Protein kinase C-mediated inhibition of an inward rectifier potassium channel by substance P in nucleus basalis neurons

In nucleus basalis neurons, substance P (SP) causes a slow excitation, mediated through a pertussis toxininsensitive G protein, by suppressing an inward rectifier K + channel. Here we report that SP applied outside the patch pipette inhibited the single-channel activity, recorded on-cell, of the inw...

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 1995-05, Vol.14 (5), p.999-1008
Main Authors: Takano, Koji, Stanfield, Peter R, Nakajima, Shigehiro, Nakajima, Yasuko
Format: Article
Language:English
Subjects:
Alkaloids - pharmacology
Animals
Cells, Cultured
Ethers, Cyclic - pharmacology
Neurons - physiology
Okadaic Acid
Phosphoprotein Phosphatases - antagonists & inhibitors
Phosphoprotein Phosphatases - metabolism
Phosphorylation
Potassium Channel Blockers
Potassium Channels - physiology
Protein Kinase C - antagonists & inhibitors
Protein Kinase C - metabolism
Rats
Signal Transduction
Staurosporine
Substance P - pharmacology
Substantia Innominata - physiology
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Summary:In nucleus basalis neurons, substance P (SP) causes a slow excitation, mediated through a pertussis toxininsensitive G protein, by suppressing an inward rectifier K + channel. Here we report that SP applied outside the patch pipette inhibited the single-channel activity, recorded on-cell, of the inward rectifier. The PKC inhibitors staurosporine and PKC(19–36) suppressed this effect in whole-cell mode and in on-cell single-channel mode. A diacylglycerol analog mimicked the SP effect, and PKC(19–36) suppressed this analog effect. SP irreversibly suppressed the inward rectifier in neurons treated with okadaic acid. These results indicate that a diffusible messenger mediates the SP effect, that its signal transduction involves phosphorylation by PKC, and that dephosphorylation by a serine/threonine protein phosphatase mediates its recovery.
ISSN:0896-6273
1097-4199
DOI:10.1016/0896-6273(95)90338-0