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, but
not -
, in en face arterial endothelium
Department of Physiology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3
Rapid, nongenomic effects of
17
-estradiol (E2) in endothelial cells are postulated to
arise from membrane-associated estrogen receptors (ERs), which have not
been visualized in vascular tissue. To identify membrane ERs, we used
multiple site-directed ER
or ER antibodies to label en face rat
cerebral and coronary arterial endothelia. Western blots revealed a
novel 55-kDa ER isoform. Three-dimensional images of cells labeled
with these antibodies and markers for the nucleus and caveolin-1 were
acquired with a wide-field microscope, deconvolved, and numerically
analyzed. We found ER in the nucleus and cell periphery, where
one-third colocalized with caveolin-1. The receptor location was
dependent on the epitope of the antibody. Human ovarian surface
epithelium produced similar results; but in rat myometrium, the
distribution was epitope independent and nuclear. ER distribution
was predominately intranuclear and epitope independent. A small amount
of ER colocalized with ER within the nucleus. The results were
identical in both arterial preparations and insensitive to
E2. We postulate that the different ER conformations at
the membrane, in the nucleus, and between different cell types allow
E2 to trigger cell- and location-specific signaling cascades.
estrogen receptors; immunocytochemistry; immunofluorescence; deconvolution; caveolin-1; colocalization
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