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


     

Am J Physiol Endocrinol Metab 259: E284-E291, 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 Ahmed, A.
Right arrow Articles by Rennie, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ahmed, A.
Right arrow Articles by Rennie, M. J.

AJP - Endocrinology and Metabolism, Vol 259, Issue 2 E284-E291, Copyright © 1990 by American Physiological Society

ARTICLES

Characteristics of glutamine transport in sarcolemmal vesicles from rat skeletal muscle

A. Ahmed, P. M. Taylor and M. J. Rennie
Department of Anatomy and Physiology, University of Dundee, United Kingdom.

Amino acid transport was measured in rat sarcolemmal vesicles (approximately 0.5 microliters/mg protein). Initial (45 s) uptake of glutamine tracer was stereospecific and saturable [Km 90 +/- 14 microM; maximum velocity (Vmax) 60 +/- 3 pmol.mg protein-1.min-1], it was Na+ dependent (but tolerated Li+ instead), and was stimulated by inside negative membrane potential. Transport of glutamine (5 microM) was inhibited by asparagine, histidine, alanine, serine, and phenylalanine at 1 mM (25-74%), but leucine and N-methylaminoisobutyric acid (MeAIB) did not significantly inhibit glutamine uptake. Glutamine efflux was accelerated by an outwardly directed Na+ concentration gradient. L-[14C]asparagine uptake was Na+ dependent and strongly inhibited by glutamine. L-[3H]serine uptake was Na+ dependent but did not tolerate Li(+)-for-Na+ substitution. L-[3H]phenylalanine uptake was Na+ independent. Differences between the ion dependence of glutamine, serine, and phenylalanine uptake and the lack of glutamine transport inhibition by MeAIB indicated that glutamine is not transported by systems ASC, L, or A. The properties of the glutamine transporter in sarcolemmal vesicles resemble those of the system Nm previously characterized in perfused skeletal muscle.


This article has been cited by other articles:


Home page
 J. Physiol.Home page
H. J. Herr, J. R. Bernard, D. W. Reeder, D. A. Rivas, J. J. Limon, and B. B. Yaspelkis III
Insulin-stimulated plasma membrane association and activation of Akt2, aPKC {zeta} and aPKC {lambda} in high fat fed rodent skeletal muscle
J. Physiol., June 1, 2005; 565(2): 627 - 636.
[Abstract] [Full Text] [PDF]

Home page
 DiabetesHome page
L. P. Turcotte, J. R. Swenberger, M. Zavitz Tucker, and A. J. Yee
Increased Fatty Acid Uptake and Altered Fatty Acid Metabolism in Insulin-Resistant Muscle of Obese Zucker Rats
Diabetes, June 1, 2001; 50(6): 1389 - 1396.
[Abstract] [Full Text]

Home page
 J. Appl. Physiol.Home page
L. P. Turcotte, J. R. Swenberger, M. Z. Tucker, and A. J. Yee
Training-induced elevation in FABPPM is associated with increased palmitate use in contracting muscle
J Appl Physiol, July 1, 1999; 87(1): 285 - 293.
[Abstract] [Full Text] [PDF]


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