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Interleukin-1-beta induces cytosolic phospholipase A-2 and prostaglandin H synthase in rheumatoid synovial fibroblasts



Interleukin-1-beta induces cytosolic phospholipase A-2 and prostaglandin H synthase in rheumatoid synovial fibroblasts



Arthritis & Rheumatism 37(5): 653-661



Objective. In order to investigate potential regulatory mechanisms for the increased production of prostaglandin E-2 (PGE-2) in interleukin-1B (IL-1-beta)stimulated rheumatoid synovial fibroblasts (RSF), this study examined the induction of phospholipase A-2. (PLA-2) and prostaglandin H synthase (PGHS) enzymes and the correlation of these events with PGE-2 production in IL-1-beta-stimulated RSF. Methods. Protein and messenger RNA (mRNA) levels of cytosolic PLA-2 (cPLA-2) and PGHS-2 enzymes in IL-1-beta-stimulated RSF were measured by Western and Northern blotting, respectively, using specific antisera and complementary DNA probes. Enzymatic activity of cPLA-2 was determined in cell-free reaction mixtures utilizing mixed micelles of 14C-phosphatidylcholine and Triton X-100 as the substrate. PGE-2 levels were quantitated using a commercial enzyme immunoassay kit. Results. Incubation of RSF with IL-1-beta increased the mRNA and protein levels for the high molecular weight cPLA-2 as well as for the mitogen/growth factor-responsive PGHS (PGHS-2). The IL-1 receptor antagonist completely abolished the induction of these two enzymes and the stimulation of PGE-2 production by IL-1-beta in RSF. In contrast, levels of the other known forms of these enzymes, i.e., the 14-kd secretory group II PLA-2 (sPLA-2) and the constitutive form of PGHS (PGHS-1), were unaffected by IL-1-beta treatment. Conclusion. These are the first data to demonstrate the coordinate induction by IL-1 of cPLA-2 and PGHS-2 in RSF. The time-course for the induction of these enzymes suggests that their increase contributes to the increased production of PGE-2, in IL-1-treated RSF, and may help explain the capacity of RSF to produce large amounts of PGE-2.

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