渥曼青霉素对佛波酯诱导的DNA合成和磷脂酰胆碱水解具有相反的作用。

Wortmannin has opposite effects on phorbol ester-induced DNA synthesis and phosphatidylcholine hydrolysis.

作者信息

Kiss Z, Tomono M

机构信息

Hormel Institute, University of Minnesota, Austin 55912, USA.

出版信息

FEBS Lett. 1995 Sep 4;371(2):185-7. doi: 10.1016/0014-5793(95)00902-l.

DOI:10.1016/0014-5793(95)00902-l

PMID:7672124

Abstract

The tumor promoter phorbol 12-myristate 13-acetate (PMA) and hormonal activators of protein kinase C (PKC) commonly stimulate phospholipase D (PLD)-mediated formation of phosphatidic acid from phosphatidylcholine (PtdCho) in fibroblasts and other cell types. On the basis that phosphatidic acid is a mitogen, PLD is often considered to have a major role in the regulation of cell growth by PKC activators. However, we found that in NIH 3T3 fibroblasts wortmannin, an inhibitor of phosphatidylinositol 3-kinase (PI3K), strongly inhibited DNA synthesis induced by 100 nM PMA, while it actually enhanced PMA-stimulated PtdCho hydrolysis. These results indicate that stimulation of PLD activity is either not required or not sufficient for the mitogenic action of PMA.

摘要

肿瘤促进剂佛波醇12 - 肉豆蔻酸酯13 - 乙酸酯（PMA）和蛋白激酶C（PKC）的激素激活剂通常会刺激磷脂酶D（PLD）介导的成纤维细胞和其他细胞类型中磷脂酰胆碱（PtdCho）形成磷脂酸。基于磷脂酸是一种促有丝分裂原，PLD通常被认为在PKC激活剂调节细胞生长中起主要作用。然而，我们发现，在NIH 3T3成纤维细胞中，磷脂酰肌醇3 - 激酶（PI3K）的抑制剂渥曼青霉素强烈抑制100 nM PMA诱导的DNA合成，而实际上它增强了PMA刺激的PtdCho水解。这些结果表明，对于PMA的促有丝分裂作用，刺激PLD活性既不是必需的，也不是充分的。