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Gene Review

SLC5A10  -  solute carrier family 5 (sodium/glucose...

Sus scrofa

Synonyms: SGLT1, SGLT5, SLC5A1
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Disease relevance of SGLT1


High impact information on SGLT1

  • SGLT1 mRNA levels were highest when the D-glucose concentration in the culture medium was 5 to 10 mM [3].
  • The extensive homology of the two sequences leads us to suggest that the high-affinity SGLT expressed by LLC-PK1 cells is SGLT1 [3].
  • To identify the sodium-coupled glucose transporter (SGLT), we cloned and sequenced several partial cDNAs homologous to SGLT1 from rabbit small intestine (M. A. Hediger, M. J. Coady, T. S. Ikeda, and E. M. Wright, Nature (London) 330:379-381, 1987) [3].
  • SGLT1 activity, measured by methyl alpha-D-glucopyranoside uptake, paralleled message levels except in cultures containing D-galactose [3].
  • Addition of D-mannose or D-fructose, but not D-galactose, in the presence of 5 mM D-glucose suppressed SGLT1 mRNA levels [3].

Biological context of SGLT1

  • Transfection of an anti-Hsp70 antibody into the cells inhibited the increase of SGLT1 activity [4].
  • These results suggest that Hsp70 forms a complex with SGLT1 and increases the expression level of SGLT1 in the apical membrane, resulting in up-regulation of glucose uptake [4].
  • Aminoglycoside antibiotics reduce glucose reabsorption in kidney through down-regulation of SGLT1 [5].
  • Previous studies on the small intestinal brush border membrane have shown that part of the decrease in the activity of the Na(+)-dependent glucose transporter (SGLT1) observed after oxidation could be secondary to the derangement in membrane fluidity that accompanied oxidative damage [6].
  • Therefore, SGLT1 gene expression may respond either to the cellular energy status or to the concentration of a hexose metabolite(s) [3].

Anatomical context of SGLT1


Associations of SGLT1 with chemical compounds

  • We investigated whether sodium-dependent glucose transporter (SGLT1) interacts with Hsp70 to increase SGLT1 activity [4].
  • To obtain evidence about SGLT1 down-regulation in vivo, we studied the mRNA expression of SGLT1 using gentamicin C-treated murine kidney and found that gentamicin C down-regulated SGLT1 in vivo as well as in vitro [5].
  • Then the cells were treated with various concentrations of apoE3, lactoferrin and bovine serum albumin with or without 100 microg/ml of GMC, and the SGLT1-dependent methyl alpha-D-glucopyranoside (AMG) uptake and levels of SGLT1 expression were determined [8].
  • During growth to confluence, 2dglc uptake increased to a maximum, then decreased at the time of confluence, coincident with a rise in uptake capacity for alpha-methyl-D-glucoside, a hexose that interacts only with the apical SGLT [9].
  • Specific glucose transport inhibitor studies using phlorizin, phloretin and cytochalasin B confirmed the polarised distribution of SGLT and GLUT in LLC-PK1 cells [9].

Regulatory relationships of SGLT1


Other interactions of SGLT1

  • We previously reported that aminoglycoside antibiotics reduce SGLT1-dependent glucose transport in pig proximal tubular epithelial LLC-PK1 cells in parallel with the order of their nephrotoxicity [8].
  • Previously we cloned membrane associated (M(r) 62000-67000) polypeptides from pig (pRS1), rabbit (rbRS1) and man (hRS1) which modified transport activities that were expressed in Xenopus laevis oocytes by the Na(+)-D-glucose cotransporter SGLT1 and/or the organic cation transporter OCT2 [12].
  • Biophysical characteristics of the pig kidney Na+/glucose cotransporter SGLT2 reveal a common mechanism for SGLT1 and SGLT2 [13].
  • Taken together, HS increases in the number of SGLT1 protein in apical membrane mediated via TGF-beta 1 signaling pathway [11].

Analytical, diagnostic and therapeutic context of SGLT1

  • SGLT1 mRNA levels were significantly increased after treatment of confluent cultures with HMBA, paralleling increases in the transport activity and immunodetectable 75 kD cotransporter subunit [14].
  • Northern blot and PCR analysis of clonal cell populations indicated SGLT1 mRNA was not detectable in subconfluent cultures, but 2.2 and 3.9 kb SGLT1 mRNA species appeared after cell confluence, accompanying expression of the transport activity [14].
  • RESULTS: Western blot analysis clearly demonstrated the presence of Na-K-ATPase, NKCC1 and SGLT1 proteins in both bulbar and palpebral conjunctiva [15].
  • METHODS: Mouse monoclonal antibodies against the alpha1-subunit of Na-K-ATPase and Na-K-Cl cotransporter (NKCC1) and a rabbit polyclonal antibody against the Na-glucose cotransporter (SGLT1) were used in immunoblotting and immunofluorescent labeling of frozen fixed sections isolated from either the bulbar and palpebral regions of the conjunctiva [15].
  • Expression of the Na(+)/glucose cotransporter-1 (SGLT-1) was assayed in PAECs and PCA endothelium by RT-PCR [16].


  1. Reorganization of ZO-1 by sodium-dependent glucose transporter activation after heat stress in LLC-PK1 cells. Ikari, A., Nakano, M., Suketa, Y., Harada, H., Takagi, K. J. Cell. Physiol. (2005) [Pubmed]
  2. Nutritional effects of surgical and medical treatment for short bowel syndrome. Sigalet, D.L., Lees, G.M., Aherne, F.X., Fedorak, R., Keelan, M., Thomson, A.B., van Aerde, J. JPEN. Journal of parenteral and enteral nutrition. (2001) [Pubmed]
  3. Regulation of glucose transporters in LLC-PK1 cells: effects of D-glucose and monosaccharides. Ohta, T., Isselbacher, K.J., Rhoads, D.B. Mol. Cell. Biol. (1990) [Pubmed]
  4. Up-regulation of sodium-dependent glucose transporter by interaction with heat shock protein 70. Ikari, A., Nakano, M., Kawano, K., Suketa, Y. J. Biol. Chem. (2002) [Pubmed]
  5. Aminoglycoside antibiotics reduce glucose reabsorption in kidney through down-regulation of SGLT1. Takamoto, K., Kawada, M., Usui, T., Ishizuka, M., Ikeda, D. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  6. Oxidative and drug-induced alterations in brush border membrane hemileaflet fluidity, functional consequences for glucose transport. Jourd'heuil, D., Meddings, J.B. Biochim. Biophys. Acta (2001) [Pubmed]
  7. Cloning of a membrane-associated protein which modifies activity and properties of the Na(+)-D-glucose cotransporter. Veyhl, M., Spangenberg, J., Püschel, B., Poppe, R., Dekel, C., Fritzsch, G., Haase, W., Koepsell, H. J. Biol. Chem. (1993) [Pubmed]
  8. Apolipoprotein E3 (apoE3) safeguards pig proximal tubular LLC-PK1 cells against reduction in SGLT1 activity induced by gentamicin C. Takamoto, K., Kawada, M., Ikeda, D., Yoshida, M. Biochim. Biophys. Acta (2005) [Pubmed]
  9. Polarity of transport of 2-deoxy-D-glucose and D-glucose by cultured renal epithelia (LLC-PK1). Miller, J.H., Mullin, J.M., McAvoy, E., Kleinzeller, A. Biochim. Biophys. Acta (1992) [Pubmed]
  10. SAAT1 is a low affinity Na+/glucose cotransporter and not an amino acid transporter. A reinterpretation. Mackenzie, B., Panayotova-Heiermann, M., Loo, D.D., Lever, J.E., Wright, E.M. J. Biol. Chem. (1994) [Pubmed]
  11. Recovery from heat shock injury by activation of Na+-glucose cotransporter in renal epithelial cells. Ikari, A., Nakano, M., Ishibashi, M., Kawano, K., Suketa, Y., Harada, H., Takagi, K. Biochim. Biophys. Acta (2003) [Pubmed]
  12. The transport modifier RS1 is localized at the inner side of the plasma membrane and changes membrane capacitance. Valentin, M., Kühlkamp, T., Wagner, K., Krohne, G., Arndt, P., Baumgarten, K., Weber, W., Segal, A., Veyhl, M., Koepsell, H. Biochim. Biophys. Acta (2000) [Pubmed]
  13. Biophysical characteristics of the pig kidney Na+/glucose cotransporter SGLT2 reveal a common mechanism for SGLT1 and SGLT2. Mackenzie, B., Loo, D.D., Panayotova-Heiermann, M., Wright, E.M. J. Biol. Chem. (1996) [Pubmed]
  14. Regulation of Na+/glucose cotransporter (SGLT1) mRNA in LLC-PK1 cells. Yet, S.F., Kong, C.T., Peng, H., Lever, J.E. J. Cell. Physiol. (1994) [Pubmed]
  15. Immunolocalization of Na-K-ATPase, Na-K-Cl and Na-glucose cotransporters in the conjunctival epithelium. Turner, H.C., Alvarez, L.J., Bildin, V.N., Candia, O.A. Curr. Eye Res. (2000) [Pubmed]
  16. Acute effects of glucose and insulin on vascular endothelium. Taubert, D., Rosenkranz, A., Berkels, R., Roesen, R., Schömig, E. Diabetologia (2004) [Pubmed]
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