The effect of amino acid infusion on leg protein turnover assessed by L‐[15N]phenylalanine and L‐[1‐13C]leucine exchange
- 1 February 1990
- journal article
- research article
- Published by Wiley in European Journal of Clinical Investigation
- Vol. 20 (1) , 41-50
- https://doi.org/10.1111/j.1365-2362.1990.tb01789.x
Abstract
A stable isotope technique depending on the use of [15N]phenylalanine and [l-13C]leucine to assess exchange was utilized to measure the components of protein turnover of the human leg and the effects of amino acid infusion. Eight healthy subjects (28.5 .+-. 2.5 years) were studied when post-absorptive in the basal state and again during infusion of a mixed amino acid solution (55 g l-1, 1.52 ml kg-1 h-1). During the basal period leucine oxidation by the leg was 4.4 .+-. 2.0 nmol 100 g-1 min-1 and this increased threefold during amino acid infusion (13.6 .+-. 3.1 nmol 100 g-1 min-1, mean .+-. SEM, P = 0.003). Amino acid infusion abolished the net negative balance between incorporation of leucine into, and release from, protein (basal, -31.8 .+-. 5.8; during infusion, +3.1 .+-. 7.1 nmol 100 g-1 P = 0.001). Phenylalanine exchange showed a similar pattern (basal, -13.7 .+-. 1.8; during infusion, -0.8 .+-. 3.0 nmol 100 g-1 min-1, P = 0.003). Basal entry of leucine into leg protein (i.e. protein synthesis) was 70.0 .+-. 10.8 nmol 100 g-1 min-1 and this increased during amino acid infusion to 87.3 .+-. 14.1 nmol 100 g-1 min-1 (P = 0.11). Phenylalanine entry to protein also increased with amino acid infusion (29.1 .+-. 4.5 vs. 38.3 .+-. 5.8 nmol 100 g-1 min-1, P = 0.09). Release from protein of leucine (101.8 .+-. 9.1 vs. 84.2 .+-. 9.1 nmol 100 g-1 min-1, P = 0.21) and of phenylalanine (42.8 .+-. 4.2 vs. 39.1 .+-. 4.2 nmol 100 g-1 min-1, P = 0.50) was unchanged by amino acid infusion. The results suggest that, in the post-absorptive state in man, infusion of mixed amino acids, without additional energy substrates; reverses amino acid balance by a mechanism which includes stimulation of muscle protein synthesis but which does not alter protein break-down. Interpretation of the results obtained concurrently on whole-body protein turnover suggests that the increase in muscle protein synthesis contributes substantially to the whole-body increase, but the fall in whole-body breakdown with exogenous amino acids is independent of changes in muscle.Keywords
This publication has 37 references indexed in Scilit:
- PREVENTION OF DISUSE MUSCLE ATROPHY BY MEANS OF ELECTRICAL STIMULATION: MAINTENANCE OF PROTEIN SYNTHESISThe Lancet, 1988
- Automated measurement of the concentration and13C enrichment of carbon dioxide in breath and blood samples using the finnigan MAT breath gas analysis systemJournal of Mass Spectrometry, 1988
- Conchotome and needle percutaneous biopsy of skeletal muscle.Journal of Neurology, Neurosurgery & Psychiatry, 1987
- Transport kinetics of amino acids across the resting human leg.Journal of Clinical Investigation, 1987
- Effect of physiologic hyperinsulinemia on skeletal muscle protein synthesis and breakdown in man.Journal of Clinical Investigation, 1987
- Direct determination of leucine metabolism and protein breakdown in humans using L-[1-13C,15N]-leucine and the forearm modelEuropean Journal of Clinical Investigation, 1985
- Preparation of CO2 from blood and protein-bound amino acid carboxyl groups for quantification and13C-isotope measurementsJournal of Mass Spectrometry, 1984
- Regulation of Leucine Metabolism in Man: A Stable Isotope StudyScience, 1981
- Quantitation of 2-ketoacids in biological fluids by gas chromatography chemical ionization mass spectrometry ofO-trimethylsily-quinoxalinol derivativesJournal of Mass Spectrometry, 1981
- Oxidation of plasma FFA in lean and obese humansMetabolism, 1968