Mauduit P, Zoukhri D, Rossignol B
Laboratoire de Biochimie des Transports Cellulaires, Biochimie, CNRS UA 1116, Université de Paris Sud, Orsay, France.
FEBS Lett. 1989 Jul 31;252(1-2):5-11. doi: 10.1016/0014-5793(89)80880-4.
The analysis of the cytosolic fraction from rat exorbital lacrimal gland with DEAE-cellulose ion-exchange chromatography showed the presence of a peak of protein kinase activity which was dependent on the presence of phosphatidylserine and diolein as well as calcium. This activity showed the same properties as the previously reported protein kinase C (PKC). Moreover, we have shown for the first time that this kinase or a kinase that coeluted from the column with PKC could be activated by a phorbol ester, PMA, in a phospholipid-free system, i.e. in the absence of any cofactor of PKC. These findings emphasize the need for caution in the interpretation of experimental results obtained when using phorbol esters to probe for a role of PKC in many regulatory processes.
用DEAE - 纤维素离子交换色谱法分析大鼠眶外泪腺的胞质部分，结果显示存在一个蛋白激酶活性峰，该活性依赖于磷脂酰丝氨酸、二油精以及钙的存在。这种活性表现出与先前报道的蛋白激酶C（PKC）相同的特性。此外，我们首次表明，这种激酶或与PKC从柱上共洗脱的一种激酶，在无磷脂系统中，即在没有任何PKC辅助因子的情况下，可被佛波酯PMA激活。这些发现强调了在解释使用佛波酯探究PKC在许多调节过程中的作用时所获得的实验结果时需要谨慎。
