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J. Biol. Chem., Vol. 278, Issue 11, 9503-9513, March 14, 2003
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From the Department of Biomedical Engineering, Lerner Research
Institute, and We demonstrate that in humans, two
metalloproteases, ADAMTS-9 (1935 amino acids) and ADAMTS-20
(1911 amino acids) are orthologs of GON-1, an ADAMTS protease required
for gonadal morphogenesis in Caenorhabditis elegans.
ADAMTS-9 and ADAMTS-20 have an identical modular structure, are
distinct in possessing 15 TSRs and a unique C-terminal domain, and have
a similar gene structure, suggesting that they comprise a new subfamily
of human ADAMTS proteases. ADAMTS20 is very sparingly
expressed, although it is detectable in epithelial cells of the breast
and lung. However, ADAMTS9 is highly expressed in embryonic
and adult tissues, and therefore we characterized the ADAMTS-9 protein
further. Although the ADAMTS-9 zymogen has many proprotein convertase
processing sites, pulse-chase analysis, site-directed mutagenesis, and
amino acid sequencing demonstrated that maturation to the active form
occurs by selective proprotein convertase (e.g. furin)
cleavage of the Arg287-Phe288 bond. Although
lacking a transmembrane sequence, ADAMTS-9 is retained near the cell
surface as well as in the ECM of transiently transfected COS-1 and 293 cells. COS-1 cells transfected with ADAMTS9 (but not
vector-transfected cells) proteolytically cleaved bovine versican and
aggrecan core proteins at the Glu441-Ala442
bond of versican V1 and the Glu1771-Ala1772
bond of aggrecan, respectively. In contrast, the ADAMTS-9 catalytic domain alone was neither localized to the cell surface nor able to
confer these proteolytic activities on cells, demonstrating that
the ancillary domains of ADAMTS-9, including the TSRs, are required
both for specific extracellular localization and for its versicanase
and aggrecanase activities.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF488803 (ADAMTS9) and AF488804 (ADAMTS20).
Characterization of ADAMTS-9 and ADAMTS-20 as a Distinct ADAMTS
Subfamily Related to Caenorhabditis elegans GON-1*
,¶, and
**
Orthopedic Research Center, Cleveland Clinic
Foundation, Cleveland, Ohio 44195, § Vascular Biology, The
Hope Heart Institute, Seattle, Washington 98104-2046, and the
Department of Pharmacology, Faculty of Medicine,
Universite de Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada
*
This work was supported in part by a grant from the
Northeast Ohio Chapter of the Arthritis Foundation, a Yamanouchi USA
Foundation Award, and National Institutes of Health (NIH) Grant AR47074
(to S. A.), by NIH Grant HL18645 (to T. W.), and by Canadian
Institutes of Health Research Grant MOP-13755 (to R. L.). Tissue
samples were provided by the Cooperative Human Tissue Network, which is funded by NCI, NIH.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.
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