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(Received for publication, March 22, 1996)
From the The epidermal growth factor (EGF) family hormones
amphiregulin (AR), transforming growth factor-
Volume 271, Number 33,
Issue of August 16, 1996
pp. 20047-20052
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
, Heparin-binding Epidermal Growth Factor-like Factor, and
Amphiregulin to Neu, ErbB-3, and ErbB-4
,
,
,
Department of Pathology, Yale University
School of Medicine, New Haven, Connecticut 06520-8023, ¶ Department of Surgical Research, Children's Hospital and
Harvard Medical School, Boston, Massachusetts 02115-5746, '' Bristol-Myers-Squibb Pharmaceutical Research Institute,
Seattle, Washington 98121, and Sugen, Inc.,
Redwood City, California 94063-4720
(TGF-), and
heparin-binding EGF-like growth factor (HB-EGF) are thought to play
significant roles in the genesis or progression of a number of human
malignancies. However, the ability of these ligands to activate all
four erbB family receptors has not been evaluated. Therefore, we have
assessed the stimulation of erbB family receptor tyrosine
phosphorylation by these hormones in a panel of mouse Ba/F3 cell lines
expressing the four erbB family receptors, singly and in pairwise
combinations. We also measured the stimulation of
interleukin-3-independent survival or proliferation in this panel of
Ba/F3 cell lines to compare the patterns of erbB family receptor
coupling to physiologic responses induced by these peptides. EGF,
TGF-, AR, and HB-EGF all stimulated qualitatively similar patterns
of erbB family receptor tyrosine phosphorylation and coupling to
physiologic responses. Therefore, EGF, TGF-, AR, and HB-EGF are
functionally identical in this model system and behave differently from
the EGF family hormones betacellulin and neuregulins.
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