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J Biol Chem, Vol. 273, Issue 41, 26969-26976, October 9, 1998
From INSERM U490, Centre Universitaire des Saints-Pères, 45 rue des Saints-Pères, 75006 Paris, France
Oxidative stress interferes with several cellular
functions, in particular transcriptional regulation. We show here that
the human cytochrome P450 1A1 (CYP1A1) is down-regulated at the
transcriptional level by oxidative stress. Basal as well as
2,3,7,8-tetrachloro-p-dioxin-induced promoter activities
are strongly impaired by H2O2 treatment or glutathione depletion with L-buthionine-(S,R)-sulfoximine.
Tumor necrosis factor
Down-regulation of Cytochrome P450 1A1 Gene Promoter by Oxidative
Stress
CRITICAL CONTRIBUTION OF NUCLEAR FACTOR 1
inhibits CYP1A1 expression, and this
inhibition is prevented by the antioxidant pyrrolidine dithiocarbamate.
We show that these regulations depend on the integrity of the nuclear factor 1 (NFI) site located in the proximal promoter. We therefore examined the redox regulation of this transcription factor. Treatment of human HepG2 or rat H4 hepatoma cells with
H2O2 or
L-buthionine-(S,R)-sulfoximine inactivates the binding of
the NFI transcription factor to its DNA consensus sequence.
Furthermore, H2O2 treatment leads to a dose-dependent decrease of reporter gene expressions driven
by promoters containing NFI binding sites. Glutathione depletion and
catalase inhibition also repress a NFI-driven promoter. Under the same
conditions, the CP-1 transcription factor activity is not affected by
oxidative stress. Thus, NFI seems particularly sensitive to oxidative
stress. This accounts, at least partially, for the regulation of
cyp1A1 gene expression.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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