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J. Biol. Chem., Vol. 265, Issue 19, 11035-11043, Jul, 1990

Progesterone-binding site of adult male rat liver microsomes

M Yamada, K Indo, T Nishigami, K Nakasho and H Miyaji
Department of Pathology, Hyogo College of Medicine, Japan.

We investigated in greater detail the relationship between steroid structures and their binding affinities to the microsomal progesterone- binding site of the adult male rat liver. Only six steroids of the 100 compounds tested, namely, progesterone, 3 alpha-hydroxy-5 alpha-pregnan- 20-one, 3 alpha,11 beta-dihydroxy-5 alpha-pregnan-20-one, 5 alpha- pregnane-3,20-dione, pregnenolone, and pregnenolone-3-sulfate, had high binding affinities to this site. Thus, we were able to draw a conclusion on the steroid structure which should be required for the best interaction with this site. That is, regardless of the whole molecule's lipophilicity, such a steroid should possess not only a planar A-B ring configuration but also the same side chains as progesterone with C-17 beta-acetyl and non-hydroxyl groups. The exception to this are hydrophilic C-3 groups, which may somewhat increase binding affinities in some cases. We compared the steroid specificity of this binding site with those of various other progesterone-binding components. As a result, this site appears to be a novel type of progesterone binder. We, furthermore, examined the relationship between this microsomal progesterone-binding site and the microsomal progesterone-metabolizing activity. The results, although preliminary, suggest that this binding site does not participate universally in the progesterone-metabolizing processes.
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