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J Biol Chem, Vol. 275, Issue 11, 7470-7473, March 17, 2000
and the c-Abl Tyrosine
Kinase in the Cellular Response to Oxidative Stress*
From the Dana-Farber Cancer Institute, Harvard Medical School,
Boston, Massachusetts 02115
Protein kinase C (PKC) isoforms are
phosphorylated on tyrosine in the response of cells to oxidative
stress. The present studies demonstrate that treatment of cells with
hydrogen peroxide (H2O2) induces binding
of the PKC
isoform and the c-Abl protein-tyrosine kinase. The
results show that c-Abl phosphorylates PKC in the H2O2 response. We also show that PKC
phosphorylates and activates c-Abl in vitro. In cells,
induction of c-Abl activity by H2O2 is
attenuated by the PKC inhibitor, rottlerin, and by overexpression of
the regulatory domain of PKC. These findings support a functional interaction between PKC and c-Abl in the cellular response to oxidative stress.
To whom correspondence should be addressed. Tel.: 617-632-3141;
Fax: 617-632-2934; E-mail: donald_kufe@dfci.harvard.edu.
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