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Am J Physiol Heart Circ Physiol 284: H1295-H1306, 2003. First published December 12, 2002; doi:10.1152/ajpheart.00781.2002
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Vol. 284, Issue 4, H1295-H1306, April 2003

Epitope-dependent localization of estrogen receptoralpha , but not -beta , in en face arterial endothelium

Pauline Dan, Joyce C. Y. Cheung, David R. L. Scriven, and Edwin D. W. Moore

Department of Physiology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3

Rapid, nongenomic effects of 17beta -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 ERalpha or ERbeta antibodies to label en face rat cerebral and coronary arterial endothelia. Western blots revealed a novel 55-kDa ERalpha 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 ERalpha 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. ERbeta distribution was predominately intranuclear and epitope independent. A small amount of ERalpha colocalized with ERbeta within the nucleus. The results were identical in both arterial preparations and insensitive to E2. We postulate that the different ERalpha 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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