Opposite Effect of Phorbol Ester PMA on PTGS2 and PGDH mRNA Expression in Human Chorion Trophoblast Cells
@article{Casciani2008OppositeEO, title={Opposite Effect of Phorbol Ester PMA on PTGS2 and PGDH mRNA Expression in Human Chorion Trophoblast Cells}, author={Valentina Casciani and Emanuela Marinoni and Alan D. Bocking and Massimo Moscarini and Romolo di Iorio and John R. G. Challis}, journal={Reproductive Sciences}, year={2008}, volume={15}, pages={40 - 50} }
Prostaglandins (PGs) induce the mechanism of labor in humans. The enzymes responsible for PG synthesis and metabolism are prostaglandin-endoperoxide synthase 2 (PTGS2) and 15-hydroxyprostaglandin dehydrogenase (PGDH). In human chorion trophoblast cells, calcium ionophore A23187 upregulates PTGS2 and downregulates PGDH protein and mRNA. The authors hypothesize that this regulation requires activation of protein kinase C (PKC) and mitogen-activated protein kinases (MAPKs). Human chorion…
10 Citations
Effect of calcium ionophore A23187 on prostaglandin synthase type 2 and 15-hydroxy-prostaglandin dehydrogenase expression in human chorion trophoblast cells.
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References
SHOWING 1-10 OF 52 REFERENCES
Regulation of prostaglandin H2 synthase-2 expression in primary human amnion cells by tyrosine kinase dependent mechanisms.
- BiologyBiochimica et biophysica acta
- 1998
Stimulation of synthesis de novo of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase in human promyelocytic leukaemia (HL-60) cells by phorbol ester.
- Biology, Computer ScienceThe Biochemical journal
- 1991
The rapid turnover of 15-PGDH indicates that the enzyme activity depends on continued enzyme synthesis, and this could be susceptible to hormone and drug control mechanisms.
Comparative study of vanadate- and phorbol ester-induced cyclo-oxygenase-2 expression in human endothelial cells.
- Biology, ChemistryThrombosis and haemostasis
- 1999
Our previous study showed that vanadate, an inhibitor of protein tyrosine phosphatases, induced the expression of cyclo-oxygenase (COX)-2 in a protein-tyrosine-kinase (PTK)-dependent manner in human…
Regulation of prostaglandin E2 synthesis in human amnion by protein kinase C.
- Biology, ChemistryProstaglandins
- 1990
MAPK regulation of prostaglandin E2 production by lipopolysaccharide-stimulated macrophages is not dependent on nuclear factor kappaB.
- Biology, MedicineThe Journal of surgical research
- 2003
Dexamethasone inhibits the induction of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase by phorbol ester in human promonocytic U937 cells.
- Biology, MedicineBiochimica et biophysica acta
- 2000
Reciprocal regulation of cyclooxygenase-2 and 15-hydroxyprostaglandin dehydrogenase expression in A549 human lung adenocarcinoma cells.
- BiologyCarcinogenesis
- 2006
The contention that COX-2 and 15-PGDH are regulated reciprocally in A549 cells is supported, as the levels of IL-1beta-induced COx-2 expression appeared to correlate inversely with those of 15- PGDH expression in the cells.
Gene expression of arachidonate cyclooxygenase pathway leading to the delayed synthesis of prostaglandins E2 and F2alpha in response to phorbol 12-myristate 13-acetate and action of these prostanoids during life cycle of adipocytes.
- BiologyBiochimica et biophysica acta
- 2006
Regulation of Cyclooxygenases by Protein Kinase C
- BiologyThe Journal of Biological Chemistry
- 1996
Despite regulated expression of COX-2 by PMA and the existence of consensus sequences for PKC phosphorylation, it appears that it is an unfavorable substrate for this enzyme.