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Somatostatin-induced inhibition of neuronal Ca2+ current modulated by cGMP-dependent protein kinase

A Correction to this article was published on 27 October 1994

Abstract

NEUROTRANSMITTER release is frequently regulated by peptides that modulate neuronal calcium channels. Whole-cell recordings show that the ion permeability1 and voltage dependence2 of these channels are controlled by a membrane-associated pathway involv-ing GTP-binding proteins. Here we use perforated-patch recordings to show that, in addition to this pathway, the peptide somatostatin inhibits the calcium current in chick ciliary ganglion neurons by a second soluble pathway involving a cyclic GMP-dependent protein kinase (cGMP-PK). This somatostatin inhibi-tion of Ca2+ current did not desensitize and was not characterized by the slowing of Ca2+-current activation (kinetic slowing) observed in whole-cell recordings. When cGMP-PK was inhibited, somatostatin inhibition of Ca2+ current resembled that observed with whole-cell recordings. cGMP agonists mimic the effect of somatostatin only in perforated patch recordings. An endogenous cGMP-PK therefore forms part of the mechanism by which soma-tostatin induces a sustained inhibition of neuronal calcium channels.

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Meriney, S., Gray, D. & Pilar, G. Somatostatin-induced inhibition of neuronal Ca2+ current modulated by cGMP-dependent protein kinase. Nature 369, 336–339 (1994). https://doi.org/10.1038/369336a0

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