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

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 microM and 10 microM. 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.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Kozawa O,Suzuki A,Shinoda J,Oiso Y

doi

10.1016/0898-6568(94)00080-u

subject

Has Abstract

pub_date

1995-03-01 00:00:00

pages

219-23

issue

3

eissn

0898-6568

issn

1873-3913

pii

089865689400080U

journal_volume

7

pub_type

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