ACTIVATION OF ENDOGENOUS PROTEIN-KINASE-C ENHANCES CURRENTS THROUGH ALPHA-1 AND ALPHA-2 GLYCINE RECEPTOR CHANNELS

被引:36
作者
NISHIZAKI, T
IKEUCHI, Y
机构
[1] Department of Physiology, Kobe University School of Medicine, Chuo-ku, Kobe, 650
关键词
XENOPUS OOCYTE; GLYCINE RECEPTOR; ALPHA-1; SUBUNIT; ALPHA-2; PROTEIN KINASE C; WHOLE-CELL VOLTAGE;
D O I
10.1016/0006-8993(95)00543-Y
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The effects of Ca2+/phospholipid dependent (PKC) phosphorylation on the current amplitudes of alpha 1 and alpha 2 glycine receptors expressed in Xenopus oocytes were examined by whole cell voltage clamp recording. In studies using phorbol esters, PKC phosphorylation has been shown to reduce glycine-induced currents. Endogenous PKC activation by pretreatment with serum, however, enhanced the currents to around 140% in both alpha 1 and alpha 2 glycine receptors. This effect was completely blocked by a specific PKC inhibitor, GF109203X. Instead, treatment with a potent PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA) revealed a decrease in glycine-gated channel currents. Thus, the present results demonstrate that glycine receptor phosphorylation mediated by endogenous pathway of PKC activation potentiates glycine-induced currents and phorbol esters may have a direct action on glycine receptor channels independent of PKC activation.
引用
收藏
页码:214 / 216
页数:3
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