Cloning of cDNA encoding an @entity2125 -dependent isoform of 11 beta-hydroxysteroid dehydrogenase in XXXX kidney.

@entity230 @entity2125 @entity821 @entity1 @entity1238 @entity742 @entity101 @entity535 @entity19674 @entity1110 @entity2819 @entity19673 @entity701 @entity35 @entity19672
11 beta-Hydroxysteroid dehydrogenase (11-HSD) catalyzes the conversion of @entity701 to @entity821 and @entity2819 to @entity19672 . This activity may be required to confer normal ligand specificity upon the @entity19673 . Although an isozyme of 11-HSD was previously isolated from @entity35 liver, a different isozyme is apparently expressed in mineralocorticoid target tissues. We isolated a @entity742 kidney cDNA clone encoding this isozyme by expression screening using @entity1238 oocytes. The cDNA is 1.8 kb in length and encodes a protein of 427 @entity535 residues with a predicted M(r) of 46,700. When expressed in oocytes, this enzyme functions as an @entity2125 -dependent 11 beta-hydrogenase with very high affinity for @entity230 , but it has no detectable reductase activity. It is 37% identical in @entity535 sequence to an @entity2125 -dependent isozyme of @entity19674 dehydrogenase, but only 20% identical to the @entity1110 -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 @entity742 genome. In @entity1 , this gene is a candidate locus for the syndrome of apparent mineralocorticoid excess, a form of @entity101 postulated to result from 11-HSD deficiency in mineralocorticoid target tissues.
