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17ß-Estradiol Stimulates Arachidonate Release from Human Amnion-Like WISH Cells through a Rapid Mechanism Involving a Membrane Receptor

Department of Biology, Sections of General Physiology and Comparative Anatomy, University of Ferrara, 44100-I Ferrara, Italy

Address all correspondence and requests for reprints to: Dr. Maria E. Ferretti, Department of Biology, Section of General Physiology, University of Ferrara, via Luigi Borsari 46, 44100-I Ferrara, Italy. E-mail: clm{at}dns.unife.it.

17ß-Estradiol (17ß-E₂) greatly and dose-dependently stimulates [³H]arachidonic acid (AA) release from the human amnion-like Wistar Institute Susan Hayflick (WISH) cells. This action is abolished by the phospholipase A₂ inhibitor AACOCF₃, significantly reduced by the estrogen receptor (ER) antagonist ICI 182,780, and uninfluenced by cycloheximide. The estradiol-BSA conjugate E₂coBSA, which binds putative membrane ERs and is unable to enter the cell, also highly stimulates [³H]AA release from WISH cells, although to a lesser extent compared with 17ß-E₂. The fluorescent conjugate E₂coBSA-FITC specifically binds to the surface of a subset of intact WISH cells, and labeling intensity appears dose and time dependent. Cell permeabilization results in a dense intracellular staining, mainly in the peripheral cytoplasm. H-150, an antibody against the N terminus of human ERß, also labels the plasma membrane of intact WISH cells and the cytoplasm of permeabilized cells. Almost no labeling is observed using ER-21, an antibody against the N terminus of human ER. RT-PCR evidences the presence of mRNA for ERß, not for ER. Our data suggest that 17ß-E₂ stimulates [³H]AA release from WISH cells through an apparently nongenomic pathway and interaction with membrane binding sites. These last are, at least in part, similar if not identical to ERß.

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