大鼠泪腺表达蛋白激酶C的α亚型。进一步证明了佛波酯激活且不依赖磷脂的蛋白激酶活性。

The rat lacrimal gland expresses the alpha isoform of PKC. Further evidence for the PMA-activated and phospholipid-independent protein kinase activity.

作者信息

Zoukhri D, Pelosin J M, Mauduit P, Chambaz E, Sergheraert C, Rossignol B

机构信息

Laboratoire de Biochimie des Transports Cellulaires, CNRS URA 1116, Université de Paris Sud, Orsay, France.

出版信息

Cell Signal. 1992 Jan;4(1):111-9. doi: 10.1016/0898-6568(92)90012-w.

DOI:10.1016/0898-6568(92)90012-w

PMID:1571202

Abstract

The molecular heterogeneity of protein kinase C (PKC) is now widely documented. In our first report, we characterized the rat lacrimal gland PKC along with a phorbol 12-myristate 13-acetate (PMA)-activated and phospholipid-independent protein kinase activity [Mauduit P., Zoukhri D. and Rossignol B. (1989) Fedn Eur. biochem. Socs Lett. 252, 5-11. In this work, we show that when the rat lacrimal gland cytosolic fraction is chromatographed on hydroxyapatite, only one peak of PKC activity can be detected. Comparison with a rat brain cytosolic fraction indicated that it is PKC-alpha which is expressed in the rat lacrimal gland. This result was confirmed by the use of polyclonal antibodies raised against rat brain PKC-alpha, beta and gamma isoforms. We also provide evidence that free arachidonic acid activates PKC, as does PMA, in a calcium and phospholipid-free system.

摘要

蛋白激酶C（PKC）的分子异质性现已得到广泛证实。在我们的第一篇报告中，我们对大鼠泪腺PKC以及佛波醇12 - 肉豆蔻酸酯13 - 乙酸酯（PMA）激活的和不依赖磷脂的蛋白激酶活性进行了表征[莫迪伊P.、祖赫里D.和罗西尼奥尔B.（1989年）《欧洲生物化学学会联合会快报》252，5 - 11。在这项工作中，我们表明，当大鼠泪腺胞质部分在羟基磷灰石上进行层析时，只能检测到一个PKC活性峰。与大鼠脑胞质部分的比较表明，在大鼠泪腺中表达的是PKC-α。通过使用针对大鼠脑PKC-α、β和γ亚型产生的多克隆抗体，这一结果得到了证实。我们还提供证据表明，在无钙和无磷脂的体系中，游离花生四烯酸与PMA一样能激活PKC。