Immunohistochemical Demonstration of the Mineralocorticoid Receptor, 11β-Hydroxysteroid Dehydrogenase-1 and-2, and Hexose-6-phosphate Dehydrogenase in Rat Ovary

An IHC survey using several monoclonal antibodies against different portions of the rat mineralocorticoid receptor (MR) molecule demonstrated significant specific MR immunoreactivity in the ovary, prompting further study of the localization of MR and of determinants of extrinsic MR ligand specificity, 11 beta-hydroxysteroid dehydrogenase (11 beta-HSD) types 1 and 2, and hexose-6-phosphate clehydrogenase (H6PDH). MR expression (real-time RT-PCR and Western blot) did riot differ significantly in whole rat ovaries at early diestrus, late diestrus, estrus, and a few hours after ovulation. MR immunostaining was most intense in corporal lutea cells, light to moderate in oocytes and granulosa cells, and least intense in theca cells. Light immunoreactivity for 11 beta-HSD2 occurred in most cells, with some mural granulosa cells; of mature follicles staining more strongly. The distribution of immunoreactivity for 11 beta-HSD1 and H6PDH required to generate NADPH, the cofactor required for reductase activity of 11 beta-HSD1, was similar, with the most-intense staining in the cytoplasm of corporal lutea and theca cells and light or no staining in the granulosa and oocytes. MR function in the ovary is as yet unclear, but distinct patterns of distribution of 11 beta-HSD1 and -2 and H6PDH suggest that the ligand for MR activation in different cells of the ovary maybe differentially regulated. (J Histochem Cytochem 57:633-641, 2009)