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Gene Review

SLC2A4  -  solute carrier family 2 (facilitated...

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Disease relevance of SLC2A4


High impact information on SLC2A4

  • Insulin-perfused muscles showed significant increases in glucose uptake and GLUT4 translocation, but AMPK activation was not significantly changed from basal levels [2].
  • 5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle [2].
  • This study was designed to determine whether the increase in glucose uptake observed with AMPK activation by AICA-riboside is due to GLUT4 translocation from an intracellular location to the plasma membranes, similar to that seen in response to contraction [2].
  • These results provide evidence that the increased glucose uptake observed with AMPK activation by AICA-riboside in perfused rat hindlimb muscles is due to an increase in the translocation of GLUT4 to surface membranes [2].
  • A GLUT4-like protein was detected by immunoblot assay in all insulin-responsive tissues from calf and goat (heart, skeletal muscle, adipose tissue) but not in liver, brain, erythrocytes and intestine [3].

Biological context of SLC2A4


Anatomical context of SLC2A4


Associations of SLC2A4 with chemical compounds

  • Previous studies have shown that the expression of the insulin-sensitive glucose transporter (GLUT4) is lower in oxidative muscles than in glycolytic muscles in bovines and goats in contrast to observations in rats [6].
  • Although the amino acid sequence of the GLUT4 COOH-terminal region is highly conserved among the species so far reported, one amino acid (Asp) of the region was replaced by His in bovine GLUT4 [4].
  • METHODS AND RESULTS: Glucose deprivation and indinavir, a GLUT4 antagonist, were used to assess the role of GLUT4 and non-GLUT4 transporters in vascular reactivity [10].
  • Indinavir caused a less profound attenuation of maximal 5-HT-mediated contraction in these vessels, corresponding to the lower GLUT4 levels in the hypertensive aortas [10].
  • We also observed a 46% decrease in GLUT4 expression in aortas from angiotensin II hypertensive mice [10].

Other interactions of SLC2A4


Analytical, diagnostic and therapeutic context of SLC2A4


  1. Weaning marginally affects glucose transporter (GLUT4) expression in calf muscles and adipose tissues. Hocquette, J.F., Castiglia-Delavaud, C., Graulet, B., Ferré, P., Picard, B., Vermorel, M. Br. J. Nutr. (1997) [Pubmed]
  2. 5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle. Kurth-Kraczek, E.J., Hirshman, M.F., Goodyear, L.J., Winder, W.W. Diabetes (1999) [Pubmed]
  3. Glucose-transporter (GLUT4) protein content in oxidative and glycolytic skeletal muscles from calf and goat. Hocquette, J.F., Bornes, F., Balage, M., Ferre, P., Grizard, J., Vermorel, M. Biochem. J. (1995) [Pubmed]
  4. Molecular cloning and mRNA expression of the bovine insulin-responsive glucose transporter (GLUT4). Abe, H., Morimatsu, M., Nikami, H., Miyashige, T., Saito, M. J. Anim. Sci. (1997) [Pubmed]
  5. Changes in gene expression of glucose transporters in lactating and nonlactating cows. Komatsu, T., Itoh, F., Kushibiki, S., Hodate, K. J. Anim. Sci. (2005) [Pubmed]
  6. Insulin-sensitive glucose transporter transcript levels in calf muscles assessed with a bovine GLUT4 cDNA fragment. Hocquette, J.F., Graulet, B., Castiglia-Delavaud, C., Bornes, F., Lepetit, N., Ferre, P. Int. J. Biochem. Cell Biol. (1996) [Pubmed]
  7. A synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain inhibits insulin action on glucose transport in rat adipocytes. Shibata, H., Omata, W., Suzuki, Y., Tanaka, S., Kojima, I. J. Biol. Chem. (1996) [Pubmed]
  8. Gene expression of resistin in adipose tissue and mammary gland of lactating and non-lactating cows. Komatsu, T., Itoh, F., Mikawa, S., Hodate, K. J. Endocrinol. (2003) [Pubmed]
  9. The insulin-dependent glucose transporter isoform 4 is expressed in bovine blastocysts. Navarrete Santos, A., Augustin, R., Lazzari, G., Galli, C., Sreenan, J.M., Fischer, B. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  10. GLUT4 facilitative glucose transporter specifically and differentially contributes to agonist-induced vascular reactivity in mouse aorta. Park, J.L., Loberg, R.D., Duquaine, D., Zhang, H., Deo, B.K., Ardanaz, N., Coyle, J., Atkins, K.B., Schin, M., Charron, M.J., Kumagai, A.K., Pagano, P.J., Brosius, F.C. Arterioscler. Thromb. Vasc. Biol. (2005) [Pubmed]
  11. In vitro and in vivo culture effects on mRNA expression of genes involved in metabolism and apoptosis in bovine embryos. Knijn, H.M., Wrenzycki, C., Hendriksen, P.J., Vos, P.L., Zeinstra, E.C., van der Weijden, G.C., Niemann, H., Dieleman, S.J. Reprod. Fertil. Dev. (2005) [Pubmed]
  12. Nutritional status induces divergent variations of GLUT4 protein content, but not lipoprotein lipase activity, between adipose tissues and muscles in adult cattle. Bonnet, M., Faulconnier, Y., Hocquette, J.F., Bocquier, F., Leroux, C., Martin, P., Chilliard, Y. Br. J. Nutr. (2004) [Pubmed]
  13. Postnatal development of glucose transporter proteins in bovine skeletal muscle and adipose tissue. Abe, H., Kawakit, Y., Hodate, K., Saito, M. J. Vet. Med. Sci. (2001) [Pubmed]
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