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Induction of Surfactant Protein A Expression by Cortisol Facilitates Prostaglandin Synthesis in Human Chorionic Trophoblasts

Department of Obstetrics and Gynecology (K.S., D.B., B.C., B.P., L.M.), University of Cincinnati, College of Medicine, Cincinnati, Ohio 45267; and School of Life Sciences (K.S.), Fudan University, Shanghai 200433, China

Address all correspondence and requests for reprints to: Dr. Kang Sun, Department of Obstetrics and Gynecology, College of Medicine, University of Cincinnati, 231 Albert Sabin Way, Cincinnati, Ohio 45267. E-mail: sunkang2000{at}yahoo.com.

Context: Surfactant protein A (SP-A) may be an important link between the maturation of fetal organs and the initiation of parturition. However, the local expression of SP-A and the effect of SP-A on prostaglandin synthesis in human fetal membranes have not been resolved.

Objective: Our objective was to examine SP-A expression and the effect of SP-A on prostaglandin synthesis in human fetal membranes.

Design: SP-A expression was examined with immunohistochemistry and PCR. The effect of SP-A on prostaglandin synthesis was investigated in cultured human chorionic trophoblasts.

Patients: Patients were normal-term pregnant women undergoing elective cesarean sections.

Results: Both SP-A protein and mRNA were present in amnion epithelial cells, fibroblasts, and chorionic trophoblasts. Cortisol (10^–7 and 10^–6 M, 24 h) induced SP-A expression in cultured chorionic trophoblasts, which could be blocked by the glucocorticoid receptor antagonist RU486. Treatment of chorionic trophoblasts with SP-A (10–100 µg/ml, 24 h) caused a dose-dependent increase of prostaglandin E₂ release and an induction of cyclooxygenase type 2 but not cytosolic phospholipase A₂ and microsomal prostaglandin E synthase expression.

Conclusions: SP-A can be synthesized locally in human fetal membranes, which can be induced by glucocorticoids. SP-A appeared to induce prostaglandin E₂ synthesis in chorionic trophoblasts via induction of cyclooxygenase type 2 expression.

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