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1 Endocrine Section and Research Service, G.V. (Sonny) Montgomery VA Medical Center, Jackson, MS, USA; Division of Endocrinology, The University of Mississippi Medical Center, Jackson, MS, USA; Department of Medicine, University of Missouri-Columbia, Columbia, MO, USA
2 Department of Veterinary Biomedical Sciences, University of Missouri-Columbia, Columbia, MO, USA
3 Department of Medicine, University of Missouri-Columbia, Columbia, MO, USA
4 Division of Endocrinology, The University of Mississippi Medical Center, Jackson, MS, USA
5 Department of Pathology, The University of Mississippi Medical Center, Jackson, MS, USA
* To whom correspondence should be addressed. E-mail: elise.gomezsanchez{at}med.va.gov.
The 11-beta-hydroxysteroid dehydrogenase type1 (11
HSD1) is an NADP+-dependent oxido-reductase, usually reductase, of major glucocorticoids. The NAD+-dependent 11HSD2 is an oxidase that inactivates cortisol and corticosterone, conferring extrinsic specificity of the mineralocorticoid receptor for aldosterone. We reported that addition of a reducing agent to renal homogenates results in the monomerization of 11HSD2 dimers and a significant increase in NAD+-dependent corticosterone conversion. Estrogenic effects on expression, dimerization, and activity of the kidney 11HSD1 and 2 enzymes are described herein. Renal 11HSD1 mRNA and protein expression were decreased to very low levels by estradiol (E2) treatment of both intact and castrated male rats; testosterone had no effect. NADP+-dependent enzymatic activity of renal homogenates from E2-treated rats measured under non-reducing conditions was less than that of homogenates from intact animals. Addition of 10mM dithiothreitol to aliquots from these same homogenates abrogated the difference in NADP+-dependent activity between E2-treated and control rats. In contrast, 11HSD2 mRNA and protein expressions were significantly increased by E2-treatment. There was a marked increase in the number of juxtamedullary proximal tubules stained by the antibody against 11HSD2 after the administration of E2. Notwithstanding, neither the total corticosterone and 11-dehydrocorticosterone excreted in the urine, nor their ratio, differed between E2 or vehicle-treated rats. NAD+-dependent enzymatic activity in the absence or presence of a reducing agent demonstrated that the increase in 11HSD2 protein was not associated with an increase in in vitro activity unless the dimers were reduced to monomers.
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