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Am J Physiol Cell Physiol 281: C1365-C1372, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 4, C1365-C1372, October 2001

Stimulation of GLUT-1 glucose transporter expression in response to hyperosmolarity

Daw-Yang Hwang and Faramarz Ismail-Beigi

Departments of Physiology and Biophysics and Medicine, Case Western Reserve University, Cleveland, Ohio 44106

Glucose transporter isoform-1 (GLUT-1) expression is stimulated in response to stressful conditions. Here we examined the mechanisms mediating the enhanced expression of GLUT-1 by hyperosmolarity. GLUT-1 mRNA, GLUT-1 protein, and glucose transport increased after exposure of Clone 9 cells to 600 mosmol/l (produced by addition of mannitol). The stimulation of glucose transport was biphasic: in the early phase (0-6 h) a ~2.5-fold stimulation of glucose uptake was associated with no change in the content of GLUT-1 mRNA, GLUT-1 protein, or GLUT-1 in the plasma membrane, whereas the ~17-fold stimulation of glucose transport during the late phase (12-24 h) was associated with increases in both GLUT-1 mRNA (~7.5-fold) and GLUT-1 protein content. Cell sorbitol increased after 3 h of exposure to hyperosmolarity. The increase in GLUT-1 mRNA content was associated with an increase in the half-life of the mRNA from 2 to 8 h. A 44-bp region in the proximal GLUT-1 promoter was necessary for basal activity and for the two- to threefold increases in expression by hyperosmolarity. It is concluded that the increase in GLUT-1 mRNA content is mediated by both enhanced transcription and stabilization of GLUT-1 mRNA and is associated with increases in GLUT-1 content and glucose transport activity.

glucose transporter isoform-1; sorbitol; aldose reductase; GLUT-1 messenger ribonucleic acid; GLUT-1 promoter; GLUT-1 messenger ribonucleic acid half-life


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