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J Biol Chem, Vol. 274, Issue 39, 27689-27693, September 24, 1999

Regulation of Cyclooxygenase-2 Expression by Phosphatidate Phosphohydrolase in Human Amnionic WISH Cells

Christina A. Johnson, María A. Balboa, Jesús Balsinde, and Edward A. Dennis

From the Department of Chemistry and Biochemistry, Revelle College and School of Medicine, University of California at San Diego, La Jolla, California 92093-0601

Prostaglandins are known to play a key role in the initiation of labor in humans, but the mechanisms governing their synthesis in amnion are largely unknown. In this study, we have examined the regulatory pathways for prostaglandin E2 (PGE2) production during protein kinase C-dependent activation of human WISH cells. In these cells, PGE2 synthesis appears to be limited not by free arachidonic acid availability but by the expression levels of cyclooxygenase-2 (COX-2). Concomitant with the cells being able to synthesize and secrete PGE2, we detected significant elevations of both COX-2 protein and mRNA levels. Specific inhibition of COX-2 by NS-398 totally ablated PGE2 synthesis. All of these responses were found to be strikingly dependent on an active phosphatidate phosphohydrolase 1 (PAP-1). Inhibition of PAP-1 activity by three different strategies (i.e. use of bromoenol lactone, propranolol, and ethanol) resulted in inhibition of COX-2 expression and hence of PGE2 production. These data unveil a novel signaling mechanism for the regulation of PGE2 production via regulation of COX-2 expression and implicate phosphatidate phosphohydrolase 1 as a key regulatory component of eicosanoid metabolic pathways in the amnion.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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