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Título: | Group V phospholipase A2-derived lysophosphatidylcholine mediates cyclooxygenase-2 induction in lipopolysaccharide-stimulated macrophages |
Autor: | Ruipérez, Violeta CSIC ORCID CVN; Casas, Javier CSIC ORCID CVN; Balboa, María A. CSIC ORCID; Balsinde, Jesús CSIC ORCID | Fecha de publicación: | 2007 | Editor: | American Association of Immunologists | Citación: | Journal of Immunology 179(1): 631-638 (2007) | Resumen: | Activation of macrophages and macrophage cell lines by bacterial LPS elicits a delayed phase of PG biosynthesis that appears to be entirely mediated by cyclooxygenase-2 (COX-2). In previous work, we found that a catalytically active group V secreted phospholipase A2 (sPLA2-V) was required for COX-2 induction, but the nature of the sPLA2-V metabolite involved was not defined. In this study, we identify lysophosphatidylcholine (lysoPC) as the sPLA2-V downstream mediator involved in COX-2 induction by LPS-stimulated macrophages. Inhibition of sPLA2-V by RNA interference or by the cell-permeable compound scalaradial blocked LPS-induced COX-2 expression, and this inhibition was overcome by incubating the cells with a nonhydrolyzable lysoPC analog, but not by arachidonic acid or oleic acid. Moreover, inhibition of sPLA2-V by scalaradial also prevented the activation of the transcription factor c-Rel, and such an inhibition was also selectively overcome by the lysoPC analog. Collectively, these results support a model whereby sPLA2-V hydrolysis of phospholipids upon LPS stimulation results in lysoPC generation, which in turn regulates COX-2 expression by a mechanism involving the transcriptional activity of c-Rel. Copyright © 2007 by The American Association of Immunologists, Inc. | URI: | http://hdl.handle.net/10261/71688 | Identificadores: | issn: 0022-1767 e-issn: 1550-6606 |
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