Effects of flooding amino acids on incorporation of labeled amino acids into human muscle protein

1998 ◽  
Vol 275 (1) ◽  
pp. E73-E78 ◽  
Author(s):  
Kenneth Smith ◽  
Nigel Reynolds ◽  
Shaun Downie ◽  
Ayyub Patel ◽  
Michael J. Rennie
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Large Dose ◽  
Human Skeletal Muscle ◽  
Muscle Protein ◽  
Human Muscle ◽  
Leucine Incorporation ◽  
Nonessential Amino Acids ◽  
Stimulation Of

We investigated the effects of the nature of the flooding amino acid on the rate of incorporation of tracer leucine into human skeletal muscle sampled by biopsy. Twenty-three healthy young men (24.5 ± 5.0 yr, 76.2 ± 8.3 kg) were studied in groups of four or five. First, the effects of flooding with phenylalanine, threonine, or arginine (all at 0.05 g/kg body wt) on the incorporation of tracer [13C]leucine were studied. Then the effects of flooding with labeled [13C]glycine [0.1 g/kg body wt, 20 atoms percent excess (APE)] and [13C]serine (0.05 g/kg body wt, 15 APE) on the incorporation of simultaneously infused [13C]leucine were investigated. When a large dose of phenylalanine or threonine was administered, incorporation of the tracer leucine was significantly increased (from 0.036 to 0.067 %/h and 0.037 to 0.070 %/h, respectively; each P < 0.01). However, when arginine, glycine, or serine was administered as a flooding dose, no stimulation of tracer leucine incorporation could be observed. These results, together with those previously obtained, suggest that large doses of individual essential, but not nonessential, amino acids are able to stimulate incorporation of constantly infused tracer amino acids into human muscle protein.

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.

Measurement of protein synthesis in human skeletal muscle: further investigation of the flooding technique

1991 ◽  
Vol 81 (s25) ◽  
pp. 557-564 ◽  
Author(s):  
M. A. McNurlan ◽  
P. Essen ◽  
S. D. Heys ◽  
V. Buchan ◽  
P. J. Garlick ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Continuous Infusion ◽  
Healthy Subjects ◽  
Human Skeletal Muscle ◽  
Quadriceps Muscle ◽  
Mean Difference ◽  
Good Agreement ◽  
Stimulation Of

1. The rate of protein synthesis in quadriceps muscle of healthy subjects estimated from the incorporation of l-[1-13C]leucine given by continuous infusion was 1.1%/day. The estimate of protein synthesis from the incorporation of a flooding amount of labelled leucine was 1.8%/day (sd 0.65). The possibility that the higher rate obtained with the flooding technique arose from stimulation of protein synthesis by the large amount of leucine is unlikely. 2. The same rate of protein synthesis (1.7%/day, sd 0.3) was obtained with a flooding amount (0.05 g/kg) of a different amino acid, l-[1-13C]phenylalanine, as was obtained with leucine. 3. Incorporation of l-[1-13C]phenylalanine was not affected by simultaneous injection of leucine (1.7%/day, sd 0.7) or valine (1.6%/day, sd 0.4). 4. Protein synthesis, assessed in a completely different way from the proportion of polyribosomes isolated from the skeletal muscle, was unaltered by the injection of 0.05 g of l-leucine/kg (44.6%, sd 8.5 versus 43.8%, sd 7.7). 5. Good agreement in estimates of protein synthesis was observed in subjects in whom both legs were measured with both l-[1-13C]leucine (mean difference 0.16%/day) and l-[1-13C]phenylalanine (mean difference 0.2%/day).

scholarly journals Testosterone injection stimulates net protein synthesis but not tissue amino acid transport

1998 ◽  
Vol 275 (5) ◽  
pp. E864-E871 ◽  
Author(s):  
Arny A. Ferrando ◽  
Kevin D. Tipton ◽  
David Doyle ◽  
Stuart M. Phillips ◽  
Joaquin Cortiella ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Acid Transport ◽  
Skeletal Muscle Protein ◽  
Net Protein

Testosterone administration (T) increases lean body mass and muscle protein synthesis. We investigated the effects of short-term T on leg muscle protein kinetics and transport of selected amino acids by use of a model based on arteriovenous sampling and muscle biopsy. Fractional synthesis (FSR) and breakdown (FBR) rates of skeletal muscle protein were also directly calculated. Seven healthy men were studied before and 5 days after intramuscular injection of 200 mg of testosterone enanthate. Protein synthesis increased twofold after injection ( P < 0.05), whereas protein breakdown was unchanged. FSR and FBR calculations were in accordance, because FSR increased twofold ( P < 0.05) without a concomitant change in FBR. Net balance between synthesis and breakdown became more positive with both methodologies ( P< 0.05) and was not different from zero. T injection increased arteriovenous essential and nonessential nitrogen balance across the leg ( P < 0.05) in the fasted state, without increasing amino acid transport. Thus T administration leads to an increased net protein synthesis and reutilization of intracellular amino acids in skeletal muscle.

Prolonged incubation of skeletal muscle increases system A amino acid transport

1991 ◽  
Vol 260 (1) ◽  
pp. C88-C95 ◽  
Author(s):  
E. A. Gulve ◽  
G. D. Cartee ◽  
J. H. Youn ◽  
J. O. Holloszy
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Time Dependent ◽  
Acid Transport ◽  
Minimum Essential Medium ◽  
Prolonged Incubation ◽  
System A ◽  
Nonessential Amino Acids

During the course of experiments involving prolonged incubation of skeletal muscle, we observed large increases in system A amino acid transport activity. System A activity was monitored with the nonmetabolizable amino acid analogue alpha-(methylamino)isobutyrate (MeAIB). When rat epitrochlearis muscles are incubated in Krebs-Henseleit buffer supplemented with 0.1% bovine serum albumin and 8 mM glucose, basal MeAIB transport doubles after 5 h and is elevated approximately sevenfold after 9 h compared with rates measured in muscles incubated for 1 h. Insulin-stimulated transport also doubles after 5 h and increases by fourfold after 9 h. The increases in basal and insulin-stimulated system A transport over time can be prevented by incubating muscles in the presence of cycloheximide. Addition of minimum essential medium essential amino acids (EAA) to the incubation medium blocks the increase in basal and insulin-stimulated MeAIB transport measured after 9 h by 85-90 and 60%, respectively. A single amino acid, glutamine, can account for half of the inhibitory effect of EAA on the time-dependent increase in basal system A transport. Amino acid metabolism is not necessary for inhibition of the rise in basal MeAIB transport. At concentrations normally present in minimum essential medium, nonessential amino acids are less effective (51% inhibition) in preventing the rise in basal transport occurring over 9 h. At three times normal concentrations, however, the ability of nonessential amino acids to prevent the time-dependent increases in basal and insulin-stimulated MeAIB transport is comparable to that of EAA. These changes in MeAIB transport with prolonged incubation are not due to muscle deterioration.(ABSTRACT TRUNCATED AT 250 WORDS)

Combined effects of hyperaminoacidemia and oxandrolone on skeletal muscle protein synthesis

2000 ◽  
Vol 278 (2) ◽  
pp. E273-E279 ◽  
Author(s):  
Melinda Sheffield-Moore ◽  
Robert R. Wolfe ◽  
Dennis C. Gore ◽  
Steven E. Wolf ◽  
Dennis M. Ferrer ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Compartment Model ◽  
Acid Mixture ◽  
Skeletal Muscle Protein ◽  
Amino Acid Infusion

We investigated whether the normal anabolic effects of acute hyperaminoacidemia were maintained after 5 days of oxandrolone (Oxandrin, Ox)-induced anabolism. Five healthy men [22 ± 3 (SD) yr] were studied before and after 5 days of oral Ox (15 mg/day). In each study, a 5-h basal period was followed by a 3-h primed-continuous infusion of a commercial amino acid mixture (10% Travasol). Stable isotopic data from blood and muscle sampling were analyzed using a three-compartment model to calculate muscle protein synthesis and breakdown. Model-derived muscle protein synthesis increased after amino acid infusion in both the control [basal control (BC) vs. control + amino acids (C+AA); P < 0.001] and Ox study [basal Ox (BOx) vs. Ox + amino acids (Ox+AA); P < 0.01], whereas protein breakdown was unchanged. Fractional synthetic rates of muscle protein increased 94% (BC vs. C+AA; P = 0.01) and 53% (BOx vs. Ox+AA; P < 0.01), respectively. We conclude that the normal anabolic effects of acute hyperaminoacidemia are maintained in skeletal muscle undergoing oxandrolone-induced anabolism.

Transmembrane transport and intracellular kinetics of amino acids in human skeletal muscle

1995 ◽  
Vol 268 (1) ◽  
pp. E75-E84 ◽  
Author(s):  
G. Biolo ◽  
R. Y. Fleming ◽  
S. P. Maggi ◽  
R. R. Wolfe
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Human Skeletal Muscle ◽  
De Novo ◽  
Transmembrane Transport ◽  
Acid Transport ◽  
De Novo Synthesis ◽  
Intracellular Amino Acid

We have used stable isotopic tracers of amino acids to measure in vivo transmembrane transport of phenylalanine, leucine, lysine, alanine, and glutamine as well as the rates of intracellular amino acid appearance from proteolysis, de novo synthesis, and disappearance to protein synthesis in human skeletal muscle. Calculations were based on data obtained by the arteriovenous catheterization of the femoral vessels and muscle biopsy. We found that the fractional contribution of transport from the bloodstream to the total intracellular amino acid appearance depends on the individual amino acid, varying between 0.63 +/- 0.02 for phenylalanine and 0.22 +/- 0.02 for alanine. Rates of alanine and glutamine de novo synthesis were approximately eight and five times their rate of appearance from protein breakdown, respectively. The model-derived rate of protein synthesis was highly correlated with the same value calculated by means of the tracer incorporation technique. Furthermore, amino acid transport rates were in the range expected from literature values. Consequently, we conclude that our new model provides a valid means of quantifying the important aspects of protein synthesis, breakdown, and amino acid transport in human subjects.

scholarly journals Human Skeletal Muscle Protein Metabolism Responses to Amino Acid Nutrition

2016 ◽  
Vol 7 (4) ◽  
pp. 828S-838S ◽  
Author(s):  
W Kyle Mitchell ◽  
Daniel J Wilkinson ◽  
Bethan E Phillips ◽  
Jonathan N Lund ◽  
Kenneth Smith ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Human Skeletal Muscle ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Muscle Protein Metabolism

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.

Ammonia and amino acid metabolism in human skeletal muscle during exercise

1992 ◽  
Vol 70 (1) ◽  
pp. 132-141 ◽  
Author(s):  
T. E. Graham ◽  
D. A. MacLean
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Steady State ◽  
Amino Acid ◽  
Human Skeletal Muscle ◽  
Branched Chain Amino Acids ◽  
Ammonia Production ◽  
Purine Nucleotide ◽  
Purine Nucleotide Cycle ◽  
Branched Chain

This review focuses on the ammonia and amino acid metabolic responses of active human skeletal muscle, with a particular emphasis on steady-state exercise. Ammonia production in skeletal muscle involves the purine nucleotide cycle and the amino acids glutamate, glutamine, and alanine and probably also includes the branched chain amino acids as well as aspartate. Ammonia production is greatest during prolonged, steady state exercise that requires 60–80% [Formula: see text] and is associated with glutamine and alanine metabolism. Under these circumstances it is unresolved whether the purine nucleotide cycle (AMP deamination) is active; if so, it must be cycling with no IMP accumulation. It is proposed that under these circumstances the ammonia is produced from slow twitch fibers by the deamination of the branched chain amino acids. The ammonia response can be suppressed by increasing the carbohydrate availability and this may be mediated by altering the availability of the branched chain amino acids. The fate of the ammonia released into the circulation is unresolved, but there is indirect evidence that a considerable portion may be excreted by the lung in expired air.Key words: glutamine, branched chain amino acids, glutamate dehydrogenase, purine nucleotide cycle.

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