AJP - Endo Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Endocrinol Metab 263: E928-E934, 1992;
0193-1849/92 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nair, K. S.
Right arrow Articles by Welle, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nair, K. S.
Right arrow Articles by Welle, S.

AJP - Endocrinology and Metabolism, Vol 263, Issue 5 E928-E934, Copyright © 1992 by American Physiological Society


ARTICLES

Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans

K. S. Nair, R. G. Schwartz and S. Welle
Department of Medicine, University of Vermont College of Medicine, Burlington 05401.

Leucine has been proposed as an in vivo regulator of protein metabolism, although the evidence for this in humans remains inconclusive. To test this hypothesis, we infused either L-leucine (154 +/- 1 mumol.kg-1 x h-1) or saline intravenously in six healthy men in two separate studies. L-Leucine infusion increased plasma concentrations of leucine and alpha-ketoisocaproate from 112 +/- 6 and 38 +/- 3 mumol/l to 480 +/- 27 (P < 0.001) and 94 +/- 13 mumol/l (P < 0.001), respectively, without any significant change in circulating insulin or C peptide levels. Leucine infusion decreased plasma concentrations of several amino acids and decreased whole body valine flux and valine oxidation (using L-[1-13C]valine as a tracer) and phenylalanine flux (using [2H5]-phenylalanine as a tracer). According to arteriovenous differences across the leg, the net balance of phenylalanine, valine, and lysine shifted toward greater retention during leucine infusion, whereas alanine balance did not change. Valine release and phenylalanine release from the leg (estimated from the dilution of respective tracers) decreased, indicating inhibition of protein degradation by leucine infusion. We conclude that leucine decreases protein degradation in humans and that this decreased protein degradation during leucine infusion contributes to the decrease in plasma essential amino acids. This study suggests a potential role for leucine as a regulator of protein metabolism in humans.


This article has been cited by other articles:


Home page
Br. J. Sports. Med.Home page
A H Manninen
Hyperinsulinaemia, hyperaminoacidaemia and post-exercise muscle anabolism: the search for the optimal recovery drink
Br. J. Sports Med., November 1, 2006; 40(11): 900 - 905.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
C. S. Katsanos, H. Kobayashi, M. Sheffield-Moore, A. Aarsland, and R. R. Wolfe
A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly
Am J Physiol Endocrinol Metab, August 1, 2006; 291(2): E381 - E387.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
J. Escobar, J. W. Frank, A. Suryawan, H. V. Nguyen, S. R. Kimball, L. S. Jefferson, and T. A. Davis
Physiological rise in plasma leucine stimulates muscle protein synthesis in neonatal pigs by enhancing translation initiation factor activation
Am J Physiol Endocrinol Metab, May 1, 2005; 288(5): E914 - E921.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
R. Koopman, A. J. M. Wagenmakers, R. J. F. Manders, A. H. G. Zorenc, J. M. G. Senden, M. Gorselink, H. A. Keizer, and L. J. C. van Loon
Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects
Am J Physiol Endocrinol Metab, April 1, 2005; 288(4): E645 - E653.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
H. K. R. Karlsson, P.-A. Nilsson, J. Nilsson, A. V. Chibalin, J. R. Zierath, and E. Blomstrand
Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise
Am J Physiol Endocrinol Metab, July 1, 2004; 287(1): E1 - E7.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online