scholarly journals Unaffected Arm Muscle Hypercatabolism in Dysphagic Subacute Stroke Patients: The Effects of Essential Amino Acid Supplementation

2014 ◽  
Vol 2014 ◽  
pp. 1-17 ◽  
Author(s):  
Roberto Aquilani ◽  
Mirella Boselli ◽  
Giuseppe D’Antona ◽  
Paola Baiardi ◽  
Federica Boschi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Essential Amino Acids ◽  
Amino Acid Supplementation ◽  
Stroke Patients ◽  
Unaffected Side ◽  
Stroke Population ◽  
Subacute Stroke

Alterations in muscle protein turnover of the unaffected side of stroke patients could contribute to physical disability. We investigated whether hypercatabolic activity occurred in unaffected arm muscle and whether supplemented essential amino acids (EAAs) could limit muscle hypercatabolism (MH). Thirty-eight dysphagic subacute stroke subjects (<3 months after acute event) (29 males + 9 females; 69.7 ± 11.4 yrs) were enrolled and randomized to receive 8 g/day EAAs (n= 19; EAA group) or isocaloric placebo (maltodextrin;n= 19, Plac group). Before randomization, all patients had their arterial (A) and venous (V) amino acids measured and muscle (A − V) differences calculated in the unaffected arm. Eight matched and healthy subjects served as controls. When compared to healthy controls, the entire stroke population showed significant muscle release (= negative value A − V) of the amino acid phenylalanine (phenyl-) indicating a prevalence of MH. Moreover, randomized EAA and Plac groups had similar rates of MH. After 38 days from the start of the protocol, the EAA group but not the Plac group had MH converted to balanced protein turnover or anabolic activity. We concluded that muscle protein metabolism of the unaffected arm of dysphagic subacute stroke individuals could be characterized by MH which can be corrected by supplemented EAAs.

Influence of fatty acids on ammonia and amino acid flux from active human muscle

1991 ◽  
Vol 261 (2) ◽  
pp. E168-E176 ◽  
Author(s):  
T. E. Graham ◽  
B. Kiens ◽  
M. Hargreaves ◽  
E. A. Richter
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Muscle Protein ◽  
Knee Extensor ◽  
Essential Amino Acids ◽  
Order Effect ◽  
Work Capacity ◽  
Human Muscle ◽  
Control Series ◽  
Ammonia Release

This study examined the dynamics of ammonia and amino acid exchange of human muscle during prolonged steady-state one-legged exercise at 80% of knee extensor maximal work capacity. Subjects (n = 10) performed leg extensor exercise for 1 h (control series), rested for 40 min while an infusion of Intralipid and heparin was begun, and then exercised the contralateral leg with the identical protocol [free fatty acid (FFA) series]. In the control series, ammonia efflux rose progressively, and 4.4 +/- 0.6 mmol were released in 1 h compared with 2.4 +/- 0.5 mmol (P less than 0.05) in the FFA series. The exercise was associated with large effluxes of total amino acids from the active muscle over the hour (12.8 +/- 4.3 and 10.3 +/- 3.3 mmol for control and FFA, respectively). Glutamine and alanine accounted for 47 and 64% of the efflux for the control and FFA series, respectively, while comparable values for essential amino acids were 24 and 20%. The latter implies that a net muscle protein catabolism was occurring during the exercise. The FFA treatment was associated not only with a reduced muscle ammonia release but also with a decreased (P less than 0.05) arterial concentration of nine amino acids (alanine, methionine, lysine, hydroxyproline, serine, glycine, proline, asparagine, and ornithine). Interpretation is limited due to the treatment order effect, but these data are compatible with the hypothesis that plasma clearance was affected by FFA.

scholarly journals Use of plasma-free amino acids as biomarkers for detecting and predicting disease risk

2020 ◽  
Vol 78 (Supplement_3) ◽  
pp. 79-85
Author(s):  
Kenji Nagao ◽  
Takeshi Kimura
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino ◽  
Disease Risk ◽  
The Elderly ◽  
Essential Amino Acids ◽  
Clinical Findings ◽  
Amino Acid Supplementation ◽  
Diabetes Prediction ◽  
Plasma Free Amino Acids

Abstract This paper reviews developments regarding the use of plasma-free amino acid (PFAA) profiles as biomarkers for detecting and predicting disease risk. This work was initiated and first published in 2006 and was subsequently developed by Ajinomoto Co., Inc. After commercialization in 2011, PFAA-based tests were adopted in over 1500 clinics and hospitals in Japan, and numerous clinician-led studies have been performed to validate these tests. Evidence is accumulating that PFAA profiles can be used for diabetes prediction and evaluation of frailty; in particular, decreased plasma essential amino acids could contribute to the pathophysiology of severe frailty. Integration of PFAA evaluation as a biomarker and effective essential amino acid supplementation, which improves physical and mental functions in the elderly, could facilitate the development of precision nutrition, including personalized solutions. This present review provides the background for the technology as well as more recent clinical findings, and offers future possibilities regarding the implementation of precision nutrition.

High protein wheats for poultry. 1. Use in broiler diets

1971 ◽  
Vol 11 (53) ◽  
pp. 619 ◽  
Author(s):  
W Turner ◽  
GG Payne
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Amino Acid ◽  
Crude Protein ◽  
Maximum Level ◽  
Essential Amino Acids ◽  
High Protein ◽  
Amino Acid Supplementation ◽  
Dietary Factor ◽  
Protein Diets

High protein wheat was the sole cereal in 20 and 25 per cent crude protein broiler starter diets. On the. 25 per cent protein diet, performance was maximized without amino acid supplementation. Using high protein wheat in 20 per cent protein diets, growth rate was improved by l-lysine supplementation of 0.3 per cent. However, this growth rate was not at a maximum level. Some other dietary factor was necessary, and this did not appear to be essential amino acids, singly or in combination.

scholarly journals Advantages and limitations of the protein digestibility-corrected amino acid score (PDCAAS) as a method for evaluating protein quality in human diets

2012 ◽  
Vol 108 (S2) ◽  
pp. S333-S336 ◽  
Author(s):  
Gertjan Schaafsma
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Protein Digestibility ◽  
Essential Amino Acids ◽  
Tissue Growth ◽  
Biological Efficiency ◽  
Amino Acid Supplementation ◽  
Reference Pattern ◽  
Plant Protein Sources

PDCAAS is a widely used assay for evaluating protein quality. It is a chemical score, which is derived from the ratio between the first limiting amino acid in a test protein and the corresponding amino acid in a reference amino acid pattern and corrected for true faecal N digestibility. Chemical scores exceeding 100 % are truncated to 100 %. The advantages of the PDCAAS are its simplicity and direct relationship to human protein requirements. The limitations are as follows: the reference pattern is based on the minimum amino acid requirements for tissue growth and maintenance and does not necessarily reflect the optimum intake. Truncated PDCAAS of high-quality proteins do not give any information about the power of these proteins to compensate, as a supplement, for low levels of dietary essential amino acids in low-quality proteins. It is likely that faecal N digestibility does not take into account the loss from the colon of indispensable amino acids that were not absorbed in the ileum. Anti-nutritional factors, such as lectins and trypsin inhibitors, in several plant protein sources can cause heightened endogenous losses of amino acids, an issue which is particularly relevant in animal feedstuffs. The assumption that amino acid supplementation can completely restore biological efficiency of the protein source is incorrect since the kinetics of digestion and absorption between supplemented free amino acids and amino acids present in dietary proteins, are different.

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 Myostatin Inhibition-Induced Increase in Muscle Mass and Strength Was Amplified by Resistance Exercise Training, and Dietary Essential Amino Acids Improved Muscle Quality in Mice

Nutrients ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 1508
Author(s):  
Jiwoong Jang ◽  
Sanghee Park ◽  
Yeongmin Kim ◽  
Jiyeon Jung ◽  
Jinseok Lee ◽  
...  
Keyword(s):  
Amino Acids ◽  
Muscle Mass ◽  
Mitochondrial Biogenesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Essential Amino Acids ◽  
Muscle Quality ◽  
Resistance Exercise Training ◽  
Muscle Protein Turnover ◽  
Myostatin Inhibition

It has been frequently reported that myostatin inhibition increases muscle mass, but decreases muscle quality (i.e., strength/muscle mass). Resistance exercise training (RT) and essential amino acids (EAAs) are potent anabolic stimuli that synergistically increase muscle mass through changes in muscle protein turnover. In addition, EAAs are known to stimulate mitochondrial biogenesis. We have investigated if RT amplifies the anabolic potential of myostatin inhibition while EAAs enhance muscle quality through stimulations of mitochondrial biogenesis and/or muscle protein turnover. Mice were assigned into ACV (myostatin inhibitor), ACV+EAA, ACV+RT, ACV+EAA +RT, or control (CON) over 4 weeks. RT, but not EAA, increased muscle mass above ACV. Despite differences in muscle mass gain, myofibrillar protein synthesis was stimulated similarly in all vs. CON, suggesting a role for changes in protein breakdown in muscle mass gains. There were increases in MyoD expression but decreases in Atrogin-1/MAFbx expression in ACV+EAA, ACV+RT, and ACV+EAA+RT vs. CON. EAA increased muscle quality (e.g., grip strength and maximal carrying load) without corresponding changes in markers of mitochondrial biogenesis and neuromuscular junction stability. In conclusion, RT amplifies muscle mass and strength through changes in muscle protein turnover in conjunction with changes in implicated signaling, while EAAs enhance muscle quality through unknown mechanisms.

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 Order of amino acid inclusion in the diet of DeKalb White laying hens

2016 ◽  
Vol 37 (3) ◽  
pp. 1539 ◽  
Author(s):  
Danilo Vargas Gonçalves Vieira ◽  
Thiago De Sousa Melo ◽  
José Humberto Vilar da Silva ◽  
Fernando Guilherme Perazzo Costa ◽  
Danilo Teixeira Cavalcante ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crude Protein ◽  
Egg Production ◽  
Laying Hens ◽  
Essential Amino Acids ◽  
Control Treatment ◽  
Amino Acid Supplementation ◽  
Haugh Unit

Three hundred and twenty-four DeKalb White laying hens aged 42 weeks were distributed in a completely randomised design with nine treatments and six replicates of six birds in each treatment. The experiment lasted 112 days. Diets were: T1 = 16.02% crude protein - CP [Met + Lys + Thr + Trp + Val]; T2 = 14.02% CP [Met + Lys + Thr + Trp + Ile + Val]; T3 = 14.02% CP [no amino acid supplementation]; T4 = 14.02% CP [Met + Lys + Thr + Trp]; T5 = 14.02% CP [Met + Lys + Thr]; T6 = 14.02% CP [Met]; T7 = 14.02% CP [Lys]; T8 = 14.02% CP [Thr]; T9 = 14.02% CP [Trp]. Regarding the quality of the eggs, the percentage of yolk and albumen, shell thickness and Haugh unit were not affected by the different diets. The percentage of shell, specific gravity and albumen height showed significant differences. We found that supplementation of only one amino acid in the diet (T7, T8 or T9), with the exception of methionine (T6), worsened performance relative to the control. Supplementation of three amino acids (methionine, lysine and threonine; T5) or four amino acids (methionine, lysine, threonine and tryptophan; T4) worsened egg production and conversion per mass and per dozen eggs; however, feed intake and egg weight and mass were similar to the control treatment. When all amino acids (methionine, lysine, threonine, tryptophan, isoleucine and valine; T2) were supplemented performance was similar to the control treatment in all variables. Supplementation of methionine, lysine and threonine is essential for birds in the laying phase; however the addition of six essential amino acids (lysine, methionine, threonine, tryptophan, valine and isoleucine) to the diet of laying hens is important for a good productive performance comparable with the control treatment T1. However, the inclusion of the latter two (isoleucine and valine) is justified only if the production cost is lower.

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.

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