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J Biol Chem, Vol. 273, Issue 37, 24115-24121, September 11, 1998

Evidence That Protein Kinase C Mediates Phorbol Ester Inhibition of Calphostin C- and Tumor Necrosis Factor--induced Apoptosis in U937 Histiocytic Lymphoma Cells

From the School of Biological Sciences, Faculty of Science and Engineering, Flinders University of South Australia, Adelaide, South Australia 5001, Australia

Protein kinase C (PKC) activators, such as the tumor-promoting phorbol esters, have been reported to protect several cell lines from apoptosis induced by a variety of agents. Recent evidence suggests that PKC is involved in protection of cardiac myocytes from hypoxia-induced cell death (Gray, M. O., Karliner, J. S., and Mochly-Rosen, D. (1997) J. Biol. Chem. 272, 30945-30951). We investigated the protective effects of the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) on U937 histiocytic lymphoma cells induced to undergo apoptosis by tumor necrosis factor- (TNF-) or by the specific PKC inhibitor calphostin C. U937 cells were transiently permeabilized with a peptide (V1-2) derived from the V1 region of PKC that has been reported to specifically block translocation of PKC. The V1-2 peptide blocked the inhibitory effect of TPA on both TNF-- and calphostin C-induced apoptosis. A scrambled version of V1-2 and a peptide reported to inhibit PKC translocation (C2-4) had no effect on the ability of TPA to inhibit apoptosis. These results suggest that PKC is required for the protective effect of TPA in TNF-- and calphostin C-induced apoptosis. Furthermore, calphostin C reduced membrane-associated PKC activity and immunoreactivity, suggesting that PKC may play an important role in leukemic cell survival.

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