Abstract
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 Arg(220) (mouse sequence annotation), occurs at the cell surface. ADAMTS7B is an active metalloproteinase as shown by its ability to cleave alpha(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.
Highlights
The extracellular matrix (ECM)1 is an information-rich assembly influencing cell proliferation, apoptosis, and cell migration
Primary Structure of ADAMTS7B—Shortly after the acceptance of our original publication on ADAMTS7 [18], a human cDNA (GenBankTM/EBI accession number AL110226, submitted August 13, 1999) that overlapped with our DNA sequence at its C terminus was deposited by the German Cancer Research Center
The existence of putative ADAMTS7B has been readily apparent by data base analysis since 1999, and its domain organization has been previously noted in the literature [34, 35] and in online resources
Summary
The extracellular matrix (ECM)1 is an information-rich assembly influencing cell proliferation, apoptosis, and cell migration. Purification and analysis of full-length mouse ADAMTS7B were essentially similar, except that the cell layer was first washed with 0.5 M NaCl to release the protein from the cell surface; this was pooled with the medium from these cultures and purified and analyzed as described above. Gly-Ser dipeptides (Fig. 2) are present within the mucin domain, some in appropriate sequence context for GAG attachment [27], but they are not at identical locations in mouse and human ADAMTS7B.
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