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J. Biol. Chem., Vol. 276, Issue 13, 10263-10271, March 30, 2001
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From the Perlecan, a widespread heparan sulfate
proteoglycan, functions as a bioactive reservoir for growth factors by
stabilizing them against misfolding or proteolysis. These factors,
chiefly members of the fibroblast growth factor (FGF) gene family, are coupled to the N-terminal heparan sulfate chains, which augment high
affinity binding and receptor activation. However, rather little is
known about biological partners of the protein core. The major goal of
this study was to identify novel proteins that interact with the
protein core of perlecan. Using the yeast two-hybrid system and domain
III of perlecan as bait, we screened ~0.5 106
cDNA clones from a keratinocyte library and identified a
strongly interactive clone. This cDNA corresponded to
FGF-binding protein (FGF-BP), a secreted protein previously shown to
bind acidic and basic FGF and to modulate their activities. Using a
panel of deletion mutants, FGF-BP binding was localized to the second
EGF repeat of domain III, a region very close to the binding site for
FGF7. FGF-BP could be coimmunoprecipitated with an antibody against perlecan and bound in solution to recombinant domain III-alkaline phosphatase fusion protein. Immunohistochemical analyses revealed colocalization of FGF-BP and perlecan in the pericellular stroma of
various squamous cell carcinomas suggesting a potential in vivo interaction. Thus, FGF-BP should be considered a novel
biological ligand for perlecan, an interaction that could influence
cancer growth and tissue remodeling.
Fibroblast Growth Factor-binding Protein Is a Novel Partner for
Perlecan Protein Core*
§¶,¶,,,
, and**
Department of Pathology, Anatomy and Cell
Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, the Division of Cell, Molecular and Developmental Biology,
American Type Culture Collection, Manassas, Virginia 20110, and the
** Cellular Biology and Signaling Program, Kimmel Cancer Center, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107
*
This work was supported by National Institutes of Health
Grants RO1 CA39481 and RO1 CA47282 (to R. V. I).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pathology,
Anatomy and Cell Biology, Rm. 249, Jefferson Alumni Hall, Thomas Jefferson University, 1020 Locust St., Philadelphia, PA 19107. E-mail: iozzo@lac.jci.tju.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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