Immunohistochemical localization of aromatase cytochrome P-450 and estradiol dehydrogenase in the syncytiotrophoblast of the human placenta

N. Fournet-Dulguerov, N. J. MacLusky, C. Z. Leranth, R. Todd, C. R. Mendelson, E. R. Simpson, F. Naftolin

Research output: Contribution to journalArticlepeer-review

131 Scopus citations

Abstract

Immunohistochemistry employing immunoglobulin G fractions raised against aromatase cytochrome P-450 and antiserum against 17β-estradiol dehydrogenase was used to localize these two steroid-converting enzymes in the human placenta. Immunostaining for both enzymes was found exclusively in the syncytiotrophoblast, while the underlying cytotrophoblast and the villus core did not stain. Ultrastructural examination of aromatase cytochrome P-450- and 17β-estradiol dehydrogenaselabeled sections disclosed immunoreactive product in the membranes of the endoplasmic reticulum; the nucleus, mitochondria, Golgi apparatus, and secretory granules were free of staining. These findings suggest that the syncytiotrophoblast is actively involved in the synthesis and metabolism of estrogens and in their role in placental endocrine function.

Original languageEnglish (US)
Pages (from-to)757-764
Number of pages8
JournalJournal of Clinical Endocrinology and Metabolism
Volume65
Issue number4
DOIs
StatePublished - Oct 1987

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Biochemistry, medical

Fingerprint Dive into the research topics of 'Immunohistochemical localization of aromatase cytochrome P-450 and estradiol dehydrogenase in the syncytiotrophoblast of the human placenta'. Together they form a unique fingerprint.

Cite this