Functional expression of cDNAs for bovine 11β-hydroxylase-aldosterone synthases, P450(11β)-2 and -3 and their chimeras

Yasuki Nonaka, Mitsuhiro Okamoto, Ken Ichirou Morohashi, Shirou Kirita, Toshihide Hashimoto, Tsuneo Omura

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Two molecular species of bovine P450(11β), P450(11β)-2 and P450(11β)-3 have been identified, in which the amino acid differences were found at the 6th, 36th and 82nd positions from the NH2-termini of the mature proteins. They catalyzed the 11β-, 18- and 19-hydroxylation and aldosterone formation from 11-deoxycorticosterone, and the rate of production of 18-hydroxycorticosterone and aldosterone by P450(11β)-3 was greater than that by P450(11β)-2 [Morohashi et al., J. Biochem. 107 (1990) 635-640]. In this study, chimeric clones were constructed whose 6th, 36th and 82nd amino acid residues were exchanged with each other. Two original clones and six chimeric clones were expressed in COS-7 cells, and their steroidogenic activities studied. The ratio of aldosterone or 18-hydroxycorticosterone production to corticosterone production by one clone was compared with that of the other. The ratios for the four clones having Gly36 [P450(11β)-3 type] were 0.08-0.22, whereas those for the clones having Ser36 [P450(11β)-2 type] were 0.03-0.05, suggesting that the Gly36 structure is important for aldosterone production.

Original languageEnglish
Pages (from-to)779-780
Number of pages2
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume41
Issue number3-8
DOIs
Publication statusPublished - Mar 1992

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

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