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  • Title: Potent activation of phospholipase D by phenylarsine oxide in rat basophilic leukemia (RBL-2H3) cells.
    Author: Kumada T, Nakashima S, Miyata H, Nozawa Y.
    Journal: Biochem Biophys Res Commun; 1994 Mar 15; 199(2):792-8. PubMed ID: 8135825.
    Abstract:
    A putative protein tyrosine phosphatase inhibitor, phenylarsine oxide (PAO), potentiated phospholipase D (PLD) activity concentration-dependently in [3H] oleic acid-labeled rat basophilic leukemia (RBL-2H3) cells without significant increase in phosphatidylinositol-specific phospholipase C (PI-PLC) activity. Although PAO induced tyrosine phosphorylation of several proteins, both PAO-induced PLD activation and tyrosine phosphorylation were not affected by a protein tyrosine kinase inhibitor, genistein. Another tyrosine kinase inhibitor, herbimycin A, prevented the PAO-induced PLD stimulation but had no effect on protein tyrosine phosphorylation. However, depletion of protein kinase C (PKC) greatly reduced PAO-stimulated PLD activity. These results indicate that PKC but not tyrosine kinase may be involved in PAO-mediated PLD activation.
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