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Biochem Biophys Res Commun. 1998 Aug 28;249(3):797-803.

Molecular cloning and characterization of the rat ovarian 20 alpha-hydroxysteroid dehydrogenase gene.

Author information

1
Department of Physiology and Biophysics, University of Illinois at Chicago 60612, USA.

Abstract

The rat 20 alpha-hydroxysteroid dehydrogenase (20 alpha-HSD) is an enzyme responsible for the catabolism of progesterone to the inactive 20 alpha-hydroxprogesterone. We have previously shown that the expression of this enzyme is not regulated by post-translational modification, but at the level of transcription. In this study we have established that the 20 alpha-HSD gene contains nine exons and have isolated a 2.5 kb promoter region. The transcription start site was identified and a TATA box was found. 5' deletions of this promoter significantly decreased basal promoter activity. Treatment with forskolin led to a dose dependent inhibition of the 2.5kg-20 alpha-HSD-luciferase construct. Computer analysis identified one CRE, two Nur77 response elements, two putative AP1 sites and one progesterone response element half-site. In summary, we have identified and partially characterized the promoter region of the rat ovarian 20 alpha-HSD and demonstrated that the regulatory elements for 20 alpha-HSD are present within a 2.5 kb 5' flanking region of the gene.

PMID:
9731216
DOI:
10.1006/bbrc.1998.9229
[Indexed for MEDLINE]

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