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Activation of protein kinase C is required for protection of cells against apoptosis induced by singlet oxygen
Author(s) -
Zhuang Shougang,
Lynch Mary C,
Kochevar Irene E
Publication year - 1998
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/s0014-5793(98)01222-8
Subject(s) - protein kinase c , apoptosis , phosphorylation , singlet oxygen , microbiology and biotechnology , reactive oxygen species , phorbol , kinase , signal transduction , chemistry , protein kinase a , biochemistry , biology , oxygen , organic chemistry
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.