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Originally published In Press as doi:10.1074/jbc.M009737200 on January 26, 2001

J. Biol. Chem., Vol. 276, Issue 16, 13372-13378, April 20, 2001
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Versican V1 Proteolysis in Human Aorta in Vivo Occurs at the Glu441-Ala442 Bond, a Site That Is Cleaved by Recombinant ADAMTS-1 and ADAMTS-4*

John D. SandyDagger §, Jennifer WestlingDagger §, Richard D. Kenagy||, M. Luisa Iruela-Arispe**, Christie VerscharenDagger , Juan Carlos Rodriguez-Mazaneque**, Dieter R. ZimmermannDagger Dagger , Joan M. Lemire||, Jens W. Fischer||, Thomas N. Wight||, and Alexander W. Clowes||

From the Dagger  Shriners Hospital for Children, Tampa, Florida 33612, the || Department of Surgery, University of Washington School of Medicine, Seattle, Washington 98195, the ** Department of Molecular, Cell and Developmental Biology, University of California at Los Angeles, Los Angeles, California 90095, and the Dagger Dagger  Molecular Biology Laboratory, Department of Pathology, University of Zurich, 8091 Zurich, Switzerland

Mature human aorta contains a 70-kDa versican fragment, which reacts with a neoepitope antiserum to the C-terminal peptide sequence DPEAAE. This protein therefore appears to represent the G1 domain of versican V1 (G1-DPEAAE441), which has been generated in vivo by proteolytic cleavage at the Glu441-Ala442 bond, within the sequence DPEAAE441-A442RRGQ. Because the equivalent aggrecan product (G1-NITEGE341) and brevican product (G1-EAVESE395) are generated by ADAMTS-mediated cleavage of the respective proteoglycans, we tested the capacity of recombinant ADAMTS-1 and ADAMTS-4 to cleave versican at Glu441-Ala442. Both enzymes cleaved a recombinant versican substrate and native human versican at the Glu441-Ala442 bond and the mature form of ADAMTS-4 was detected by Western analysis of extracts of aortic intima. We conclude that versican V1 proteolysis in vivo can be catalyzed by one or more members of the ADAMTS family of metalloproteinases.

* This work was supported in part by United States Public Health Services Grants HL30946, RR00166, and HL07828, by an award from the American Heart Association (to J. W.), by National Institutes of Health Grant R01CA 77420 (to M. L. I. A.), and by a grant from the Swiss Science Foundation (31-55718.98, to D. Z.).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 this work.

Supported by the Shriners of North America and the Arthritis Foundation. To whom correspondence should be addressed: Shriners Hospital for Children, 12502 North Pine Dr., Tampa, FL 33612-9499. Tel.: 813-972-2250; Fax: 813-975-7127; E-mail: jsandy@shctampa.usf.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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