TY - JOUR
T1 - Progesterone-regulated cyclic modulation of membrane metalloendopeptidase (enkephalinase) in human endometrium
AU - Casey, M. L.
AU - Smith, J. W.
AU - Nagai, K.
AU - Hersh, L. B.
AU - MacDonald, P. C.
PY - 1991/12/5
Y1 - 1991/12/5
N2 - 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.
AB - 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.
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M3 - Article
C2 - 1744100
AN - SCOPUS:0026349469
SN - 0021-9258
VL - 266
SP - 23041
EP - 23047
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 34
ER -