Olivier A R, Parker P J
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
J Cell Physiol. 1992 Aug;152(2):240-4. doi: 10.1002/jcp.1041520204.
The expression of members of the Ca2+ and phospholipid-dependent protein kinase (PKC) family were studied in murine Swiss 3T3 cells. In addition to PKC-alpha, the presence of immunoreactive PKC-delta, -epsilon, and zeta was detected. Treatment with 500 nM 12-0-tetradecanoylphorbol-13-acetate (TPA) led to the down-regulation of alpha, delta, and epsilon isoforms, but not that of zeta. Higher concentrations of TPA similarly had no effect on the level of PKC-zeta. In contrast to PKC-alpha, the membrane localization of PKC-delta, -epsilon, and -zeta was not enhanced by extraction in Ca(2+)-containing buffers, whereas acute TPA treatment increased membrane association of PKC-alpha, -delta, and -epsilon but not that of PKC-zeta.
在小鼠瑞士3T3细胞中研究了Ca2+和磷脂依赖性蛋白激酶（PKC）家族成员的表达。除了PKC-α外，还检测到了免疫反应性PKC-δ、-ε和-ζ的存在。用500 nM 12-0-十四酰佛波醇-13-乙酸酯（TPA）处理导致α、δ和ε亚型的下调，但ζ亚型未下调。更高浓度的TPA同样对PKC-ζ水平没有影响。与PKC-α相反，在含Ca(2+)的缓冲液中提取并没有增强PKC-δ、-ε和-ζ的膜定位，而急性TPA处理增加了PKC-α、-δ和-ε的膜结合，但没有增加PKC-ζ的膜结合。
