title: The effect of amino acid infusion on leg protein turnover assessed by L-[15N]phenylalanine and L-[1-13C]leucine exchange.
abstract: A stable isotope technique depending on the use of [15N]phenylalanine and [1-13C]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 negative amino acid balance by a mechanism which includes stimulation of muscle protein synthesis but which does not alter protein breakdown. 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.
authors.affiliation: Department of Anatomy & Physiology, University of Dundee, Scotland, UK.
authors.forename: W M
authors.initials: WM
authors.lastname: Bennet
authors.forename: A A
authors.initials: AA
authors.lastname: Connacher
authors.forename: C M
authors.initials: CM
authors.lastname: Scrimgeour
authors.forename: M J
authors.initials: MJ
authors.lastname: Rennie
mesh_terms: D000328:Adult; D000596:Amino Acids / Q000008:administration & dosage / Q000378:metabolism*; D002247:Carbon Isotopes; D005260:Female; D006728:Hormones / Q000097:blood; D006801:Humans; D007262:Infusions, Intravenous; D007866:Leg; D007930:Leucine / Q000378:metabolism; D008297:Male; D009124:Muscle Proteins / Q000378:metabolism; D009587:Nitrogen Isotopes; D010649:Phenylalanine / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D006728:Hormones; D009124:Muscle Proteins; D009587:Nitrogen Isotopes; D011506:Proteins; D010649:Phenylalanine; D007930:Leucine