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Originally published In Press as doi:10.1074/jbc.M210529200 on February 25, 2003

J. Biol. Chem., Vol. 278, Issue 19, 17491-17499, May 9, 2003
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Perlecan Protein Core Interacts with Extracellular Matrix Protein 1 (ECM1), a Glycoprotein Involved in Bone Formation and Angiogenesis*

Maurizio MongiatDagger §, Jian FuDagger §, Rachel OldershawDagger , Robert GreenhalghDagger , Allen M. Gown, and Renato V. IozzoDagger ||**

From the Dagger  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

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.

* 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.

§ Both authors contributed equally to the results of this work.

** 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 © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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