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• W2063641757 startingPage "125" @default.
• W2063641757 abstract "Treatment of human synovial cells with interleukin-1 (IL-1) results in a large increase in the production of prostaglandin E, (PGE2), a function in which the activation of phospholipase A2 (PLA2) is a key step. In order to identify the enzymes that are linked to IL-1-mediated arachidonate availability and subsequent PGE2 production, we have investigated the changes in gene expression of the 85-kDa cytosolic PLA2 (cPLA2), the 14-kDa secretory PLA2 (sPLA2) and the two forms of cyclooxygenase in human synoviocytes after stimulation with recombinant IL-1β. Northern-blot analysis revealed that both cPLA2 and cyclooxygenase-2 mRNA were progressively upregulated upon exposure to IL-1 for 5 hours and the glucocorticoid, dexamethasone, blocked the increased expression of these two genes. In contrast, IL-1-induced sPLA2 gene expression determined in the same cell samples was weak and most often rapid, and dexamethasone further stimulated it. In addition, IL-1 did not modify the levels of the constitutive cyclooxygenase-1. The cPLA2 and cyclooxygenase-2 enzymic activities are dependent upon de novo synthesis of mRNA and protein, since they were inhibited by actinomycin D and cycloheximide. Our data suggest that the IL-1-induced production of PGE2 in human synoviocytes can be attributed to the stimulation of both cPLA2 and cyclooxygenase-2. These enzymes may represent appropriate targets for selective blockade of prostanoid production in the inflammed joints." @default.
• W2063641757 created "2016-06-24" @default.
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• W2063641757 date "2008-06-28" @default.
• W2063641757 modified "2023-10-17" @default.
• W2063641757 title "Interleukin-1-Induced Prostaglandin E2 Biosynthesis in Human Synovial Cells Involves the Activation of Cytosolic Phospholipase A2 and Cyclooxygenase-2" @default.
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• W2063641757 doi "https://doi.org/10.1111/j.1432-1033.1994.0t125.x" @default.
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