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(Received for publication, February 21, 1996, and in revised form, August 29, 1996)
From the Stimulation of phospholipase D (PLD)-mediated
hydrolysis of phosphatidylcholine (PtdCho) by phorbol 12-myristate
13-acetate (PMA) has been shown to be mediated by the
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28912-28917
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Is a Major Mediator of the Stimulatory Effect
of Phorbol Ester on Phospholipase D-mediated Hydrolysis of
Phosphatidylethanolamine
,
,
Hormel Institute, University of Minnesota,
Austin, Minnesota 55912 and the ¶ Lilly Research Laboratories,
Lilly Corporate Center, Indianapolis, Indiana 46285
- and
I-isoforms of protein kinase C (PKC). To determine the role of
various PKC isozymes in the regulation of PLD-mediated
phosphatidylethanolamine (PtdEtn) hydrolysis, MCF-7 human breast
carcinoma cells overexpressing the - and 
-isoforms, and R6 rat
fibroblasts overexpressing the -, I-, and 
-isoforms were used.
In the vector control MCF-7 cells, which contain low levels of PKC-,
PMA (100 nM) had only small effects on the hydrolysis of
PtdEtn (1.1-1.35-fold) and PtdCho (1.15-1.6-fold). Stable expression
of PKC- in MCF-7 cells, which was accompanied by increased levels of
the I- and -isoforms as well, greatly enhanced both PMA-induced
PLD-mediated formation of phosphatidylethanol (~5-fold) and the
hydrolysis of PtdEtn (2.5-2.9-fold) and PtdCho (5.5-7.2-fold). The
effects of PMA on the hydrolysis of PtdEtn (and PtdCho) in
MCF-7/PKC- cells were significantly inhibited by 0.5-3
µM concentrations of Gö 6976, a selective inhibitor
of the conventional PKC subfamily. Stable expression of PKC- in R6
fibroblasts enhanced, at a shorter (10 min) incubation time, the
effects of PMA on the hydrolysis of both PtdEtn and, to a lesser
extent, PtdCho. In contrast, stable expression of PKC-I in R6
fibroblasts, which originally did not contain this enzyme, enhanced the
effects of PMA only on PtdCho, but not PtdEtn, hydrolysis.
Overexpression of either PKC- in MCF-7 cells or PKC- in R6 and
NIH 3T3 fibroblasts had no detectable effects on PMA-induced hydrolysis
of PtdEtn. Collectively, the results suggest that PKC- has a major
role in the mediation of phorbol ester action on PtdEtn hydrolysis,
while PtdCho hydrolysis may be regulated by both the and I
isoforms.
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