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The regulation of cell proliferation or cell death by extracellular factors are the most intensely studied subjects in cell biology. Many conceptual problems remain to be clarified concerning the mechanisms that regulate the programmed cell death. In this work, we focus our attention on the possible role of protein kinase C activation during dimethyl sulfoxide (DMSO)-induced cell death. The present results suggest that the frequency of DMSO-dependent apoptosis of RPMI 8402 thymic lymphoma cells is increased by phorbol ester acetate supplementation. Enhancement of apoptosis can be abolished by cotreatment with the bisindolylmaleimide, a specific PKC inhibitor. The association between PMA and DMSO treatment provokes an early activation of an intracellular signaling mechanism that results, via sustained diacylglycerol elevation, in a possible long-term PKC activation.
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