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Glucose Transporters

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:

Secondary Active Transport

Secondary Active Transport

One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme "pump" embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...

Secondary Active Transport

Secondary Active Transport

One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme “pump” embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...

Secondary Active Transport

Secondary Active Transport

Glucose Absorption Into the Small Intestine

Glucose Absorption Into the Small Intestine

Complex carbohydrates consumed cannot be absorbed into the small intestine in their original form. First, they must be hydrolyzed to a monosaccharide form such as glucose or galactose. These monosaccharides are then transported across the intestinal membrane and into the blood via transcellular transport. The intestinal epithelial cells allow the movement of these monosaccharides with a defined 'entry' through membrane transporter proteins present on their apical membrane and...

The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

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Related Experiment Video

Updated: May 2, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

Human erythrocytes transport dehydroascorbic acid and sugars using the same transporter complex.

Jay M Sage¹, Anthony Carruthers²

¹Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts.

American Journal of Physiology. Cell Physiology

|March 7, 2014

Summary

Human red blood cells utilize GLUT1 to transport both dehydroascorbic acid (DHA) and sugars like 3-O-methylglucose (3-OMG). These substances compete for uptake, indicating they share the same GLUT1 transport complex.

Keywords:

GLUT1 dehydroascorbic acid transport erythrocyte glucose transport

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Published on: January 2, 2013

Area of Science:

Biochemistry
Cell Biology
Physiology

Background:

GLUT1 is the primary glucose transporter in human red blood cells (RBCs).
GLUT1 also transports dehydroascorbic acid (DHA), the oxidized form of vitamin C.
A recent study proposed DHA is GLUT1's primary substrate, challenging its role in sugar transport.

Purpose of the Study:

To characterize the transport of DHA and 3-O-methylglucose (3-OMG) in RBCs using steady-state kinetics.
To investigate the competitive interactions between DHA and 3-OMG for GLUT1-mediated transport.
To elucidate the binding sites and transport mechanism of DHA and 3-OMG on GLUT1.

Main Methods:

Measured steady-state uptake rates of DHA and 3-OMG in RBCs.
Performed competition assays using varying concentrations of DHA and 3-OMG.
Utilized RBC inside-out-membrane vesicles to study transporter interactions at the cytoplasmic surface.
Investigated the effect of intracellular 3-OMG on substrate uptake.

Main Results:

Steady-state uptake kinetics (Vmax and Km) for 3-OMG and DHA were similar.
3-OMG and DHA competed for uptake, indicating shared binding sites on GLUT1.
Competition was observed at the cytoplasmic surface of the membrane using vesicle studies.
Intracellular 3-OMG enhanced the uptake of both 3-OMG and DHA.

Conclusions:

DHA and 3-OMG bind to mutually exclusive sites on both external and internal surfaces of GLUT1.
Both dehydroascorbic acid and sugars are transported by the same GLUT1 complex.
These findings clarify the dual role of GLUT1 in transporting both vitamin C and glucose analogs.