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Reactive oxygen intermediates activate NF-kappa B in a tyrosine kinase-
dependent mechanism and in combination with vanadate activate the p56lck
and p59fyn tyrosine kinases in human lymphocytes
GL Schieven, JM Kirihara, DE Myers, JA Ledbetter and FM Uckun
Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, WA 98121.
We have previously observed that ionizing radiation induces tyrosine
phosphorylation in human B-lymphocyte precursors by stimulation of
unidentified tyrosine kinases and this phosphorylation is substantially
augmented by vanadate. Ionizing radiation generates reactive oxygen
intermediates (ROI). Because H2O2 is a potent ROI generator that readily
crosses the plasma membrane, we used H2O2 to examine the effects of ROI on
signal transduction. We now provide evidence that the tyrosine kinase
inhibitor herbimycin A and the free radical scavenger N- acetyl-cysteine
inhibit both radiation-induced and H2O2-induced activation of NF-kappa B,
indicating that activation triggered by ROI is dependent on tyrosine kinase
activity. H2O2 was found to stimulate Ins-1,4,5-P3 production in a tyrosine
kinase-dependent manner and to induce calcium signals that were greatly
augmented by vanadate. The synergistic induction of tyrosine
phosphorylation by H2O2 plus vanadate included physiologically relevant
proteins such as PLC gamma 1. Although treatment of cells with H2O2 alone
did not affect the activity of src family kinases, treatment with H2O2 plus
vanadate led to activation of the p56lck and p59fyn tyrosine kinases. The
combined inhibition of phosphatases and activation of kinases provides a
potent mechanism for the synergistic effects of H2O2 plus vanadate.
Induction of tyrosine phosphorylation by ROI may thus lead to many of the
pleiotropic effects of ROI in lymphoid cells, including downstream
activation of PLC gamma 1 and NF-kappa B.
Volume 82,
Issue 4,
pp. 1212-1220,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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