Effects of an amino acid solution enriched with either branched chain amino acids or ornithine-α-ketoglutarate on the postoperative intracellular amino acid concentration of skeletal muscle

1990 ◽  
Vol 77 (2) ◽  
pp. 214-218 ◽  
Author(s):  
F. Hammarqvist ◽  
J. Wernerman ◽  
R. Ali ◽  
E. Vinnars
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Acid Solution ◽  
Acid Concentration ◽  
Branched Chain Amino Acids ◽  
Amino Acid Concentration ◽  
Amino Acid Solution ◽  
Intracellular Amino Acid ◽  
Branched Chain

Short-term studies on the use of amino acids as an osmotic agent in continuous ambulatory peritoneal dialysis

1987 ◽  
Vol 73 (5) ◽  
pp. 471-478 ◽  
Author(s):  
T. H. J. Goodship ◽  
S. Lloyd ◽  
P. W. McKenzie ◽  
M. Earnshaw ◽  
I. Smeaton ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Solution ◽  
Serum Insulin ◽  
Branched Chain Amino Acids ◽  
High Concentration ◽  
Short Term ◽  
Amino Acid Solution ◽  
Metabolic Complications ◽  
Branched Chain

1. A 1% amino acid dialysis solution with a high concentration of the branched-chain amino acids has been compared with 1.36% glucose in short-term studies. 2. The 1% amino acid solution was as effective an agent as 1.36% glucose with respect to ultrafiltration and clearance of creatinine, urea and potassium. 3. Levels of branched-chain amino acids rose to the upper end of the normal range within 1 h and remained at this level over the entire period of the study. Total and non-essential amino acids had returned to baseline by the end of the cycle. 4. Blood glucose rose to significantly greater levels during the 1.36% glucose exchange than during the 1% amino acid exchange. There was an increase in serum insulin levels during both cycles; this was significantly greater with the 1% amino acid solution than the 1.36% glucose. 5. There was no evidence of short-term metabolic complications with the 1% amino acid solution.

Removal of infused amino acids by splanchnic and leg tissues in humans

1986 ◽  
Vol 250 (4) ◽  
pp. E407-E413 ◽  
Author(s):  
R. A. Gelfand ◽  
M. G. Glickman ◽  
R. Jacob ◽  
R. S. Sherwin ◽  
R. A. DeFronzo
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Uptake ◽  
Branched Chain Amino Acids ◽  
Acid Uptake ◽  
Acid Infusion ◽  
Amino Acid Infusion ◽  
Significant Uptake ◽  
Branched Chain

To compare the contributions of splanchnic and skeletal muscle tissues to the disposal of intravenously administered amino acids, regional amino acid exchange was measured across the splanchnic bed and leg in 11 normal volunteers. Postabsorptively, net release of amino acids by leg (largely alanine and glutamine) was complemented by the net splanchnic uptake of amino acids. Amino acid infusion via peripheral vein (0.2 g X kg-1 X h-1) caused a doubling of plasma insulin and glucagon levels and a threefold rise in blood amino acid concentrations. Both splanchnic and leg tissues showed significant uptake of infused amino acids. Splanchnic tissues accounted for approximately 70% of the total body amino acid nitrogen disposal; splanchnic uptake was greatest for the glucogenic amino acids but also included significant quantities of branched-chain amino acids. In contrast, leg amino acid uptake was dominated by the branched-chain amino acids. Based on the measured leg balance, body skeletal muscle was estimated to remove approximately 25-30% of the total infused amino acid load and approximately 65-70% of the infused branched-chain amino acids. Amino acid infusion significantly stimulated both the leg efflux and the splanchnic uptake of glutamine (not contained in the infusate). We conclude that when amino acids are infused peripherally in normal humans, splanchnic viscera (liver and gut) are the major sites of amino acid disposal.

Interorgan metabolism of amino acids in streptozotocin-diabetic ketoacidotic rat

1983 ◽  
Vol 244 (2) ◽  
pp. E151-E158 ◽  
Author(s):  
J. T. Brosnan ◽  
K. C. Man ◽  
D. E. Hall ◽  
S. A. Colbourne ◽  
M. E. Brosnan
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Branched Chain Amino Acids ◽  
Diabetic Rats ◽  
Normal Rat ◽  
Diabetic Brain ◽  
Streptozotocin Diabetic Rats ◽  
Branched Chain ◽  
Amino Acid Concentrations

Amino acid concentrations in whole blood, liver, kidney, skeletal muscle, and brain were measured and arteriovenous differences calculated for head, hindlimb, kidney, gut, and liver in control and streptozotocin-diabetic rats. In the control rats, glutamine was released by muscle and utilized by intestine, intestine released citrulline and alanine, liver removed alanine, and the kidneys removed glycine and produced serine. In diabetic rats, the major changes from the pattern of fluxes seen in the normal rat were the release of many amino acids from muscle, with glutamine and alanine predominating, and the uptake of these amino acids by the liver. Glutamine removal by the intestine was suppressed in diabetes, but a large renal uptake of glutamine was evident. Branched-chain amino acids were removed by the diabetic brain, and consequently, brain levels of a number of large neutral amino acids were decreased in diabetes.

Role of Leucine in Protein Metabolism During Exercise and Recovery

2002 ◽  
Vol 27 (6) ◽  
pp. 646-662 ◽  
Author(s):  
Donald K. Layman
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Branched Chain Amino Acids ◽  
New Findings ◽  
Branched Chain

Exercise produces changes in protein and amino acid metabolism. These changes include degradation of the branched-chain amino acids, production of alanine and glutamine, and changes in protein turnover. One of the amino acid most affected by exercise is the branched-chain amino acid leucine. Recently, there has been an increased understanding of the role of leucine in metabolic regulations and remarkable new findings about the role of leucine in intracellular signaling. Leucine appears to exert a synergistic role with insulin as a regulatory factor in the insulin/phosphatidylinositol-3 kinase (PI3-K) signal cascade. Insulin serves to activate the signal pathway, while leucine is essential to enhance or amplify the signal for protein synthesis at the level of peptide initiation. Studies feeding amino acids or leucine soon after exercise suggest that post-exercise consumption of amino acids stimulates recovery of muscle protein synthesis via translation regulations. This review focuses on the unique roles of leucine in amino acid metabolism in skeletal muscle during and after exercise. Key words: branched-chain amino acids, insulin, protein synthesis, skeletal muscle

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.

P.98 Muscle intracellular amino acid concentrationsin normal and hyperammonemic rats infused with branched-chain amino acids (BCAA)

1995 ◽  
Vol 14 ◽  
pp. 62
Author(s):  
R. Breitkreutz ◽  
R. Schmidt ◽  
T. Wurmb ◽  
U. Staedt ◽  
F. Behne ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Branched Chain Amino Acids ◽  
Intracellular Amino Acid ◽  
Branched Chain
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