Nishizaki T, Ikeuchi Y
Department of Physiology, Kobe University School of Medicine, Japan.
FEBS Lett. 1996 Jan 2;378(1):1-6. doi: 10.1016/0014-5793(95)01399-7.
Adenosine evoked whole-cell potassium currents and enhanced intracellular free Ca2+ concentration ([Ca2+]i) in superior colliculus neurons through a P2Y purinoceptor linked to a pertussis toxin-insensitive G-protein, possibly Gq-protein, which is involved in a protein kinase C (PKC) activation pathway. The [Ca2+]i increase was inhibited by a phospholipase C (PLC) inhibitor, whereas the evoked currents were not affected by a PLC inhibitor or a phospholipase A2 (PLA2) inhibitor. Adenosine elicited single channel currents via PKC activation in cell-attached patches and furthermore, those currents with conductances of the same slope were induced even in excised patches, suggesting that PKC can be activated only by cell membrane factors without intracellular components. These results thus indicate that the P2Y purinoceptor-coupled potassium channel is regulated via a novel PKC activation pathway independent of PLC or PLA2.
腺苷通过与百日咳毒素不敏感的G蛋白(可能是Gq蛋白)偶联的P2Y嘌呤受体,在中脑上丘神经元中诱发全细胞钾电流并提高细胞内游离钙离子浓度([Ca2+]i),该G蛋白参与蛋白激酶C(PKC)激活途径。[Ca2+]i的增加受到磷脂酶C(PLC)抑制剂的抑制,而诱发电流不受PLC抑制剂或磷脂酶A2(PLA2)抑制剂的影响。腺苷通过PKC激活在细胞贴附片膜中引发单通道电流,此外,即使在切除的膜片中也能诱导出具有相同斜率电导的电流,这表明PKC仅能被细胞膜因子激活,而无需细胞内成分。因此,这些结果表明,P2Y嘌呤受体偶联的钾通道是通过一条独立于PLC或PLA2的新型PKC激活途径进行调节的。