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Figure 6


Fig. 6. Expression of the full-length HRSL3 protein (HREVFL) was controlled by incubation with the HRSL3-specific antibody (H-REV107-1). HRSL3 regulates PKC{zeta}, which is required for HRSL3-induced apoptosis. (A) Phosphorylation of the indicated signaling proteins was analyzed by immunoblotting using antibodies specific for their phosphorylated forms. Immunoblotting against total amount of the proteins was used as a loading control. Expression of the HRSL3 protein, full-length and truncated form, was controlled by incubation with the HRSL3-specific antibody. (B) OVCAR-3 cells were either treated with 1, 10 and 20 nM of OA and with an inhibitor of the PI 3-kinase (LY294002; LY), or transfected with HRSL3. To determine the concentration of OA that inhibits PP2A activity only partially, phosphorylation of MEK1/2 and ERK1/2 kinases was examined using the corresponding antibodies (left panel). Then caspase-9 cleavage was analyzed (right panel). Actin- and caspase-9-specific antibodies were used as loading controls. (C) Phosphorylation of PKC{zeta} is induced by treatment with both OA and HRSL3. Cells were treated with 10 nM OA, with DMSO or transfected with HRSL3 or the empty vector. Phospho-PKC{zeta} or total PKC{zeta} were measured by western blotting using the appropriate antibodies. (D) Twelve hours prior to transfection, OVCAR-3 cells were treated with the myristoylated PKC{zeta}-specific pseudosubstrate. Then the cells were transfected with HRASL3 expression plasmid and caspase cleavage was analyzed 48 hours after transfection.





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