The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells

Abstract The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal membranes by causing matrix degradation. The aim of this study was to assess the mediating role of PGs on lipopolysaccharide (LPS)-induced MMP9 secretion in vitro. ELISA, zymography, and Western blotting were performed on cells and medium from cultures of purified chorion trophoblasts (CTs) and syncytiotrophoblasts (STs) from the human placenta and fetal membranes treated with LPS, meloxicam, (a selective prostaglandin-endoperoxide synthase 2 [PTGS2, previously known as cyclooxygenase 2] inhibitor), or replacement PGE2 or PGF2alpha. LPS significantly (P < 0.01) increased proMMP9 secretion and prostaglandin E2 (PGE2) output by cultured CTs and STs, but there was no effect on tissue inhibitor of matrix m...