Activation of protein kinase C is required for protection of cells against apoptosis induced by singlet oxygen.
We evaluated the role of protein kinase C (PKC) in the regulation of apoptosis triggered by singlet oxygen. Activation of PKC by short-term 12-O-tetradecanoyl phorbol 13-acetate (TPA) treatment inhibited apoptosis, whereas inhibition of PKC with several inhibitors potentiated this process. The antiapoptotic effect of TPA was accompanied by phosphorylation of extracelluar signal-regulated kinase 1/2 (ERK1/2). Pretreatment of cells with MEK inhibitor, PD98059, inhibited TPA-induced phosphorylation of ERK1/2 and the cytoprotective ability of TPA. These results suggest that activation of PKC in HL-60 cells confers protection against apoptosis induced by singlet oxygen and that ERK1/2 mediates antiapoptotic signaling of PKC.
Zhuang
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Wellman Laboratories of Photomedicine, Massachusetts General Hospital, Harvard Medical School, Boston 02114, USA.
Lynch
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MC
Kochevar
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IE
D017209:Apoptosis; D053938:DNA Fragmentation; D004789:Enzyme Activation; D018922:HL-60 Cells; D006801:Humans; D010100:Oxygen / Q000494:pharmacology*; D010787:Photosensitivity Disorders; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012395:Rose Bengal / Q000494:pharmacology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D013997:Time Factors
D012395:Rose Bengal; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D010100:Oxygen