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Stümpel F, Burcelin R, Jungermann K, et al. Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2001;98(20):11330-5doi: 10.1073/pnas.211357698.
Stümpel, F., Burcelin, R., Jungermann, K., & Thorens, B. (2001). Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America, 98(20), 11330-5. https://doi.org/10.1073/pnas.211357698
Stümpel, F, et al. "Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum." Proceedings of the National Academy of Sciences of the United States of America vol. 98,20 (2001): 11330-5. doi: https://doi.org/10.1073/pnas.211357698
Stümpel F, Burcelin R, Jungermann K, Thorens B. Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11330-5. doi: 10.1073/pnas.211357698. Epub 2001 Sep 18. PMID: 11562503; PMCID: PMC58729.
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Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11330-5. doi: 10.1073/pnas.211357698. Epub 2001 Sep 18.

Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum.

Proceedings of the National Academy of Sciences of the United States of America

F Stümpel, R Burcelin, K Jungermann, B Thorens

Affiliations

  1. Georg-August-University Göttingen, Institute for Biochemistry and Molecular Cell Biology, Humboldtallee 23, 37073 Göttingen, Germany.

PMID: 11562503 PMCID: PMC58729 DOI: 10.1073/pnas.211357698

Abstract

Glucose is absorbed through the intestine by a transepithelial transport system initiated at the apical membrane by the cotransporter SGLT-1; intracellular glucose is then assumed to diffuse across the basolateral membrane through GLUT2. Here, we evaluated the impact of GLUT2 gene inactivation on this transepithelial transport process. We report that the kinetics of transepithelial glucose transport, as assessed in oral glucose tolerance tests, was identical in the presence or absence of GLUT2; that the transport was transcellular because it could be inhibited by the SGLT-1 inhibitor phlorizin, and that it could not be explained by overexpression of another known glucose transporter. By using an isolated intestine perfusion system, we demonstrated that the rate of transepithelial transport was similar in control and GLUT2(-/-) intestine and that it was increased to the same extent by cAMP in both situations. However, in the absence, but not in the presence, of GLUT2, the transport was inhibited dose-dependently by the glucose-6-phosphate translocase inhibitor S4048. Furthermore, whereas transport of [(14)C]glucose proceeded with the same kinetics in control and GLUT2(-/-) intestine, [(14)C]3-O-methylglucose was transported in intestine of control but not of mutant mice. Together our data demonstrate the existence of a transepithelial glucose transport system in GLUT2(-/-) intestine that requires glucose phosphorylation and transfer of glucose-6-phosphate into the endoplasmic reticulum. Glucose may then be released out of the cells by a membrane traffic-based pathway similar to the one we previously described in GLUT2-null hepatocytes.

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