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 language | English (US) |
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Pages (from-to) | 111-115 |
Number of pages | 5 |
Journal | Steroids |
Volume | 59 |
Issue number | 2 |
DOIs | |
State | Published - Feb 1994 |
Keywords
- 11β-hydroxysteroid dehydrogenase
- appararent minealocortoid excess
- cortisol
- cortisone
- hypertension
- mineralocorticoid receptor
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology
- Pharmacology
- Clinical Biochemistry
- Organic Chemistry