AJP - Endo Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Endocrinol Metab 274: E516-E526, 1998;
0193-1849/98 $5.00
This Article
Right arrow Full Text
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 Malide, D.
Right arrow Articles by Simpson, I. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Malide, D.
Right arrow Articles by Simpson, I. A.
Vol. 274, Issue 3, E516-E526, March 1998

Distinct localization of GLUT-1, -3, and -5 in human monocyte-derived macrophages: effects of cell activation

Daniela Malide1, Theresa M. Davies-Hill1, Mark Levine2, and Ian A. Simpson1

1 Experimental Diabetes, Metabolism, and Nutrition and 2 Molecular and Clinical Nutrition Sections, Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892

We determined subcellular localization of GLUT-1, GLUT-3, and GLUT-5 as human monocytes differentiate into macrophages in culture, and effects of the activating agents N-formyl-methionyl-leucyl-phenylalanine (fMLP) and phorbol myristate acetate (PMA). Western blot analysis demonstrated progressively increased GLUT-1, rapidly decreased GLUT-3, and a delayed increase of GLUT-5 expression during differentiation. Confocal microscopy revealed that each isoform displayed a unique subcellular distribution and cell-activation response. GLUT-1 was localized primarily to the cell surface but was also detected in the perinuclear region in a pattern characteristic of recycling endosomes. GLUT-3 exhibited predominantly a distinct vesicle-like staining but was present only in monocytes. GLUT-5 was found primarily at the cell surface but was detectable intracellularly. Activation with fMLP induced similar GLUT-1 and GLUT-5 redistributions from intracellular compartments toward the cell surface. PMA elicited a similar translocation of GLUT-1, but GLUT-5 was redistributed from the plasma membrane to a distinct intracellular compartment that appeared connected to the cell surface. These results suggest specific subcellular targeting of each transporter isoform and differential regulation of their trafficking pathways in cultured macrophages.

glucose transporter targeting; recycling pathways; phagocytic cells; protein kinase C; confocal microscopy


This article has been cited by other articles:


Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
V. Douard and R. P. Ferraris
Regulation of the fructose transporter GLUT5 in health and disease
Am J Physiol Endocrinol Metab, August 1, 2008; 295(2): E227 - E237.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
I. A. Simpson, D. Dwyer, D. Malide, K. H. Moley, A. Travis, and S. J. Vannucci
The facilitative glucose transporter GLUT3: 20 years of distinction
Am J Physiol Endocrinol Metab, August 1, 2008; 295(2): E242 - E253.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
D. P. Schuster, S. L. Brody, Z. Zhou, M. Bernstein, R. Arch, D. Link, and M. Mueckler
Regulation of lipopolysaccharide-induced increases in neutrophil glucose uptake
Am J Physiol Lung Cell Mol Physiol, April 1, 2007; 292(4): L845 - L851.
[Abstract] [Full Text] [PDF]


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