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Activation of protein kinase C‐α is essential for stimulation of cell proliferation by ceramide 1‐phosphate
Author(s) -
Gangoiti Patricia,
Granado Maria H.,
Arana Lide,
Ouro Alberto,
Gomez-Muñoz Antonio
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.086
Subject(s) - phospholipase d , protein kinase c , microbiology and biotechnology , cell growth , phosphatidylinositol , ceramide , phosphorylation , kinase , signal transduction , biochemistry , phospholipase c , chemistry , biology , apoptosis
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‐α) 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‐α was independent of prior stimulation of phosphatidylinositol‐dependent or phosphatidylcholine‐dependent phospholipase C activities, but required activation of sphingomyelin synthesis. Inhibition of PKC‐α activation also blocked C1P‐stimulated macrophage proliferation indicating that this enzyme is essential for the mitogenic effect of C1P.