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J. Biol. Chem., Vol. 278, Issue 19, 17491-17499, May 9, 2003
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From the The goal of this study was to discover novel
partners for perlecan, a major heparan sulfate proteoglycan of basement
membranes, and to examine new interactions through which perlecan may
influence cell behavior. We employed the yeast two-hybrid system and
used perlecan domain V as bait to screen a human keratinocyte cDNA library. Among the strongest interacting clones, we isolated a ~1.6-kb cDNA insert that encoded extracellular matrix protein 1 (ECM1), a secreted glycoprotein involved in bone formation and angiogenesis. The sequencing of the clone revealed the existence of a
novel splice variant that we name ECM1c. The interaction was validated
by co-immunoprecipitation studies, using both cell-free systems and
mammalian cells, and the specific binding site within each molecule was
identified employing various deletion mutants. The C terminus of ECM1
interacted specifically with the epidermal growth factor-like
modules flanking the LG2 subdomain of perlecan domain V. Perlecan and
ECM1 were also co-expressed by a variety of normal and transformed
cells, and immunohistochemical studies showed a partial expression
overlap, particularly around dermal blood vessels and adnexal
epithelia. ECM1 has been shown to regulate endochondral bone formation,
stimulate the proliferation of endothelial cells, and induce
angiogenesis. Similarly, perlecan plays an important role in
chondrogenesis and skeletal development, as well as harboring pro- and
anti-angiogenic activities. Thus, a physiological interaction could
also occur in vivo during development and in pathological events, including tissue remodeling and tumor progression.
Perlecan Protein Core Interacts with Extracellular Matrix
Protein 1 (ECM1), a Glycoprotein Involved in Bone Formation and
Angiogenesis*
§,§,,,
**
Department of Pathology, Anatomy and Cell
Biology and the Cellular Biology and Signaling Program, Kimmel
Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania
19107 and ¶ PhenoPath Laboratories,
Seattle, Washington 98103
*
This work was supported in part by National Institutes of
Health Grants RO1 CA47282 and RO1 CA39481 (to R. V. I.),
United States Department of the Army Grants DAMD17-00-1-0663 and
DAMD17-00-1-0425 (to R. V. I.), and a fellowship from the
American-Italian Cancer Foundation, New York (to M. M.).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.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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