The glyceryl ester of prostaglandin E2 mobilizes calcium and activates signal transduction in RAW264.7 cells.

Nirodi CS, Crews BC, Kozak KR, Morrow JD, Marnett LJ
Proc Natl Acad Sci U S A. 2004 101 (7): 1840-5

PMID: 14766978 · PMCID: PMC357014 · DOI:10.1073/pnas.0303950101

Glyceryl prostaglandins (PG-Gs) are generated by the oxygenation of the endocannabinoid, 2-arachidonylglycerol, by cyclooxygenase 2. The biological consequences of this selective oxygenation are uncertain because the cellular activities of PG-Gs have yet to be defined. We report that the glyceryl ester of PGE(2), PGE(2)-G, triggers rapid, concentration-dependent Ca(2+) accumulation in a murine macrophage-like cell line, RAW264.7. Ca(2+) mobilization is not observed after addition of PGE(2), PGD(2)-G, or PGF(2alpha)-G but is observed after addition of PGF(2alpha). Moreover, PGE(2)-G, but not PGE(2), stimulates a rapid but transient increase in the levels of inositol 1,4,5-trisphosphate (IP(3)) as well as the membrane association and activation of PKC. PGE(2)-G induces a concentration-dependent increase in the levels of phosphorylated extracellular signal regulated kinases 1 and 2 through a pathway that requires the activities of PKC, IP(3) receptor, and phospholipase C beta. The results indicate that PGE(2)-G triggers Ca(2+) mobilization, IP(3) synthesis, and activation of PKC in RAW264.7 macrophage cells at low concentrations. These responses are independent of the hydrolysis of PGE(2)-G to PGE(2).

MeSH Terms (16)

Animals Calcium Calcium Signaling Cell Line Dinoprostone Enzyme Activation Gene Expression Regulation Genes, Reporter Inositol 1,4,5-Trisphosphate Macrophages Mice Mitogen-Activated Protein Kinases Phosphorylation Protein Kinase C Receptors, Prostaglandin Signal Transduction

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