PMID: 9430822Feb 7, 1998Paper

Functional and expression analysis of ovine steroid 11 beta-hydroxylase (cytochrome P450 11 beta)

Endocrine Research
W C BoonJ P Coghlan

Abstract

In this study, the ovine steroid 11 beta-hydroxylase (P450(11 beta) or CYP11B) cDNA previously reported by us (1) was transfected into COS-7 cells. Using 3H-11-deoxycorticosterone (3H-DOC) as the substrate, and paper partition chromatography for separation of steroid products, the expressed enzyme was shown to catalyse the conversion of DOC to corticosterone (B), 18-hydroxy-11-deoxycorticosterone (18-OH-DOC), 18-hydroxy-corticosterone (18-OH-B), and aldosterone (ALDO). These results suggest that the expressed ovine cDNA exhibited 11 beta-hydroxylase, 18-hydroxylase and aldosterone synthesis activities. The enzymatic activity of the enzyme was further analysed by adding unlabelled steroids to compete with 3H-DOC. The conversion of 3H-DOC to 3H-ALDO was inhibited by the addition of excess DOC, B and 18-OH-DOC, indicating that all these steroids were potential substrates of the enzyme. The results also demonstrated that 18-hydroxylation could occur before 11 beta-hydroxylation with this enzyme. However, the addition of excess cold 18-OH-B had no significant effect on the level of 3H-ALDO that was synthesised. This result could imply that 18-OH-B is not an intermediate involved in the conversion of DOC to aldosterone, or, more like...Continue Reading

References

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Citations

Nov 11, 1998·Clinical and Experimental Pharmacology & Physiology. Supplement·W C BoonJ G McDougall
Mar 21, 2020·Molecular Biology and Evolution·Carrie F Olson-Manning
Jun 5, 1998·Clinical and Experimental Pharmacology & Physiology·W C BoonJ P Coghlan
Jan 15, 1999·Endocrine Research·W C EngelandJ C Rose
Nov 11, 1998·Clinical and Experimental Pharmacology & Physiology. Supplement·E M WintourL Shandley
Aug 18, 2005·Biochemical and Biophysical Research Communications·Mitsuhiro OkamotoJunko Doi

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