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Department of Cardiovascular Physiology, University of Goettingen, Goettingen, Germany
1Correspondence: Department of Cardiovascular Physiology, University of Goettingen, Humboldtallee 23, 37073 Goettingen, Germany. E-mail: hecker{at}veg-physiol.med.uni-goettingen.de
We investigated the hypothesis that the antiatherosclerotic effect of
17ß-estradiol (E2) is due to a shift in the nitric oxide
(NO)/superoxide (O2-) balance in the vessel
wall, thereby increasing the bioavailability of NO. In human umbilical
vein cultured endothelial cells, E2 (1–100 nmol/l), but
not 17
-estradiol, caused a time- and concentration-dependent
decrease in expression of the NADPH oxidase subunit gp91phox (up to
60% inhibition at both the mRNA and protein level). This effect was
prevented by coincubation with the estrogen receptor antagonists
tamoxifen and ICI 182,780 (1 µmol/l each). Within the same
concentration range, E2 also up-regulated endothelial
nitric oxide synthase expression (
twofold). Moreover, preincubation
of the cells with E2 or a gp91phox antisense
oligonucleotide significantly decreased their capacity to generate
O2- on phorbol ester stimulation (i.e.,
assembly of the active NADPH oxidase complex). Blockade of NO synthase
activity, on the other hand, had no effect on phorbol ester-stimulated
O2- formation. In addition, E2
(100 nmol/l) inhibited the increase in adhesion molecule and chemokine
expression in cells exposed to cyclic strain. Cyclic strain enhanced
endothelial O2- formation, thereby offsetting
the inhibitory effect of NO on the expression of these gene products.
E2 thus seems to act as an antioxidant at the genomic level
which by improving the NO/O2- balance
normalizes expression of proatherosclerotic gene products in
endothelial cells.—Wagner, A. H., Schroeter, M. R., Hecker,
M. 17ß-Estradiol inhibition of NADPH oxidase expression in human
endothelial cells.
Key Words: endothelial nitric oxide synthase • estrogen • monocyte chemoattractant protein-1 • CD54 • superoxide
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