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1 Department of Physiology/Endocrinology, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at Gothenburg University, Gothenburg, Sweden
2 Reproductive Medicine, Department of Obstetrics and Gynecology, Institute of Clinical Sciences, Sahlgrenska Academy, Sahlgrenska University Hospital, Gothenburg University, Gothenburg, Sweden; Department of Physiology/Endocrinology, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at Gothenburg University, Gothenburg, Sweden
3 Centre for Cellular Imaging, Core facilities, The Sahlgrenska Academy at Gothenburg University, Gothenburg, Sweden
4 Perinatal Center, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at Gothenburg University, Gothenburg, Sweden
5 Division of Endocrinology, Department of Internal Medicine, The Sahlgrenska Academy at Gothenburg University, Gothenburg, Sweden
6 Reproductive Medicine, Department of Obstetrics and Gynecology, Institute of Clinical Sciences, Sahlgrenska Academy, Sahlgrenska University Hospital, Gothenburg University, Gothenburg, Sweden
* To whom correspondence should be addressed. E-mail: ruijin.shao{at}fysiologi.gu.se.
In the present study, we have investigated the intracellular localization and regulatory patterns for ERbeta isoforms in rat fallopian tubes. Western blot analysis reveals that two ERbeta isoforms corresponding to ERbeta1 and ERbeta2 are expressed in rat fallopian tubes. However, ERbeta2 is the predominant form of ERbeta in this tissue. Confocal imaging and immunohistochemical analysis provide ample evidences that ERbeta expression is limited almost exclusively to the ciliated epithelial cells in contrast to ERalpha, which is widely distributed. Furthermore, within the ciliated epithelial cells, ERbeta is colocalized with beta-tubulin IV at stem portion of the cilia. We show that ERbeta2 protein expression is tightly regulated by 17beta-estradiol (E2) or diarylpropionitrile (DPN) in a time-dependent manner without changes in ERbeta1 expression. These estrogenic effects are inhibited by an ER antagonist ICI 182,780. In addition, significant alteration of ERbeta immunoreactivity is only detected histologically in the ampullary region. Since the cilia are considered an essential determinant of tubal transport, we demonstrate that E2- or DPN-induced ERbeta2 activation is associated with alterations in tubal protein expression crucial for the regulation of calcium-dependent ciliary beating. Given the coordinated regulation and interaction of ER and progesterone receptor in the cilia, we hypothesize that tubal ERbeta2 may facilitate the estrogen-mediated transport process by processing protein-protein interaction under physiological and/or pathological conditions. This study shows for the first time that a previously unrecognized localization of ERbeta isoform in rat fallopian tubes.
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