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J. Biol. Chem., Vol. 268, Issue 16, 11946-11950, Jun, 1993
C Godson, KS Bell and PA Insel
A major unresolved issue in the area of signal transduction relates to the
role of particular isoforms of protein kinase C (PKC) in mediating cellular
responses subsequent to activation of that enzyme. We have addressed this
issue by the use of antisense technology. We have stably transfected
Madin-Darby canine kidney cells with antisense PKC alpha, PKC beta, or both
PKC alpha and -beta cDNAs. The transfected cDNA was integrated and
expressed. We have isolated cells in which expression of PKC alpha is
inhibited. In cells transfected with antisense PKC alpha or both PKC alpha
and -beta, phorbol ester-stimulated release of arachidonate and its
metabolites was inhibited, whereas in cells transfected with antisense PKC
beta cDNA alone, phorbol ester- stimulated arachidonate release was not
significantly different from control cells. We thus demonstrate the use of
a novel technique to inhibit PKC isoform expression. We show that
inhibition of expression of PKC alpha causes a loss in phospholipase
A2-mediated arachidonate release. Antisense-inhibited expression of PKC
isoforms may provide a useful approach to define additional functions of
particular PKC isoforms.
Inhibition of expression of protein kinase C alpha by antisense cDNA inhibits phorbol ester-mediated arachidonate release
Department of Pharmacology, University of California, San Diego, La Jolla 92093.
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