Boado R J, Pardridge W M
Department of Medicine, CCLA School of Medicine 90095, USA.
Comp Biochem Physiol B Biochem Mol Biol. 1997 Oct;118(2):309-12. doi: 10.1016/s0305-0491(97)00170-3.
The blood-brain barrier GLUT1 glucose transporter is under post-transcriptional regulation, and the 5'-untranslated region (5'-UTR) of the GLUT1 mRNA increases its translational rate in mammalian cells. To obtain more insight into the mechanism of translational control of GLUT1, the present investigation studied the translational efficiency of capped full-length synthetic human (h) and rabbit (rab) GLUT1 mRNA and both 5'- and 3'-UTR deleted hGLUT1 mRNAs in both mammalian and plant cell free translation systems. Translation efficiency of both h- and rabGLUT1 mRNA was increased 3- to 6-fold in rabbit retyculocyte lysate (RRL) compared with wheat germ extract (WGE). Confirming previous observations, deletion of 5'- and 5'/-3'-UTR markedly reduced the translation efficiency of the h-GLUT1 transcript in RRL. On the contrary, these deletions markedly increased the translation of GLUT1 in WGE. The present data provide additional evidence suggesting that the 5'-UTR of the GLUT1 mRNA contains cis-acting elements involved in the translational activation of the GLUT1 gene in mammalian cells and that factors involved in this cis/trans-acting interaction are either absent or down-regulated in plant systems.