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The Journal of Neuroscience, July 1, 1999, 19(13):5293-5300
Involvement of cGMP-Dependent Protein Kinase in Adrenergic
Potentiation of Transmitter Release from the Calyx-Type Presynaptic
Terminal
Hiromu
Yawo
Department of Neurophysiology, Tohoku University School of
Medicine, Sendai 980-8575, Japan
I have previously reported that norepinephrine (NE) induces a
sustained potentiation of transmitter release in the chick ciliary ganglion through a mechanism pharmacologically distinct from any known
adrenergic receptors. Here I report that the adrenergic potentiation of
transmitter release was enhanced by a phosphodiesterase inhibitor,
3-isobutyl-1-methylxanthine (IBMX) and by zaprinast, an inhibitor of
cGMP-selective phosphodiesterase. Exogenous application of the
membrane-permeable cGMP, 8-bromo-cGMP (8Br-cGMP), potentiated the
quantal transmitter release, and after potentiation, the addition of NE
was no longer effective. On the other hand, 8Br-cAMP neither potentiated the transmitter release nor occluded the NE-induced potentiation. The NE-induced potentiation was blocked by neither nitric
oxide (NO) synthase inhibitor nor NO scavenger. The quantal transmitter
release was not potentiated by NO donors, e.g., sodium nitroprusside.
The NE-induced potentiation and its enhancement by IBMX was antagonized
by two inhibitors of protein kinase G (PKG), Rp isomer of
8-(4-chlorophenylthio) guanosine-3',5'-cyclic monophosphorothioate and KT5823. As with NE-induced
potentiation, the effects of 8Br-cGMP on both the resting intraterminal
[Ca2+]
([Ca2+]i) and the action
potential-dependent increment of
[Ca2+]i ( Ca) in the presynaptic
terminal were negligible. The reduction of the paired pulse ratio of
EPSC is consistent with the notion that the NE- and cGMP-dependent
potentiation of transmitter release was attributable mainly to an
increase of the exocytotic fusion probability. These results indicate
that NE binds to a novel adrenergic receptor that activates guanylyl
cyclase and that accumulation of cGMP activates PKG, which may
phosphorylate a target protein involved in the exocytosis of synaptic vesicles.
Key words:
adrenergic receptors; cGMP; protein kinase G; presynaptic
terminal; synaptic plasticity; neurotransmitter release
Copyright © 1999 Society for Neuroscience 0270-6474/99/19135293-08$05.00/0
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