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Vol. 53, Issue 2, 221-227, February 1998
1-Adrenergic
Receptors in Madin-Darby Canine Kidney Cells is Independent
of PKC and -
Activation
Department of Pharmacology, University of California at San Diego,
La Jolla, California 92093-0636
We have demonstrated previously that protein kinase C
(PKC) plays a key role in regulating phospholipase D
(PLD) activation by nucleotides and the phorbol ester
phorbol-12-myristate-13-acetate in Madin-Darby canine kidney (MDCK-D1)
cells. In the current work, we investigated PLD activation in MDCK-D1
cells triggered by the adrenergic receptor agonist epinephrine and its
mechanism of activation. Epinephrine, acting through the
1-adrenergic receptor subtype, promoted transient
translocation of PKC and more prolonged translocation of
PKC
to the membrane fraction, indicating activation of
these two isoforms. In addition, epinephrine promoted activation of
PLD, as shown by a sustained accumulation of phosphatidylethanol. All
of these events were blocked by pretreatment of cells with the
1-adrenergic antagonist prazosin. D609, an inhibitor of
phosphatidylcholine hydrolysis, blocked translocation of
PKC and PKC but did not inhibit PLD
activation. Unlike results with PMA, or with the P2
purinergic receptor agonist ATP, epinephrine-stimulated PLD activity
was not inhibited in MDCK-D1 cells in which PKC expression is attenuated by an antisense cDNA construct or in cells in
which PKC activity was inhibited by 1 µM GF 109203X. However, PLD activation by epinephrine was abolished by concomitant incubation of cells with the calcium chelator EGTA. These data, together with previous results, are consistent with the hypothesis that
in MDCK-D1 cells, epinephrine acting on 1-adrenergic
receptors, promotes a rapid increase in cytosolic Ca2+ that
promotes activation of PLD through an as-yet poorly defined mechanism.
The data demonstrate that different types of G protein-linked receptors
that activate PLD can mediate this activation in either a PKC
activation-dependent or -independent manner within a single cell type.
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