Mizukami Y, Hirata T, Yoshida K
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Japan.
FEBS Lett. 1997 Jan 20;401(2-3):247-51. doi: 10.1016/s0014-5793(96)01481-0.
Protein kinase C zeta (PKC zeta), a member of the atypical PKC subgroup, is insensitive to Ca2+, diacylglycerol, and phorbol esters, but is activated by phospholipids such as phosphatidylinositol-3,4,5-triphosphate, a product of phosphatidylinositol 3-kinase (PI3-kinase). Here we show that PKC zeta translocates from the cytosol to the 1000 x g pellet (nuclear-myofibrillar) fraction during ischemia for 40 min in Langendorff-perfused rat hearts. In addition, immunohistochemical observation shows that ischemia induces the translocation of PKC zeta to the nucleus. The nuclear translocation during ischemia is inhibited in a dose-dependent manner by wortmannin (10(-9)-10(-7) M), an inhibitor of PI3-kinase.
蛋白激酶Cζ（PKCζ）是非典型PKC亚组的成员，对Ca2+、二酰基甘油和佛波酯不敏感，但可被磷脂如磷脂酰肌醇-3,4,5-三磷酸（磷脂酰肌醇3激酶（PI3激酶）的产物）激活。在此我们表明，在Langendorff灌注的大鼠心脏缺血40分钟期间，PKCζ从细胞质转位至1000×g沉淀（核-肌原纤维）组分。此外，免疫组织化学观察显示缺血诱导PKCζ转位至细胞核。缺血期间的核转位被PI3激酶抑制剂渥曼青霉素（10^(-9)-10^(-7) M）以剂量依赖性方式抑制。
