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  • Title: Activation of protein kinase C-alpha is essential for stimulation of cell proliferation by ceramide 1-phosphate.
    Author: Gangoiti P, Granado MH, Arana L, Ouro A, Gomez-Muñoz A.
    Journal: FEBS Lett; 2010 Feb 05; 584(3):517-24. PubMed ID: 19948174.
    Abstract:
    We previously demonstrated that ceramide-1-phosphate (C1P) stimulates fibroblast and macrophage proliferation, but the mechanisms involved in this action have only been partially described. Here we demonstrate that C1P induces translocation of protein kinase C-alpha (PKC-alpha) from the soluble to the membrane fraction of bone marrow-derived macrophages. Translocation of this enzyme was accompanied by its phosphorylation on Ser 657 residue. Activation of PKC-alpha was independent of prior stimulation of phosphatidylinositol-dependent or phosphatidylcholine-dependent phospholipase C activities, but required activation of sphingomyelin synthesis. Inhibition of PKC-alpha activation also blocked C1P-stimulated macrophage proliferation indicating that this enzyme is essential for the mitogenic effect of C1P.
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