Genistein inhibits potentiation by wortmannin of protein kinase C-activated phospholipase D in osteoblast-like cells

Osamu Kozawa, Atsushi Suzuki, Junji Shinoda, Yutaka Oiso

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

We previously showed that protein kinase C (PKC) induces phosphatidylcholine-hydrolysing phospholipase D activation in osteoblast-like MC3T3-E1 cells and that tyrosine kinase is involved in this activation. Wortmannin, a potent inhibitor of phosphatidylinositol 3-kinase, markedly enhanced the formation of choline induced by 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of PKC in MC3T3-E1 cells. The effect of wortmannin was dose-dependent between 0.1 μM and 10 μM. ML-7, an inhibitor of myosin light chain kinase, had little effect on the TPA-induced formation of choline. Genistein, an inhibitor of protein tyrosine kinases, significantly suppressed the potentiation by wortmannin. These results strongly suggest that phosphatidylinositol 3-kinase is involved in the regulation of phospholipase D activation by PKC in osteoblast-like cells.

Original languageEnglish
Pages (from-to)219-223
Number of pages5
JournalCellular Signalling
Volume7
Issue number3
DOIs
Publication statusPublished - 01-01-1995
Externally publishedYes

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Phospholipase D
Genistein
Osteoblasts
Phosphatidylinositol 3-Kinase
Protein Kinase C
Tetradecanoylphorbol Acetate
Choline
Protein-Tyrosine Kinases
Myosin-Light-Chain Kinase
Phosphatidylcholines
wortmannin

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

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abstract = "We previously showed that protein kinase C (PKC) induces phosphatidylcholine-hydrolysing phospholipase D activation in osteoblast-like MC3T3-E1 cells and that tyrosine kinase is involved in this activation. Wortmannin, a potent inhibitor of phosphatidylinositol 3-kinase, markedly enhanced the formation of choline induced by 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of PKC in MC3T3-E1 cells. The effect of wortmannin was dose-dependent between 0.1 μM and 10 μM. ML-7, an inhibitor of myosin light chain kinase, had little effect on the TPA-induced formation of choline. Genistein, an inhibitor of protein tyrosine kinases, significantly suppressed the potentiation by wortmannin. These results strongly suggest that phosphatidylinositol 3-kinase is involved in the regulation of phospholipase D activation by PKC in osteoblast-like cells.",
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Genistein inhibits potentiation by wortmannin of protein kinase C-activated phospholipase D in osteoblast-like cells. / Kozawa, Osamu; Suzuki, Atsushi; Shinoda, Junji; Oiso, Yutaka.

In: Cellular Signalling, Vol. 7, No. 3, 01.01.1995, p. 219-223.

Research output: Contribution to journalArticle

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T1 - Genistein inhibits potentiation by wortmannin of protein kinase C-activated phospholipase D in osteoblast-like cells

AU - Kozawa, Osamu

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AB - We previously showed that protein kinase C (PKC) induces phosphatidylcholine-hydrolysing phospholipase D activation in osteoblast-like MC3T3-E1 cells and that tyrosine kinase is involved in this activation. Wortmannin, a potent inhibitor of phosphatidylinositol 3-kinase, markedly enhanced the formation of choline induced by 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of PKC in MC3T3-E1 cells. The effect of wortmannin was dose-dependent between 0.1 μM and 10 μM. ML-7, an inhibitor of myosin light chain kinase, had little effect on the TPA-induced formation of choline. Genistein, an inhibitor of protein tyrosine kinases, significantly suppressed the potentiation by wortmannin. These results strongly suggest that phosphatidylinositol 3-kinase is involved in the regulation of phospholipase D activation by PKC in osteoblast-like cells.

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