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J Biol Chem, Vol. 275, Issue 7, 5026-5030, February 18, 2000
From the Estradiol (E2) causes
endothelium-dependent vasodilation, mediated, in part, by
enhanced nitric oxide (NO) release. We have previously shown that
E2-induced activation of endothelial nitric oxide synthase
(eNOS) reduces its calcium dependence. This pathway of eNOS activation
is unique to a limited number of stimuli, including shear stress, the
response to which is herbimycin-inhibitable. Consistent with this,
herbimycin and geldanamycin pretreatment of human umbilical vein
endothelial cells (HUVEC) abrogated E2-stimulated NO
release and cGMP production, respectively. These benzoquinone ansamycins are potent inhibitors of Hsp90 function, which has recently
been shown to play a role in stimulus-dependent eNOS activation. As in response to shear, E2 induced an
Hsp90-eNOS association, peaking at 30 min and completely inhibited by
the conventional estrogen receptor antagonist ICI 182,780. These
findings suggest that Hsp90 plays an important role in the rapid,
estrogen receptor-mediated modulation of eNOS activation by estrogen.
Estrogen Stimulates Heat Shock Protein 90 Binding to Endothelial
Nitric Oxide Synthase in Human Vascular Endothelial Cells
EFFECTS ON CALCIUM SENSITIVITY AND NO RELEASE*
,,,,§, and¶
Division of Cardiovascular Medicine and
Molecular Cardiobiology, Boyer Center for Molecular Medicine and
§ Department of Pharmacology, Yale University School of
Medicine, New Haven, Connecticut 06536-0812
*
This work was supported by National Institutes of Health
Grants HL61782 (to J. R. B.) and HL61371 (to W. C. S.) and by an educational grant from Parke-Davis.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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