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Vol. 53, Issue 6, 1139-1148, June 1998
Institut für Pharmakologie, Universitätsklinikum Essen,
D-45122 Essen, Germany
We recently reported that activation of the highly efficient
phospholipase C (PLC) stimulatory m3 muscarinic acetylcholine receptor
(mAChR) can induce a long-lasting Gi-mediated heterologous potentiation of PLC stimulation in human embryonic kidney (HEK) 293 cells, which was accompanied by an increased cellular level of the PLC
substrate phosphatidylinositol-4,5-bisphosphate
[PtdIns(4,5)P2]. Here, we examined whether such a
potentiated PLC response is also induced by the rather poorly PLC
stimulatory m2 mAChR and the endogenously expressed purinergic and
lysophosphatidic acid receptors. Pretreatment of m2 mAChR-expressing
HEK 293 cells for 2 min with carbachol, followed by agonist washout and
measurement of PLC activity 
40 min later, caused a long-lasting (up
to ~90 min) heterologous potentiation of receptor- and G
protein-mediated PLC stimulation. A similar heterologous potentiation
of receptor-mediated PLC stimulation was induced by short term
activation of lysophosphatidic acid and purinergic receptors. Either of
the three receptor agonists increased the cellular level of
PtdIns(4,5)P2 by ~50%. The mAChR-induced PLC
potentiation was fully prevented by either pertussis toxin or the
protein kinase C (PKC) inhibitors staurosporine and Gö 6976, which did not affect acute PLC stimulation. On the other hand, the rise
in PtdIns(4,5)P2 was prevented only by combined treatment
of HEK 293 cells with pertussis toxin and PKC inhibitors. In
conclusion, we demonstrated that activation of poorly PLC stimulatory receptors can also induce a long-lasting Gi-mediated
heterologous potentiation of PLC signaling in HEK 293 cells and that
this novel PLC regulatory process is under the control of PKC.
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