ATP-Dependent Sugar Transport Complexity in Human Erythrocytes

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology



Document Type


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


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

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Citation: Am J Physiol Cell Physiol. 2007 Feb;292(2):C974-86. Epub 2006 Aug 23. Link to article on publisher's site

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Link to article in PubMed


Membrane transport; erythrocytes; GLUT1

PubMed ID