Cloning of cDNA encoding an NAD+-dependent isoform of 11βhydroxysteroid dehydrogenase in sheep kidney

Anil K. Agarwal, Tomoatsu Mune, Carl Monder, Perrin C. White

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


11βHydroxysteroid dehydrogenase (11-HSD) catalyzes the conversion of cortisol to cortisone and corticosterone to 11-dehydrocorticosterone. This activity may be required to confer normal ligand specificity upon the mineralocorticoid receptor. Although an isozyme of 11-HSD was previously isolated from rat liver, a different isozyme is apparently expressed in mineralocorticoid target tissues. We isolated a sheep kidney cDNA clone encoding this isozyme by expression screening using Xenopus oocytes. The cDNA is 1.8 kb in length and encodes a protein of 427 amino acid residues with a predicted Mr of 46,700. When expressed in oocytes, this enzyme functions as an NAD+-dependent 11βdehydrogenase with very high affinity for steroids, but it has no detectable reductase activity. It is 37% identical in amino acid sequence to an NAD+-dependent isozyme of 17βhydroxysteroid dehydrogenase, but only 20% identical to the NADP+-dependent liver isozyme of 11-HSD. It is expressed at high levels in the kidney and adrenal and at lower levels in the colon. The corresponding gene is present in a single copy in the sheep genome. In humans, this gene is a candidate locus for the syndrome of apparent mineralocorticoid excess, a form of hypertension postulated to result from 11-HSD deficiency in mineralocorticoid target tissues.

Original languageEnglish (US)
Pages (from-to)389-397
Number of pages9
JournalEndocrine Research
Issue number1-2
StatePublished - 1995

ASJC Scopus subject areas

  • Endocrinology


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