Oxidized low density lipoprotein stimulates protein kinase C (PKC) activity and expression of PKC-isotypes via prostaglandin-H-synthase in P388D1 cells.

Treatment of P388D1 macrophage-like cells with oxLDL enhanced protein kinase C (PKC) activity in cell extracts. Similar effects were induced by acetylated LDL (acLDL) and maleylated albumin (malBSA). Treatment with oxLDL, acLDL and malBSA was also accompanied by increased production of prostaglandins as well as by an enhanced level of prostaglandin H synthase 2 (cyclooxygenase 2, COX 2). Modified (lipo)proteins differentially affected the levels of individual cytosolic PKC-isoenzymes. Effects of oxLDL on PKC activity/expression were abrogated by indometacin, by pre-exposure to the dual lipoxygenase/cyclooxygenase inhibitor ML 3000 and by treatment with N-(2-cyclohexyloxy-4-nitrophenyl)methane sulfonamide (NS-398). These results suggest a predominantly COX 2-dependent and isotype-specific effect of modified (lipo)proteins on PKC.