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Vol. 57, Issue 6, 1165-1172, June 2000
Department of Pharmacology, University of Vienna, Vienna, Austria
UTP stimulates transmitter release and inhibits M-type K+
channels in rat superior cervical ganglion neurons via G
protein-coupled P2Y receptors. To investigate the underlying signaling
mechanisms, we treated the neurons with either pertussis or cholera
toxin; neither treatment altered the inhibition of M-type
K+ channels by 10 µM UTP. However, pertussis toxin
reduced UTP-evoked [3H]noradrenaline release by 66%.
UTP, UDP, ATP, and ADP caused accumulation of inositol trisphosphate in
a pertussis toxin-insensitive manner. Pharmacological inhibition of
inositol trisphosphate-induced Ca2+ release (by inhibition
of phospholipase C, of inositol trisphosphate receptors, and of the
endoplasmic Ca2+-ATPase) prevented the UTP-dependent
inhibition of M currents but failed to alter UTP-evoked
[3H]noradrenaline release. Chelation of intracellular
Ca2+ by
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic
acid also reduced the inhibition of M currents by UTP. In addition, all these manipulations attenuated the inhibition of M currents by bradykinin, but hardly affected the inhibitory action of oxotremorine M. These results demonstrate that UTP inhibits M-type K+
channels via an inositol trisphosphate-dependent signaling cascade that
is also used by bradykinin but not by muscarinic acetylcholine receptors. In contrast, the secretagogue action of UTP is largely independent of this signaling cascade but involves pertussis
toxin-sensitive G proteins. Thus, UTP-sensitive P2Y receptors excite
sympathetic neurons via at least two different signal transduction mechanisms.
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