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Diabetes 52:1147-1154, 2003
© 2003 by the American Diabetes Association, Inc.

A Novel Glucose-Sensing Mechanism Contributing to Glucagon-Like Peptide-1 Secretion From the GLUTag Cell Line

Fiona M. Gribble, Leanne Williams, Anna K. Simpson, and Frank Reimann

From the Department of Clinical Biochemistry, University of Cambridge, Addenbrooke’s Hospital, Cambridge, United Kingdom

Glucagon-like peptide 1 (GLP-1) secretion from intestinal L-cells is triggered by luminal nutrients. We reported previously that glucose-triggered GLP-1 release from the L-cell model GLUTag involves closure of ATP-sensitive K+ (KATP) channels. We show here that GLP-1 secretion and electrical activity of GLUTag cells is triggered not only by metabolizable sugars (glucose or fructose) but also by the nonmetabolizable monosaccharide methyl-{alpha}-glucopyranoside. Responses to glucose and methyl-{alpha}-glucopyranoside were impaired by the sodium-glucose cotransporter (SGLT) inhibitor phloridzin. SLGT1 and 3 were detected in GLUTag cells by RT-PCR. Whereas fructose closed KATP channels, methyl-{alpha}-glucopyranoside increased the membrane conductance and generated an inward current. Low concentrations of glucose and methyl-{alpha}-glucopyranoside also triggered small inward currents and enhanced the action potential frequency. We conclude that whereas low concentrations of metabolizable sugars trigger GLP-1 secretion via KATP channel closure, SGLT substrates generate small inward currents as a result of the electrogenic action of the transporter. This transporter-associated current can trigger electrical activity and secretion when the concentration of substrate is high or when outward currents are reduced by metabolic closure of the KATP channels. Electrogenic sugar entry via SGLTs provides a novel mechanism for glucose sensing by neuroendocrine cells.


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