Genetic analysis of 11β-hydroxysteroid dehydrogenase

Perrin C. White, Jihad Obeid, Anik K. Agarwal, Grace M. Tannin, Heli Nikkila

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

11β-Hydroxysteroid dehydrogenase (11β-OHSD) catalyzes the interconversion of cortisol and cortisone. This activity is postulated to protect the Type I (mineralocorticoid) receptor from excessive concentrations of cortisol, allowing aldosterone to function as a mineralocorticoid. An enzyme with 11β-OHSD activity was isolated from rat liver and the corresponding rat and human cDNA and genomic clones isolated. This enzyme is a member of the short-chain dehydrogenase family. Using site-directed mutagenesis, it was demonstrated that the amino terminus and two highly conserved residues, Tyr-179 and Lys-183, are required for enzymatic function. Examination of patients with apparent mineralocorticoid excess, a syndrome of juvenile hypertension thought to represent 11β-OHSD deficiency, did not reveal any mutations in the HSD11 gene. This disorder may involve an additional enzyme with 11β-OHSD activity or possibly another cortisol metabolizing enzyme.

Original languageEnglish (US)
Pages (from-to)111-115
Number of pages5
JournalSteroids
Volume59
Issue number2
DOIs
Publication statusPublished - 1994

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Keywords

  • 11β-hydroxysteroid dehydrogenase
  • appararent minealocortoid excess
  • cortisol
  • cortisone
  • hypertension
  • mineralocorticoid receptor

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Molecular Biology

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