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J. Biol. Chem., Vol. 268, Issue 4, 2280-2283, 02, 1993
K Ozawa, K Yamada, MG Kazanietz, PM Blumberg and MA Beaven
Previous studies indicated that rat basophilic RBL-2H3 cells contained the
Ca(2+)-dependent alpha and beta and the Ca(2+)-independent delta, epsilon,
and zeta isoforms of protein kinase C (PKC); of these, PKC beta and delta
were the most potent transducers of signals for exocytosis in
antigen-stimulated permeabilized cells. Exocytosis, nevertheless, was still
dependent on an elevated free Ca2+. (Ozawa, K., Szallasi, Z., Kazanietz, M.
G., Blumberg, P. M., Mischak, H., Mushinski, J. F., and Beaven, M. A.
(1993) J. Biol. Chem. 268, 1749- 1756). We now demonstrate that PKC alpha
and epsilon, exclusively, inhibit antigen-induced hydrolysis of inositol
phospholipids in the same permeabilized RBL-2H3 cells. Unlike secretion,
the inhibitory actions occurred at a basal concentration (0.1 microM) of
free Ca2+. The inhibitory actions of the two isozymes were potentiated by
20 nM phorbol 12-myristate 13-acetate. As indicated by the effects of the
phorbol ester, the probable mechanism was reduced tyrosine phosphorylation
of phospholipase C gamma 1. The negative regulation of phospholipase C was
apparent in intact cells, because the PKC inhibitor Ro31-7549 or
down-regulation of PKC with phorbol ester enhanced antigen- induced
hydrolysis of inositol phospholipids. The concentrations of the various
isozymes of PKC in RBL-2H3 cells, as estimated by immunoblotting studies,
were sufficient for promotion of exocytosis (i.e. beta and delta) and
inhibition of phospholipid hydrolysis (i.e. alpha and epsilon).
Different isozymes of protein kinase C mediate feedback inhibition of phospholipase C and stimulatory signals for exocytosis in rat RBL-2H3 cells
Laboratory of Chemical Pharmacology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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