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Prostaglandin E2 synthesis in human monocyte-derived dendritic cells
Johannes Norgauer1, Yvonne Ibig, Doris Gmeiner
1Department of Experimental Dermatology, University of Freiburg, D-79104 Freiburg, Germany. norgauer@haut.ukl.uni-freiburg.de
International Journal of Molecular Medicine
|June 7, 2003
Summary
Lipopolysaccharide (LPS) triggers cyclooxygenase-2 (COX-2) expression and prostaglandin E2 (PGE2) release in dendritic cells. The p38 stress-activated protein kinase pathway is crucial for this LPS-induced COX-2 regulation and PGE2 synthesis.
Area of Science:
- Immunology
- Cell Biology
Background:
- Prostaglandin E2 (PGE2) is vital for dendritic cell (DC) maturation.
- The regulation of cyclooxygenase-1 and -2 (COX-1/2) in human DCs is not fully understood.
Purpose of the Study:
- To investigate the expression and activity of COX-1/2 in human monocyte-derived DCs.
- To elucidate the signaling pathways regulating COX-1/2 and PGE2 production during DC maturation.
Main Methods:
- Differentiated human monocyte-derived DCs were stimulated with lipopolysaccharide (LPS) in the presence of 1% human plasma.
- COX-1/2 mRNA and protein expression, PGE2 release, and p38 stress-activated protein kinase (p38) activation were measured.
- The effect of p38 inhibitors on LPS-induced COX-2 expression and activity was assessed.
Main Results:
- LPS stimulation induced COX-2 mRNA and protein synthesis in DCs.
- LPS triggered the release of PGE2 from DCs.
- LPS activated p38 in DCs, and p38 inhibition blocked LPS-induced COX-2 expression and PGE2 production.
Conclusions:
- Lipopolysaccharide (LPS) induces COX-2 expression and PGE2 synthesis in human dendritic cells.
- The p38 stress-activated protein kinase pathway plays a critical role in regulating LPS-induced COX-2 expression and PGE2 production during DC maturation.