Abstract
RECENT studies have indicated that a family of structurally related proteins with distinct but overlapping tissue distributions are responsible for facilitative glucose transport in mammalian tissues1—13. Insulin primarily stimulates glucose transport by inducing the redistribution of a unique glucose transporter protein from an intracellular pool to the plasma membrane3. This 509-amino-acid integral membrane protein, termed GLUT-4 (ref. 2), is the main insulin-responsive glucose transporter in adipose and muscle tissues1—3. We have observed a dramatic decrease (tenfold) in the steady-state levels of GLUT-4 messenger RNA in adipose tissue from fasted rats or rats made insulin deficient with streptozotocin. Insulin treatment of the streptozotocin-diabetic rats or refeeding the fasted animals causes a rapid recovery of the GLUT-4 mRNA to levels significantly above those observed in untreated control animals. By contrast, the levels of the erythrocyte/HepG2/rat brain-type glucose transporter mRNA remain essentially unchanged under these conditions. These data suggest that the in vivo expression of GLUT-4 mRNA in rat adipose tissue is regulated by insulin.
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Sivitz, W., DeSautel, S., Kayano, T. et al. Regulation of glucose transporter messenger RNA in insulin-deficient states. Nature 340, 72–74 (1989). https://doi.org/10.1038/340072a0
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DOI: https://doi.org/10.1038/340072a0
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