Journal
SURGERY
Volume 151, Issue 1, Pages 13-25Publisher
MOSBY-ELSEVIER
DOI: 10.1016/j.surg.2011.07.010
Keywords
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Categories
Funding
- NIH [DK-39337]
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK039337] Funding Source: NIH RePORTER
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Background. GLUT2 is translocated to the apical membrane of enterocytes exposed to glucose concentrations >similar to 50 mM. Mechanisms of GLUT2-mediated glucose uptake in cell culture models of enterocytes have not been studied. Aim. To explore mechanism(s) of glucose uptake in 3 enterocyte-like cell lines. Methods. Glucose uptake was measured in Caco-2, RIE-1, and IEC-6 cell lines using varying concentrations of glucose (0.5-50 mM). Effects of phlorizin (SGLT1 inhibitor), phloretin (GLUT2 inhibitor), nocodazole and cylochalasin B (disrupters of cytoskeleton), calphostin C and chelerythrine (PKC inhibitors), and phorbol 12-myristate 13-acetate (PKC activator) were evaluated. Results. Phlorizin inhibited glucose uptake in. all 3 cell lines. Phloretin inhibited glucose uptake in Caco-2 and RIE-1 cells. Starving cells decreased glucose uptake in Caco-2 and RIE-1 cells. Glucose uptake was saturated at >10 mM glucose in all 3 cell lines when exposed briefly (<1 min) to glucose. After exposure for >5 min in Caco-2 and RIE-1 cells, glucose uptake did not saturate and K, and V,, increased. This increase in glucose uptake was inhibited by phloretin, nocodazole, cytochalasin 13, calphostin C, and chelerythrine. PMA enhanced glucose uptake by 20%. Inhibitors and PMA had little or no effect in the IEC-6 Conclusion. Constitutive expression of GLUT2 in the apical membrane along with additional translocation of cytoplasmic GLUT2 to the apical membrane via an intact cytoskeleton and activated PKC appears responsible for enhanced carrier-mediated glucose uptake at greater glucose concentrations (>20 mM) in Caco-2 and RIE-1 cells. IEC-6 cells do not appear to express functional GLUT2. (Surgery 2012; 151: 13-25.)
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