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


     

Am J Physiol Endocrinol Metab 258: E78-E85, 1990;
0193-1849/90 $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
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 Couet, C.
Right arrow Articles by Young, V. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Couet, C.
Right arrow Articles by Young, V. R.

AJP - Endocrinology and Metabolism, Vol 258, Issue 1 E78-E85, Copyright © 1990 by American Physiological Society

ARTICLES

Plasma amino acid kinetics during acute states of glucagon deficiency and excess in healthy adults

C. Couet, N. K. Fukagawa, D. E. Matthews, D. M. Bier and V. R. Young
School of Science, Massachusetts Institute of Technology, Cambridge 02139.

The effects of glucagon deficiency and excess on plasma leucine, lysine, and alanine were examined in six healthy young adult men, with primed continuous infusions of L-[1-13C]- or L-[5,5,5-2H3]leucine, L-[alpha-15N]-lysine, and L-[3-13C]alanine for 150 min before and during 210 min of either a glucagon-deficient euglycemic state (experiment 1), a basal glucagon state (experiment 2), or a glucagon-excess state (experiment 3). Steady-state plasma hormone levels were achieved by infusion of somatostatin (250 micrograms/h) and insulin (0.07 mU.kg-1.min-1), without (experiment 1) or with an infusion of glucagon at 0.7 ng.kg-1.min-1 (experiment 2) or 2.5 ng.kg-1.min-1 (experiment 3). Plasma branched-chain amino acid (AA) concentrations did not change with altered glucagon status, whereas significant differences were observed for plasma lysine, alanine, glycine, serine, threonine, proline, tyrosine, citrulline, and ornithine levels (0.05 greater than P greater than 0.001). Plasma leucine, lysine, and alanine fluxes and the rate of de novo alanine synthesis showed no significant changes with either glucagon deficiency or excess. These findings lead to the conclusion that glucagon-induced alterations in plasma AA profiles are not due to changes in the rate of appearance of AA from peripheral tissues but rather a consequence of changes in the fate of AA within the splanchnic region.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
D. Paddon-Jones, M. Sheffield-Moore, D. L. Creson, A. P. Sanford, S. E. Wolf, R. R. Wolfe, and A. A. Ferrando
Hypercortisolemia alters muscle protein anabolism following ingestion of essential amino acids
Am J Physiol Endocrinol Metab, May 1, 2003; 284(5): E946 - E953.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
A. H. Forslund, L. Hambraus, H. van Beurden, U. Holmback, A. E. El-Khoury, G. Hjorth, R. Olsson, M. Stridsberg, L. Wide, T. Akerfeldt, et al.
Inverse relationship between protein intake and plasma free amino acids in healthy men at physical exercise
Am J Physiol Endocrinol Metab, May 1, 2000; 278(5): E857 - E867.
[Abstract] [Full Text] [PDF]


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