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• W2017262170 abstract "Cytosolic phospholipase A2 (cPLA2) is an enzyme involved in the formation of proinflammatory mediators by catalyzing the release of arachidonic acid, thereby mediating eicosanoid biosynthesis. Using HaCaT keratinocytes as a model system, we present experimental evidence that in these cells, cPLA2 is constitutively phosphorylated and that the degree of phosphorylation dramatically increases in cells under hyperosmotic stress induced by sorbitol. In parallel, a rapid release of arachidonic acid followed by prostaglandin E2 formation was detected. Elucidating the mechanism of cPLA2 upregulation, we observed that it is mediated via epidermal growth factor receptor (EGFR) activation, since tyrphostin AG1478, a selective inhibitor of EGFR tyrosine kinase, completely inhibited cPLA2 phosphorylation. Furthermore, addition of PD98059, which is an inhibitor of MEK1 activation, but not of SB203580, which is an inhibitor of p38 stress kinase, inhibited cPLA2 phosphorylation, indicating that the ras–raf–MEK cascade is the major signalling pathway involved in cPLA2 phosphorylation. In addition, depletion of the cells from intracellular calcium does not prevent sorbitol-elicited cPLA2 phosphorylation, suggesting that this process is independent of the presence of calcium. Together, our results demonstrate that hyperosmotic stress phosphorylates cPLA2 in human keratinocytes by an EGFR-mediated process." @default.
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• W2017262170 date "2002-10-01" @default.
• W2017262170 modified "2023-09-23" @default.
• W2017262170 title "Hyperosmotic stress induces phosphorylation of cytosolic phospholipase A2 in HaCaT cells by an epidermal growth factor receptor-mediated process" @default.
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• W2017262170 doi "https://doi.org/10.1016/s0898-6568(02)00031-1" @default.
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