<Originals>The cytotoxic effect of adriamycin is not attributable to the inhibition of protein kinase C

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Adriamycin is an antineoplastic drug that appears to exert its biological effects through multiple biochemical mechanisms. We examined possible ability of adriamycin to inhibit protein kinase C activity in BALB/3T3 mouse fibroblasts by measuring the phosphorylation of the myristoylated alanine-rich C kinase substrate and the induction of c-fos transcription following treatment with 200 nM phorbol 12-myristate 13-acetate. At the concentration of 60 μM adriamycin, the phosphorylation of myristoylated alanine-rich C kinase substrate was not inhibited, but the expression of c-fos was completely inhibited. The inhibition of c-fos expression was not specifically mediated via kinase C, since both total RNA synthesis as measured by [^3H]-uridine uptake and the fraction of serum-induced c-fos expression that was not attributable to kinase C activity were inhibited by adriamycin. The present data do not support the hypothesis that the cytotoxic effect of adriamycin is attributable to the inhibition of kinase C in vivo.
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