modest Effect

In the resting state muscle protein breakdown exceeds the rate of muscle protein synthesis, meaning that the balance between synthesis and breakdown is negative. Resistance exercise improves the net balance by stimulating muscle protein synthesis, but nutrient intake is requiredfor synthesis to exceed breakdown (i.e., an anabolic response). Exercise and exogenous amino acids have an additive effect on muscle protein synthesis. There is a timecourse of the response to a steady-state change in amino acid concentration. The signal for stimulation of muscle protein synthesis appears to be the extracellular concentrations of one or more of the essential amino acids (EAAs). Further, the rate , and direction, of change in extracellular concentrations (rather than the static concentration, per se) may be the important. Ingestion of non-essential AAs is not needed to stimulate muscle protein synthesis. Carbohydrate has, at most, a modest effect to enhance the response to amino acid ingestion after exercise. Finally, a mixture of EAAs + CRO more effectively stimulates muscle protein synthesis when taken before as opposed to after exercise.

scholarly journals An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise

2000 ◽  
Vol 88 (2) ◽  
pp. 386-392 ◽  
Author(s):  
Blake B. Rasmussen ◽  
Kevin D. Tipton ◽  
Sharon L. Miller ◽  
Steven E. Wolf ◽  
Robert R. Wolfe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Venous Blood ◽  
Compartment Model ◽  
Essential Amino Acids

This study was designed to determine the response of muscle protein to the bolus ingestion of a drink containing essential amino acids and carbohydrate after resistance exercise. Six subjects (3 men, 3 women) randomly consumed a treatment drink (6 g essential amino acids, 35 g sucrose) or a flavored placebo drink 1 h or 3 h after a bout of resistance exercise on two separate occasions. We used a three-compartment model for determination of leg muscle protein kinetics. The model involves the infusion of ring-2H5-phenylalanine, femoral arterial and venous blood sampling, and muscle biopsies. Phenylalanine net balance and muscle protein synthesis were significantly increased above the predrink and corresponding placebo value ( P < 0.05) when the drink was taken 1 or 3 h after exercise but not when the placebo was ingested at 1 or 3 h. The response to the amino acid-carbohydrate drink produced similar anabolic responses at 1 and 3 h. Muscle protein breakdown did not change in response to the drink. We conclude that essential amino acids with carbohydrates stimulate muscle protein anabolism by increasing muscle protein synthesis when ingested 1 or 3 h after resistance exercise.

scholarly journals The Anabolic Response to Plant-Based Protein Ingestion

2021 ◽  
Author(s):  
Philippe J. M. Pinckaers ◽  
Jorn Trommelen ◽  
Tim Snijders ◽  
Luc J. C. van Loon
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Content ◽  
Protein Source ◽  
Protein Sources

AbstractThere 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.

An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein

1997 ◽  
Vol 273 (1) ◽  
pp. E122-E129 ◽  
Author(s):  
G. Biolo ◽  
K. D. Tipton ◽  
S. Klein ◽  
R. R. Wolfe
Keyword(s):  
Amino Acids ◽  
Blood Flow ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Protein Kinetics ◽  
Amino Acid Infusion

Six normal untrained men were studied during the intravenous infusion of a balanced amino acid mixture (approximately 0.15 g.kg-1.h-1 for 3 h) at rest and after a leg resistance exercise routine to test the influence of exercise on the regulation of muscle protein kinetics by hyperaminoacidemia. Leg muscle protein kinetics and transport of selected amino acids (alanine, phenylalanine, leucine, and lysine) were isotopically determined using a model based on arteriovenous blood samples and muscle biopsy. The intravenous amino acid infusion resulted in comparable increases in arterial amino acid concentrations at rest and after exercise, whereas leg blood flow was 64 +/- 5% greater after exercise than at rest. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest. Increases in muscle protein synthesis were also greater after exercise than at rest (291 +/- 42% vs. 141 +/- 45%). Muscle protein breakdown was not significantly affected by hyperminoacidemia either at rest or after exercise. We conclude that the stimulatory effect of exogenous amino acids on muscle protein synthesis is enhanced by prior exercise, perhaps in part because of enhanced blood flow. Our results imply that protein intake immediately after exercise may be more anabolic than when ingested at some later time.

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