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Endocrinology, Vol 133, 1915-1917, Copyright © 1993 by Endocrine Society
ARTICLES |
DA Freeman, PM Gocze and Z Porpaczy
Department of Internal Medicine, University of Oklahoma Health Sciences Center, Oklahoma City 73104.
The 5 alpha-reductase inhibitor, finasteride, inhibits progesterone synthesis in the MA-10 Leydig tumor cells. Inhibition is dose-dependent with half maximal inhibition occurring at 10 ng/ml, a concentration significantly less than serum concentrations detected in finasteride- treated patients. Experiments to localize the site of inhibition by this compound revealed that the 3 beta-hydroxysteroid dehydrogenase delta 5-->delta 4 isomerase enzyme was not blocked by finasteride, but that cholesterol side-chain cleavage was inhibited. Thus, both dibutyryl-cAMP-stimulated and 22-hydroxycholesterol-stimulated steroidogenesis were inhibited by finasteride. This effect of finasteride to block cholesterol side-chain cleavage may be species- specific. Inhibition is readily detected in the mouse-derived MA-10 cells; however, human granulosa cell steroidogenesis is finasteride- insensitive while rat Leydig cell steroidogenesis is only minimally effected by finasteride.
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F. F. G. Rommerts, S. R. King, and P. N. Span Implications of Progesterone Metabolism in MA-10 Cells for Accurate Measurement of the Rate of Steroidogenesis Endocrinology, December 1, 2001; 142(12): 5236 - 5242. [Abstract] [Full Text] [PDF] |
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