Title
ATP-Dependent Sugar Transport Complexity in Human Erythrocytes
UMMS Affiliation
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology
Date
2-13-2007
Document Type
Article
Medical Subject Headings
3-O-Methylglucose; Adenosine Triphosphate; Biological Transport; Cell Size; Cytoplasm; Equilibrative Nucleoside Transporter 1; Erythrocyte Membrane; Erythrocytes; Glucose; Glucose Transporter Type 1; Humans; Microscopy, Electron, Scanning; Models, Biological; Uridine
Abstract
Human erythrocyte glucose sugar transport was examined in resealed red cell ghosts under equilibrium exchange conditions ([sugar](intracellular) = [sugar](extracellular), where brackets indicate concentration). Exchange 3-O-methylglucose (3MG) import and export are monophasic in the absence of cytoplasmic ATP but are biphasic when ATP is present. Biphasic exchange is observed as the rapid filling of a large compartment (66% cell volume) followed by the slow filling of the remaining cytoplasmic space. Biphasic exchange at 20 mM 3MG eliminates the possibility that the rapid exchange phase represents ATP-dependent 3MG binding to the glucose transport protein (GLUT1; cellular [GLUT1] of
Rights and Permissions
Citation: Am J Physiol Cell Physiol. 2007 Feb;292(2):C974-86. Epub 2006 Aug 23. Link to article on publisher's site
Related Resources
Keywords
Membrane transport; erythrocytes; GLUT1