Nucleic Acids Research, Vol 25, Issue 20 4035-4040, Copyright © 1997 by Oxford University Press
S Hayashi, K Hajiro-Nakanishi, Y Makino, H Eguchi, J Yodoi and H Tanaka
Redox regulation of transcription factors has recently been demonstrated
for AP-1, NF-kappaB, Sp-1 and glucocorticoid receptor in vitro and in vivo.
The redox state in estrogen-dependent cells possibly influences the
function of estrogen receptor (ER), and the regulation of the function of
ER is essential for understanding of growth and differentiation of these
cells, as well as promotion and progression of estrogen-associated cancer.
In this paper, we first analyzed the effects of redox state on
transcriptional activity of ER in terms of pS2 mRNA expression and
transfection of ERE-CAT plasmid in human breast cancer cells. Addition of
H2O2 at low concentrations lowered levels of pS2 mRNA and also
down-regulated ERE-CAT activity, which was recovered by transfection of
thioredoxin (TRX) expression vector. Next, the transfection of antisense
TRX plasmid diminished ERE-CAT activity, and the activity was recovered by
co-transfected sense TRX. Furthermore, specific DNA binding activity of
recombinant ER was inhibited by sulfhydryl-modifying reagents and restored
by the addition of recombinant TRX protein in electrophoretic mobility
shift assay. These results in vitro and in vivo revealed that the
transcription activity of ER is strongly influenced by its redox state,
which is reversibly modulated by endogenous redox effector protein, TRX.
ARTICLES
Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator
Department of Biochemistry, Saitama Cancer Center Research Institute, Komuro, Ina, Saitama 362, Japan. shayashi@saitama-cc.go.jp
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