Uchiyama M, Hirai K, Hishinuma F, Akagi H
Department of Anesthesiology, Gunma University School of Medicine, Japan.
Brain Res Mol Brain Res. 1994 Jul;24(1-4):295-300. doi: 10.1016/0169-328x(94)90142-2.
Interaction of protein kinase C (PKC) with glycine receptor channels was examined using Xenopus oocytes expressing homomeric alpha 1 glycine channels. 4 beta-Phorbol 12-myristate 13-acetate (4 beta-PMA), an activator of PKC, reduced the response to glycine; this effect was inhibited in the presence of staurosporine, a PKC inhibitor. By contrast, 4 alpha-PMA, a poor PKC stimulant, did not affect the glycine currents. Thus, the PKC system is involved in negative-regulation of the glycine receptor channels. The results obtained from experiments with mutant receptors suggest that phosphorylation of the intracellular serine residue at 419 may relate to modification of the channel function.
利用表达同聚α1甘氨酸通道的非洲爪蟾卵母细胞，研究了蛋白激酶C（PKC）与甘氨酸受体通道的相互作用。PKC激活剂4β-佛波醇12-肉豆蔻酸酯13-乙酸酯（4β-PMA）降低了对甘氨酸的反应；在PKC抑制剂星形孢菌素存在的情况下，这种效应受到抑制。相比之下，较差的PKC刺激剂4α-PMA对甘氨酸电流没有影响。因此，PKC系统参与甘氨酸受体通道的负调控。对突变受体进行实验得到的结果表明，419位细胞内丝氨酸残基的磷酸化可能与通道功能的改变有关。
