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

• Published in: The Journal of biological chemistry 1991-12, Vol.266 (34), p.23041-23047
• Main Authors: LINETTE CASEY, M, SMITH, J. W, NAGAI, K, HERSH, L. B, MACDONALD, P. C
• Format: Article
• Language: English
• Subjects: Adult; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Blotting, Northern; Cell Membrane - enzymology; Cells, Cultured; endometrium; Endometrium - cytology; Endometrium - enzymology; Endometrium - ultrastructure; Enzymes and enzyme inhibitors; Female; Fundamental and applied biological sciences. Psychology; Humans; Hydrolases; Immunoblotting; Kinetics; man; membrane proteins; Menstrual Cycle; metalloendopeptidase; Metalloendopeptidases - genetics; Metalloendopeptidases - metabolism; Organ Specificity; Pregnancy; progesterone; Progesterone - blood; Progesterone - physiology; regulation; RNA, Messenger - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(18)54460-4

Membrane metalloendopeptidase (MMEP; EC 3.4.24.11; 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.