Sugar Transporters in Polarized Epithelial Cells.

Takata, Kuniaki; Iizuka, Akiko; Suzuki, Takeshi; Matsuzaki, Toshiyuki; Sugawara, Minako; Shin, Bo-Chul; Tserentsoodol, Nomingerel; Shinoda, Yasuo

doi:10.1267/ahc.32.53

Cited by 7 publications

(3 citation statements)

References 32 publications

(45 reference statements)

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“…In the cytosol, GLC is captured by phosphorylation which prevents externalization by the glucose transporter GLUT1, GLUT2, GLUT5 or GLUT9, typically present in kidney cells (Levine and Puzio-Kuter, 2010;Moreno-Sánchez et al, 2007;Nelson et al, 1996;Takata et al, 1999;Thorens, 1993). Subsequently, major amounts of G6P are converted in glycogenesis, the pentose phosphate pathway and glycolysis to UDPGlc, R5P and F6P, respectively.…”

Section: Regulation Of the Upper Part Of Glycolysis And Associated Pamentioning

confidence: 99%

Changes in intracellular metabolite pools during growth of adherent MDCK cells in two different media

Rehberg

Rath

Ritter

et al. 2013

Appl Microbiol Biotechnol

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In bioprocess engineering, the growth of continuous cell lines is mainly studied with respect to the changes in cell concentration, the resulting demand for substrates, and the accumulation of extracellular metabolites. The underlying metabolic process rests upon intracellular metabolite pools and their interaction with enzymes in the form of substrates, products, or allosteric effectors. Here, we quantitatively analyze time courses of 29 intracellular metabolites of adherent Madin-Darby canine kidney cells during cultivation in a serum-containing medium and a serum-free medium. The cells, which originated from the same pre-culture, showed similar overall growth behavior and only slight differences in their demand for the substrates glucose (GLC), glutamine (GLN), and glutamate (GLU). Analysis of intracellular metabolites, which mainly cover the glycolytic pathway, the citric acid cycle, and the nucleotide pools, revealed surprisingly similar dynamics for both cultivation conditions. Instead of a strong influence of the medium, we rather observed a growth phase-specific behavior in glycolysis and in the lower citric acid cycle. Furthermore, analysis of the lower part of glycolysis suggests the well-known regulation of pyruvate kinase by fructose 1,6-bisphosphate. The upper citric acid cycle (citrate, cis-aconitate, and isocitrate) is apparently uncoupled from the lower part (α-ketoglutarate, succinate, fumarate, and malate), which is in line with the characteristics of a truncated cycle. Decreased adenosine triphosphate and guanosine triphosphate pools, as well as a relatively low energy charge soon after inoculation of cells, indicate a high demand for cellular energy and the consumption of nucleotides for biosynthesis. We finally conclude that, with sufficient availability of substrates, the dynamics of GLC and GLN/GLU metabolism is influenced mainly by the cellular growth regime and regulatory function of key enzymes.

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Section: Regulation Of the Upper Part Of Glycolysis And Associated Pamentioning

confidence: 99%

Changes in intracellular metabolite pools during growth of adherent MDCK cells in two different media

Rehberg

Rath

Ritter

et al. 2013

Appl Microbiol Biotechnol

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“…To shed light on the localization mechanism of glucose transporters, their cDNAs were introduced into cultured epithelial cells such as MDCK cells [13,32], and Caco-2 cells [9,11]. Results obtained in these cell culture systems, however, do not necessarily represent the mechanism working in the tissue cells constituting the body in situ.…”

Section: Introductionmentioning

confidence: 99%

Introduction and Expression of Glucose Transporters in Pancreatic Acinar Cells by In Vivo Electroporation

Shinoda

Matsuzaki

Yokoo-Sugawara

et al. 2003

Acta Histochem. Cytochem

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cDNAs encoding facilitated-diffusion glucose transporters GULT1, GULT3, GULT4, and GULT5 were introduced into the rat pancreas by in-vivo electroporation method, and their expression and localization in pancreatic acinar cells were examined immunohistochemically. GLUT1 was localized at the basolateral membrane, whereas GLUT3 and GLUT5 were at the apical membrane. Restriction of GLUT3 and GLUT5 to the apical membrane makes a marked contrast to their localization to the entire plasma membrane when expressed in hepatocytes in situ.Such differential localization may be due to differential apical targeting mechanism: direct targeting in acinar cells and indirect transcytotic delivery in hepatocytes in situ. GLUT4 was present in the membrane of zymogen secretory granules in the cytoplasm in acinar cells. This observation suggests that GLUT4 is segregated to the regulated secretory pathway. Expression of glucose transporters in situ is a useful method in analyzing the targeting mechanism of membrane proteins in cells of tissues in situ.

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“…The sodium-dependent glucose transporter, SGLT1, is localized at the apical plasma membrane in absorptive epithelial cells of small intestine and proximal tubule cells of kidney, where it plays pivotal roles in the absorption and reabsorption of sugars, respectively [14, 16–18, 20, 21]. Localization of SGLT1 to apical membrane is crucial in the vectorial transport of sugars across the epithelial cell layer.…”

Section: Introductionmentioning

confidence: 99%

Apical Localization of Sodium-Dependent Glucose Transporter SGLT1 is Maintained by Cholesterol and Microtubules

Suzuki

Matsuzaki

Hagiwara

et al. 2006

Acta Histochem. Cytochem.

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A GFP-labeled sodium-dependent glucose transporter SGLT1 (SGLT-GFP) was transfected into MDCK cells. SGLT-GFP was localized at the apical membrane in confluent cells. When cellular cholesterol was depleted by methyl-β-cyclodextrin (MβCD) treatment, the localization of SGLT-GFP gradually switched from apical to whole plasma membrane. Time-lapse microscopy revealed that the effect of MβCD appeared within 30 min, and that the transition of SGLT-GFP to the whole plasma membrane was completed within 2 hr after the administration. Immunofluorescence microscopy revealed that the tight junction framework remained steady during this process. The effect of MβCD on SGLT-GFP localization was counterbalanced by the addition of cholesterol into the culture medium. Disruption of microtubules by colcemid also perturbed SGLT-GFP localization. SGLT-GFP localized to the whole plasma membrane by colcemid treatment, and apical localization was restored within 1 hr after removal of colcemid. Inhibition of protein synthesis by cycloheximide had no effect on the transition of SGLT-GFP induced by the MβCD or colcemid. These results indicated that the apical localization of SGLT-GFP is maintained by cellular cholesterol and microtubules, possibly with an apical recycling machinery.

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Sugar Transporters in Polarized Epithelial Cells.

Cited by 7 publications

References 32 publications

Changes in intracellular metabolite pools during growth of adherent MDCK cells in two different media

Changes in intracellular metabolite pools during growth of adherent MDCK cells in two different media

Introduction and Expression of Glucose Transporters in Pancreatic Acinar Cells by In Vivo Electroporation

Apical Localization of Sodium-Dependent Glucose Transporter SGLT1 is Maintained by Cholesterol and Microtubules

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