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J Biol Chem, Vol. 275, Issue 10, 7095-7100, March 10, 2000
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From the Perlecan is a multifaceted heparan sulfate
proteoglycan that is expressed not only as an intrinsic constituent of
basement membranes but also as a cell-surface and pericellular
proteoglycan. Perlecan functions as a ligand reservoir for various
growth factors that become stabilized against misfolding or proteolysis
and acts as a co-receptor for basic fibroblast growth factor by
augmenting high affinity binding and receptor activation. These
biological properties are mediated by the heparan sulfate moiety.
Rather little is known about the protein core's mediation of
functions. We have recently discovered that fibroblast growth factor-7
(FGF7) binds to perlecan protein core and that exogenous perlecan
efficiently reconstitutes FGF7 mitogenic activity in perlecan-deficient
cells. In this report we examined the specific binding of FGF7 to
various domains and subdomains of perlecan protein core. Using several experimental approaches including overlay protein assays, radioligand binding experiments, and the yeast two-hybrid system, we demonstrate that FGF7 binds specifically to the N-terminal half of domain III and
to a lesser extent to domain V, with affinity constants in the range of
60 nM. Thus, perlecan protein core should be
considered a novel biological ligand for FGF7, an interaction that
could influence cancer growth and tissue remodeling.
Department of Pathology, Anatomy and Cell
Biology, and Kimmel Cancer Center and the § Department of
Dermatology and Cutaneous Biology, Jefferson Medical College, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107 and the
¶ Commonwealth Scientific and Industrial Research Organization for
Molecular Science, Sydney, New South Wales 2114, Australia
To whom correspondence should be addressed: Dept. of
Pathology, Anatomy and Cell Biology, Rm. 249, JAH, Thomas Jefferson
University, 1020 Locust St., Philadelphia, PA 19107. E-mail:
iozzo@lac.jci.tju.edu.
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