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Departments of Medicine and Physiology, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298
The identity of G
proteins mediating CCK-stimulated phospholipase D (PLD) activity was
determined in intestinal smooth muscle cells. CCK-8 activated
Gq/11, G13, and G12, and the
monomeric G proteins Ras-homology protein (RhoA) and ADP ribosylation
factor (ARF). Activation of RhoA, but not ARF, was mediated by
G13 and inhibited by G
13 antibody.
CCK-stimulated PLD activity was partly mediated by RhoA and could be
inhibited to the same extent (47 ± 2% to 53 ± 6%) by
1) a dominant negative RhoA mutant, 2) RhoA antibody or G13 antibody, and 3)
Clostridium botulinum C3 exoenzyme. PLD activity was also
inhibited by ARF antibody, and the effect was additive to that of RhoA
antibody or C3 exoenzyme. PLD activity was inhibited by calphostin C,
bisindolylmaleimide I, and a selective protein kinase C (PKC)-
inhibitor; the inhibition was additive to that of ARF and RhoA
antibodies and C3 exoenzyme. In contrast, activated G12 was
not coupled to RhoA or ARF, and G12 antibody augmented
PLD activity. Thus agonist-stimulated PLD activity is mediated
additively by G13-dependent RhoA and by ARF and PKC- and
is modulated by an inhibitory G12-dependent pathway.
G12; protein kinase C; phospholipase D; intestinal smooth muscle
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