Immunocytochemical distribution and localization of 15-hydroxyprostaglandin dehydrogenase in human fetal membranes, decidua, and placenta.

Biochemical studies have shown the presence of type I oxidized nicotinamide-adenine dinucleotide-dependent 15-hydroxyprostaglandin dehydrogenase in human fetal membranes, decidua, and placenta. However, the localization of prostaglandin dehydrogenase within these tissues is not known. Because the distribution of prostaglandin dehydrogenase may affect the concentration of prostaglandins that reach the myometrium, we used immunocytochemistry to localize immunoreactive prostaglandin dehydrogenase in fetal membranes and placenta. We also examined whether this distribution changed with labor. Tissues were collected at term elective cesarean section or after term spontaneous labor and delivery, were fixed, embeded, and sectioned at 5 microns. Immunoreactive prostaglandin dehydrogenase was determined with a polyclonal primary antibody to human placental prostaglandin dehydrogenase and visualized with the avidin-biotin procedure. Epithelial and epithelium-derived cells were identified by positive staining with a polyclonal antikeratin primary antibody. Cytokeratin staining was observed in amniotic epithelium, trophoblast layer of chorion, invading trophoblast in decidua, and all subsets of trophoblast in the placenta. Immunoreactive prostaglandin dehydrogenase was localized to the trophoblast layer of chorion, invading trophoblast in decidua, and in syncytiotrophoblast and intermediate trophoblast but not cytotrophoblast in the placenta. In chorion, approximately 50% to 60% of the nonvacuolated trophoblast cells stained positively for prostaglandin dehydrogenase. There was no change in the localization of immunoreactive prostaglandin dehydrogenase in any tissue in association with labor.