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a Departments of Animal Sciences and
b Biochemistry and Child Health, University of Missouri at Columbia, Columbia, Missouri 65211
The potential role of estrogen receptor-ß (ERß) in normal ovarian folliculogenesis and in reproductive disorders such as ovarian follicular cysts has not been well defined. Therefore, we were interested in cloning, sequencing, and localizing ERß mRNA and protein within the bovine ovary. Bovine ERß (bERß) was amplified by reverse transcription-polymerase chain reaction (RT-PCR), then cloned and sequenced. Results showed that the open reading frame of bERß cDNA spanned 1584 nucleotides encoding a protein of 527 amino acids. The N-terminal region of bERß was found to be 80% homologous to human and mouse ERß and 79% homologous to rat ERß. Bovine ERß DNA-binding domain was 100% homologous to human, mouse, and rat ERß sequences. The C-terminal/ligand-binding domain of bERß was 89% homologous to human, 86% homologous to mouse, and 88% homologous to rat ERß. Human and bovine ERß amino acid sequences are similar in that their coding region extended farther 5' than initially reported for the published rat ERß sequence. Using in situ hybridization and immunohistochemistry, ERß mRNA and protein, respectively, were demonstrated to be present in granulosa cells of antral follicles in various stages of follicular growth. These findings suggest a role for bERß in ovarian follicular growth and maturation.
2 Correspondence: Dennis B. Lubahn, University of Missouri, 163 ASRC, 920 East Campus Drive, Columbia, MO 65211. FAX: 573 882 6827; lubahnd{at}missouri.edu
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