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Papers In Press, published online ahead of print June 21, 2004
Biomedical Engineering, ND20, Cleveland Clinic Foundation, Cleveland, OH 44195
Corresponding Author: aptes{at}bme.ri.ccf.org
We have characterized ADAMTS7B, the authentic full-length protein product of the ADAMTS7 gene. ADAMTS7B has a domain organization similar to ADAMTS12, with a total of eight thrombospondin type 1 repeats (TSRs) in its ancillary domain. Of these, seven TSRs 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 pro-domain. ADAMTS7B undergoes removal of the pro-domain by a multi-step, furin-dependent mechanism. At least some 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 a2-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.
J. Biol. Chem, 10.1074/jbc.M402380200
Submitted on March 2, 2004
Revised on June 21, 2004
Accepted on June 10, 2004
ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulphate-proteoglycan containing a mucin domain
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