Regulation by follicle-stimulating hormone of the synthesis of aromatase cytochrome p-450 in human granulosa cells

M. P. Steinkampf, C. R. Mendelson, E. R. Simpson

Research output: Contribution to journalArticle

112 Scopus citations

Abstract

The effects of FSH to increase the activity of aromatase, as well as the synthesis of the components of the aromatase enzyme complex, have been studied in human ovarian granulosa cells obtained from women undergoing oocyte retrieval. FSH increased aromatase activity, as well as the synthesis of aromatase cytochrome P-450 (P-450AROM) in a time-dependent fashion, whereas in the absence of FSH, both activity and synthesis declined with duration of culture. The effect of FSH was mimicked by forsko-lin, an activator of adenylate cyclase. FSH also increased the synthesis of NADPH-cytochrome P-450 reductase, but to a relatively modest extent. The levels of hybridizable mRNA species encoding cytochrome P-450AROM of lengths 3.0, 2.4, and 1.6 kil-obases were also increased with FSH treatment. It is concluded that the regulation of aromatase activity by FSH in human granulosa cells is mediated primarily by changes in the synthesis of cytochrome P-450AROM that this action of FSH is mediated by cAMP, and that the changes in cytochrome P-450AROM synthesis are the consequences of changes in the levels of mRNA encoding this enzyme. (Molecular Endocrinology 1: 465-471, 1987).

Original languageEnglish (US)
Pages (from-to)465-471
Number of pages7
JournalMolecular Endocrinology
Volume1
Issue number7
DOIs
StatePublished - Jul 1987

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology

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