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Oxytocin induced sodium current is mediated by cyclic amp dependent protein phosphorylation in an identified snail neuron

, : Oxytocin induced sodium current is mediated by cyclic amp dependent protein phosphorylation in an identified snail neuron. Nishizuka, Y , M Endo And C Tanaka (Ed ) Advances in Second Messenger And Phosphoprotein Research, Vol 24 The Biology And Medicine Of Signal Transduction; 7th International Conference on Cyclic Nucleotides, Calcium And Protein Phosphorylation, Kobe, Japan, October 8-13, 1989 Xxxiii+750p Raven Press: New York, New York, Usa Illus 672

The intracellular biochemical process underlying oxytocin-induced change of membrane properties was analyzed in an identified neuron of Achatina fulica Ferussac, using pressure injection technique and pharmacological tools. Oxytocin dose-dependently enhanced the negative slope resistance (NSR) region on the current-voltage relation. The oxytocin-induced current was attenuated by a reduction of extracellular Na+ and not influenced by the addition of 100 .mu.M tetrodotoxin (TTX) to the medium, suggesting that this current is predominantly due to the activation of TTX-resistant Na+ channels. In the Ca2+-free state, substituted by an equivalent amount of Co2+, the amplitude of oxytocin-induced current was somewhat reduced at the NSR region but it was not influenced at less than -60 mV. Application of 100 .mu.M isobutylemthylxanthine, a phosphodiesterase inhibitor, augmented the oxytocin-induced current. Pressure injection of 10 mM adenosine 3',5'-cyclic monophosphate (cAMP) elicited a Na+-dependent inward current similar to the oxytocin response. The further role of cAMP linked with the oxytocin-induced current was investigated using two kinds of cAMP-dependent protein kinase inhibitors, isoquinolinesulfonamide (H-8) and protein kinase inhibitor(PKI). Extracellular application of H-8 or pressure injection of PKI, prior to oxytocin application, both blocked the oxytocin-induced current. Based on these results, oxytocin-elicited inward currents may mediate cAMP-dependent protein phosphorylation mainly by activation of Na+ channels.


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