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pubmed-article:10432221pubmed:abstractTextcDNAs coding for bovine estrogen receptor beta (ERbeta) isoforms were cloned from bovine granulosa cells using a combination of several RT-PCR strategies. The cloned full-length receptor contains an open reading frame of 474 amino acids encoding a protein with high homology to the ERbeta sequences from other species. A second isoform nearly totally lacking the ligand binding domain was cloned that is expressed to relatively high levels in reproductive tissues. Expression of both ERbeta isoforms is down-regulated in corpus luteum and endometrium during the luteal phase of the female cycle. In addition, in granulosa cells several ERbeta isoforms carrying major internal deletions were detected by RT-PCR and cloned. Transient transfection studies expressing the two major bovine ERbeta isoforms together with an ERE reporter construct show estrogen-dependent transactivation by the full-length isoform, whereas the isoform lacking the ligand binding domain did not show any transactivation.lld:pubmed
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pubmed-article:10432221pubmed:authorpubmed-author:WaltherNNlld:pubmed
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pubmed-article:10432221pubmed:pagination37-45lld:pubmed
pubmed-article:10432221pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:10432221pubmed:articleTitleCloning of bovine estrogen receptor beta (ERbeta): expression of novel deleted isoforms in reproductive tissues.lld:pubmed
pubmed-article:10432221pubmed:affiliationInstitute for Hormone and Fertility Research, University of Hamburg, Germany. walther@ihf.delld:pubmed
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