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Vol. 54, Issue 4, 740-747, October 1998
Department of Biological Chemistry, Medical School, The University
of Michigan, Ann Arbor, Michigan 48109
The regulation of cytochrome P450 (CYP) 2E1, the ethanol-inducible
isoform, is particularly complex. The level is affected by a variety of
other foreign compounds, by insulin (as studied in several
laboratories), and by triiodothyronine (T3), which has not
been previously examined at the molecular level. In the present
investigation, a stably transfected HepG2 cell line harboring a rabbit
CYP2E1 minigene containing the coding sequence together with 1.6 kilobases of the 5' flanking region and the untranslated region (UTR), as well as 0.5 kilobases of the 3' UTR, was established. Western blot analysis showed that 1 µM insulin decreased
the CYP2E1 protein level in a dose- and time-dependent manner, whereas
1 µM T3 increased the level 2-fold in 1 day
and 8-fold in 5 days. Similarly, steady state CYP2E1 mRNA levels were
decreased by insulin but were increased by T3. Neither
hormone affected the transcription rate of the CYP2E1 5'
flanking region with an UTR/luciferase fusion gene, indicating that the
regulation is post-transcriptional in this system under our
experimental conditions. When the CYP2E1 3' UTR was
removed from the minigene, CYP2E1 mRNA and protein were up-regulated by
insulin but were not affected by T3. These findings,
including mRNA half-life determinations, indicate that the effects of
insulin and T3 are a result of altered mRNA stability and
that the 3' UTR of CYP2E1 contains regulatory
information for these hormone-mediated effects.
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