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(Received for publication, July 25, 1996, and in revised form, October 2, 1996)
From the Recent evidence indicates that reactive oxygen
species (ROS) may function as intracellular messengers in receptor
signaling pathways. The possible role of ROS in epidermal growth factor (EGF) signaling was therefore investigated. Stimulation of A431 human
epidermoid carcinoma cells with EGF resulted in a transient increase in
the intracellular concentration of ROS, measured with the
oxidation-sensitive fluorescent probe 2
Volume 272, Number 1,
Issue of January 3, 1997
pp. 217-221
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
ROLE IN EGF RECEPTOR-MEDIATED TYROSINE PHOSPHORYLATION
,
,
,
,
and
Laboratory of Cell Signaling, the
§ Laboratory of Cell Biology, and the 
Laboratory of
Biochemistry, NHLBI, National Institutes of Health,
Bethesda, Maryland 20892
,7-dichlorofluorescin diacetate and laser-scanning confocal microscopy. The predominant ROS
produced appeared to be H2O2, because the
EGF-induced increase in fluorescence was completely abolished by
incorporation of catalase into the cells by electroporation. The
elimination of H2O2 by catalase also inhibited
the EGF-induced tyrosine phosphorylation of various cellular proteins
including the EGF receptor and phospholipase C-
1. The dependence of
H2O2 production on the intrinsic tyrosine kinase activity of the EGF receptor and the autophosphorylation sites
located in its COOH-terminal tail was investigated. EGF failed to
induce H2O2 generation in cells expressing a
kinase-inactive EGF receptor. However, normal
H2O2 generation was observed in cells
expressing a mutant receptor from which the 126 COOH-terminal amino
acids had been deleted to remove four (out of the total of five)
autophosphorylation sites. These results suggest that EGF-induced
H2O2 formation requires the kinase activity but
probably not the autophosphorylation sites of the EGF receptor and that inhibition of protein tyrosine phosphatase activity by
H2O2 may be required for EGF-induced protein
tyrosine phosphorylation to be manifested.
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