Molecular Cloning and Characterization of the Rat Ovarian 20α-Hydroxysteroid Dehydrogenase Gene

The rat 20α-hydroxysteroid dehydrogenase (20α-HSD) is an enzyme responsible for the catabolism of progesterone to the inactive 20α-hydroxyprogesterone. We have previously shown that the expression of this enzyme is not regulated by post-translational modification, but at the level of transcription....

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Veröffentlicht in:Biochemical and biophysical research communications 1998-08, Vol.249 (3), p.797-803
Hauptverfasser: Zhong, L., Ou, J., Barkai, U., Mao, J.F., Frasor, J., Gibori, G.
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Sprache:eng
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Zusammenfassung:The rat 20α-hydroxysteroid dehydrogenase (20α-HSD) is an enzyme responsible for the catabolism of progesterone to the inactive 20α-hydroxyprogesterone. 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 20α-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 2.5kb-20α-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 20α-HSD and demonstrated that the regulatory elements for 20α-HSD are present within a 2.5 kb 5′ flanking region of the gene.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.9229