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Endocrinology, Vol 137, 1123-1128, Copyright © 1996 by Endocrine Society
ARTICLES |
BL Roland and JW Funder
Baker Institute of Medical Research, Prahan, Victoria, Australia.
In the rat, the enzyme 11beta-hydroxysteroid dehydrogenase 2 (11betaHSD2) converts the glucocorticoid corticosterone into receptor- inactive 11-dehydrocorticosterone, thereby allowing preferential access of aldosterone to mineralocorticoid receptors (MR). The present study examines the distribution of this enzyme by in situ hybridization, using a homologous complementary RNA probe for 11betaHSD2. 11betaHSD2 messenger RNA was detected in classic epithelial aldosterone target tissues (kidney, salivary glands, and colon), the female reproductive system (ovary, oviduct, uterus, and placenta), and the adrenals; levels in heart, testis, and liver were below the limits of detection. We interpret the finding of 11betaHSD2 expression in both classical MR- containing aldosterone target tissues and a variety of other tissue as evidence that in the rat, the enzyme may play physiological roles in addition to that of excluding glucocorticoids from epithelial MR.
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