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J Biol Chem, Vol. 273, Issue 32, 20589-20595, August 7, 1998
From the Departments of Enhancement of tyrosine phosphorylation in cells
by the application of pervanadate, an extremely potent phosphotyrosine
phosphatase inhibitor, provokes the rapid
metalloprotease-dependent cleavage of ErbB-4, a
transmembrane receptor tyrosine kinase. The pervanadate-induced proteolysis occurs in NIH 3T3 cells expressing transfected human ErbB-4
and in several cell lines that express endogenous ErbB-4. One product
of this proteolytic event is a membrane-anchored molecule of
approximately 80 kDa, which is heavily tyrosine phosphorylated and
which possesses tyrosine kinase catalytic activity toward an exogenous
substrate in vitro. This response to pervanadate is not
dependent on protein kinase C activation, which has previously been
demonstrated to also activate ErbB-4 cleavage. Hence, the pervanadate
and 12-O-tetradecanoylphorbol-13-acetate-induced
proteolytic cleavage of ErbB-4 seem to proceed by different mechanisms,
although both require metalloprotease activity. Moreover, pervanadate
activation of ErbB-4 cleavage, but not that of
12-O-tetradecanoylphorbol-13-acetate , is blocked by the
oxygen radical scavenger pyrrolidine dithiocarbomate. A second
phosphotyrosine phosphatase inhibitor, phenylarsine oxide, also
stimulates a similar cleavage of ErbB-4 but, unlike pervanadate, is not
sensitive to pyrrolidine dithiocarbomate. Last, pervanadate is shown to
stimulate the proteolytic cell surface processing of a second and
unrelated transmembrane molecule: the precursor for amphiregulin, an
epidermal growth factor-related molecule. Amphiregulin cleavage by
pervanadate occurred in the absence of a cytoplasmic domain and
tyrosine phosphorylation of this substrate.
Tyrosine Phosphorylation and Proteolysis
PERVANADATE-INDUCED, METALLOPROTEASE-DEPENDENT CLEAVAGE OF THE
ErbB-4 RECEPTOR AND AMPHIREGULIN
,,
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Biochemistry, ¶ Cell
Biology, and Medicine, Vanderbilt University School of Medicine,
Nashville, Tennessee 37232-0146
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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