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J. Biol. Chem., Vol. 279, Issue 34, 35159-35175, August 20, 2004

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ADAMTS7B, the Full-length Product of the ADAMTS7 Gene, Is a Chondroitin Sulfate Proteoglycan Containing a Mucin Domain^*

Robert P. T. Somerville, Jean-Michel Longpré¶, Elizabeth D. Apel||, Renate M. Lewis||, Lauren W. Wang, Joshua R. Sanes||, Richard Leduc¶**, and Suneel S. Apte

From the Department of Biomedical Engineering, Lerner Research Institute, and the Orthopedic Research Center, Cleveland Clinic Foundation, Cleveland, Ohio 44195, the ^¶Department of Pharmacology, Faculty of Medicine, University of Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada, and the ^||Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110

We have characterized ADAMTS7B, the authentic full-length protein product of the ADAMTS7 gene. ADAMTS7B has a domain organization similar to that of ADAMTS12, with a total of eight thrombospondin type 1 repeats in its ancillary domain. Of these, seven are arranged in two distinct clusters that are separated by a mucin domain. Unique to the ADAMTS family, ADAMTS7B is modified by attachment of the glycosaminoglycan chondroitin sulfate within the mucin domain, thus rendering it a proteoglycan. Glycosaminoglycan addition has potentially important implications for ADAMTS7B cellular localization and for substrate recognition. Although not an integral membrane protein, ADAMTS7B is retained near the cell surface of HEK293F cells via interactions involving both the ancillary domain and the prodomain. ADAMTS7B undergoes removal of the prodomain by a multistep furin-dependent mechanism. At least part of the final processing event, i.e. cleavage following Arg²²⁰ (mouse sequence annotation), occurs at the cell surface. ADAMTS7B is an active metalloproteinase as shown by its ability to cleave ₂-macroglobulin, but it does not cleave specific peptide bonds in versican and aggrecan attacked by ADAMTS proteases. Together with ADAMTS12, whose primary structure also predicts a mucin domain, ADAMTS7B constitutes a unique subgroup of the ADAMTS family.

Received for publication, March 2, 2004 , and in revised form, June 4, 2004.

^* This work was supported in part by National Institutes of Health Awards AR49930 (to S. S. A.) and NS19195 (to J. R. S.), a grant from the Northeast Ohio Chapter of the Arthritis Foundation (to S. S. A.), and Canadian Institutes of Health Research Grant MOP-13755 (to R. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY551090.

Both authors contributed equally to this work.

^** Fonds de la Recherche en Santé du Quebec Senior Scholar.

To whom correspondence should be addressed: Dept. of Biomedical Engineering (ND20), Lerner Research Inst., Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Tel.: 216-445-3278; Fax: 216-445-4383; E-mail: aptes{at}bme.ri.ccf.org.

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