Protein kinase C activators reduce the inositol trisphosphate-Induced outward current and the CA2+ -activated outward current in identified neurons of aplysia
✍ Scribed by M. Sawada; M. Ichinose; T. Maeno
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 770 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
Effects of intracellularly injected activators of protein kinase C on the InsP3-induced K+ current and the Ca2+-activated K+ current recorded from identified neurons (R9-Rl2) of Aplysiu kurodai were investigated with conventional voltage-clamp and pressureinjection techniques. Intracellular injection of InsP3 into identified neurons produced a 4-aminopiridine (4-AP)-resistant, tetraethylammonium (TEA)-sensitive, and quinidine-sensitive K+ current similar to the Ca2+activated K + current elicited by direct injection of Ca2+ ions into the same neurons.
The diacylglycerol analogue 1,2-oleoylacetylglycerol (OAG) at an intracellular concentration of 65 nM produced irreversible decreases in both the InsP, -induced K+ current and the Ca2+-activated K+ current. The phorbol 12,13-dibutyrate (PDBu) at an intracellular concentration of 150 nM also decreased irreversibly both the InsP3 -induced K+ current and the Ca2+-activated K+ current. These results suggest that protein kinase C activators reduce both the InsP3induced K+ current and the Ca2+-activated K+ current recorded from certain identified neurons of Aplysiu and that protein kinase C reduces the ability of Ca2+ to open K+ channels rather than affecting the ability of InsP3 to release Ca2+ from intracellular stores.