Progesterone-regulated cyclic modulation of membrane metalloendopeptidase (enkephalinase) in human endometrium

M. L. Casey, J. W. Smith, K. Nagai, L. B. Hersh, P. C. MacDonald

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84 Scopus citations


Membrane metalloendopeptidase (MMEP; EC; enkephalinase) catalyzes the degradation of endothelins, enkephalins, atrial natriuretic factor, substance P, and other small bioactive peptides. We found that MMEP is present in human endometrium, localized primarily in stromal cells of this tissue, and that the specific activity of MMEP (and immunoreactive MMEP protein) in endometrial tissue is correlated in a highly significant positive manner with the concentration of progesterone in plasma. In estrogen-treated, human endometrial stromal cells in monolayer culture, the specific activity of MMEP increases in response to treatment with progestin; and, this increase is accompanied by increases in immunoreactive MMEP protein, newly synthesized MMEP, and MMEP mRNA.

Original languageEnglish
Pages (from-to)23041-23047
Number of pages7
JournalJournal of Biological Chemistry
Issue number34
StatePublished - Dec 5 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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