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J Biol Chem, Vol. 274, Issue 8, 4489-4492, February 19, 1999
§,
, and
From the Ectopic expression of decorin induces profound
cytostatic effects in transformed cells with diverse histogenetic
backgrounds. The mechanism of action has only recently begun to be
elucidated. Exogenous decorin activates the epidermal growth factor
(EGF) receptor, thereby triggering a signaling cascade that leads to phosphorylation of mitogen-activated protein (MAP) kinase, induction of
p21, and growth suppression. In this study we demonstrate a direct
interaction of decorin with the EGF receptor. Binding of decorin
induces dimerization of the EGF receptor and rapid and sustained
phosphorylation of MAP kinase in squamous carcinoma cells. In a
cell-free system, decorin induces autophosphorylation of purified EGF
receptor by activating the receptor tyrosine kinase and can also
act as a substrate for the EGF receptor kinase itself. Using
radioligand binding assays we show that both immobilized and soluble
decorin bind to the EGF receptor ectodomain or to purified EGF
receptor. The binding is mediated by the protein core and has
relatively low affinity (Kd ~87 nM).
Thus, decorin should be considered as a novel biological ligand for the
EGF receptor, an interaction that could regulate cell growth during
remodeling and cancer growth.
Department of Pathology, Center for Extracellular Matrix Biology, Institute of
Biosciences and Technology, Texas A&M University,
Houston, Texas 77030
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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