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Endocrinology, Vol 136, 4224-4230, Copyright © 1995 by Endocrine Society

ARTICLES

Two regions of GLUT 2 glucose transporter protein are responsible for its distinctive affinity for glucose

A Buchs, L Wu, H Morita, RR Whitesell and AC Powers
Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee, USA.

The glucose transporter in the hepatocyte and pancreatic beta-cell (GLUT 2) has a lower affinity for glucose than other members of the glucose transporter family. To investigate the molecular mechanism for the distinctive affinity of GLUT 2 for glucose, we expressed chimeric GLUT 2 and GLUT 4 proteins in Xenopus oocytes and measured 3-O-methyl-D- glucose transport. In the oocyte system, GLUT 2 had a Km of 31.8 +/- 2.8 mM for 3-O-methyl-D-glucose, whereas GLUT 4 had a Km of 7.2 +/- 2.4 mM under equilibrium exchange conditions. GLUT 4/GLUT 2 chimera that contained the intracellular loop and transmembrane domains 7-12 of GLUT 2 (amino acids 239-497) had a Km similar to that of wild-type GLUT 2. A GLUT 4/GLUT 2 chimera in which the COOH-terminal 30 amino acids of GLUT 4 were replaced with the corresponding region of GLUT 2 had a 2-fold higher Km than GLUT 4, but still had a much lower Km than GLUT 2. These results indicate that both transmembrane domains 7-12 and the COOH- terminus of the protein are responsible for the distinctive glucose affinity of GLUT 2.


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L. Wu, J. D. Fritz, and A. C. Powers
Different Functional Domains of GLUT2 Glucose Transporter Are Required for Glucose Affinity and Substrate Specificity
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A. E. Buchs, S. Sasson, H. G. Joost, and E. Cerasi
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Endocrinology, March 1, 1998; 139(3): 827 - 831.
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Familial Hyperinsulinism Caused by an Activating Glucokinase Mutation
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