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• W2016204049 abstract "Phorbol esters can induce activation of two mitogen-activated protein kinase (MAPK) pathways, the extracellular signal-regulated kinase (ERK) pathway and the c-Jun N-terminal kinase (JNK) pathway. Unlike ERK activation, JNK activation by phorbol esters is somehow cell-specific. However, the mechanism(s) that contribute to the cell-specific JNK activation remain elusive. In this study, we found that phorbol 12-myristate 13-acetate (PMA) induced JNK activation only in non-small cell lung cancer (NSCLC) cells, but not in small cell lung cancer (SCLC) cells, whereas ERK activation was detected in both cell types. In NSCLC cells, PMA induced JNK activation in a time- and dose-dependent manner. JNK activation was attenuated by protein kinase C (PKC) down-regulation through prolonged pre-treatment with PMA and significantly inhibited by PKC inhibitors Gö6976 and GF109203X. Subcellular localization studies demonstrated that PMA induced translocation of PKC-α, -βII, and -ε isoforms, but not PKC-δ, from the cytosol to the membrane. Analysis of various PKC isoforms revealed that PKC-ε was exclusively absent in the SCLC cell lines tested. Ectopic expression of PKC-ε in SCLC cells restored PMA activation of JNK signaling only in the presence of PKC-α, suggesting that PKC-α and PKC-ε act cooperatively in regulating JNK activation in response to PMA. Furthermore, using dominant negative mutants and pharmacological inhibitors, we define that a putative Rac1/Cdc42/PKC-α pathway is convergent with the PKC-ε/MEK1/2 pathway in terms of the activation of JNK by PMA." @default.
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• W2016204049 date "2004-04-01" @default.
• W2016204049 modified "2023-09-29" @default.
• W2016204049 title "Cooperation between PKC-α and PKC-ε in the regulation of JNK activation in human lung cancer cells" @default.
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• W2016204049 doi "https://doi.org/10.1016/j.cellsig.2003.09.002" @default.
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