Cloning and expression of rat cDNA encoding corticosteroid 11 beta-dehydrogenase

J Biol Chem. 1989 Nov 15;264(32):18939-43.


Corticosteroid 11 beta-dehydrogenase (11-DH) catalyzes the conversion of cortisol to the inactive metabolite cortisone. Absence of 11-DH activity leads to a potentially fatal form of childhood hypertension termed apparent mineralocorticoid excess. As a first step in elucidating the molecular basis of this disorder, we isolated and characterized a rat cDNA clone encoding 11-DH. This clone hybridized to a single mRNA species in liver, kidney, and testis RNA but not to RNA from heart. The insert was 1265 base pairs long and included an 861-base pair open reading frame encoding 287 amino acids. A search of sequence databases revealed that 11-DH is identical in about 27% of amino acid residues to ribitol dehydrogenase from Klebsiella and to the product of the nodG gene from the nitrogen-fixing bacterium, Rhizobium meliloti, thus defining a new superfamily of genes encoding dehydrogenases. The 11-DH cDNA was expressed by transfection into Chinese hamster ovary cells under the control of an SV40 promoter. The expressed enzyme mediated both 11 beta-dehydrogenation and the reverse 11-oxoreduction reaction. Southern blot analysis of rat and human DNA suggested that additional genes related to 11-DH exist in both species.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 11-beta-Hydroxysteroid Dehydrogenases
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular*
  • DNA / genetics*
  • DNA / isolation & purification
  • Gene Expression*
  • Gene Library
  • Genes
  • Humans
  • Hydroxysteroid Dehydrogenases / genetics*
  • Liver / enzymology
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • Rats
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid


  • DNA
  • Hydroxysteroid Dehydrogenases
  • 11-beta-Hydroxysteroid Dehydrogenases

Associated data

  • GENBANK/J05107