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Wortmannin has opposite effects on phorbol ester‐induced DNA synthesis and phosphatidylcholine hydrolysis
Author(s) -
Kiss Zoltan,
Tomono Masahiro
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00902-l
Subject(s) - phosphatidic acid , wortmannin , phospholipase d , protein kinase c , phosphatidylinositol , dna synthesis , phorbol , chemistry , phospholipase c , phosphatidylcholine , biochemistry , kinase , microbiology and biotechnology , signal transduction , biology , phospholipid , dna , membrane
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 (P13K), 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.