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J. Biol. Chem., Vol. 279, Issue 11, 10042-10051, March 12, 2004
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From the
Center For Research in Skeletal Development and Paediatric Orthopaedics, Shriners Hospital for Children, Tampa, Florida 33612, the Departments of Internal Medicine and ||Pharmacology and Therapeutics, University of South Florida, Tampa, Florida 33620, and ¶Arthritis Department, Roche Biosciences, Palo Alto, California 94304
C-terminal truncation of ADAMTS-4 from the p68 form to the p53 form is required for activation of its capacity to cleave the Glu373-Ala374 interglobular domain bond of aggrecan. In transfected human chondrosarcoma cells, this process is not autoproteolytic because the same products form with an inactive mutant of ADAMTS4 (a disintegrin and metalloproteinase with thrombospondin-like motif 4) and truncation is completely blocked by tissue inhibitor of metalloproteinase-1. Instead, activation can be mediated by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase (MT4-MMP, MMP-17) because co-transfection with the active form of MT4-MMP markedly enhanced activation, whereas an inactive mutant of MT4-MMP was ineffective. Treatment of co-transfected cells with phosphatidylinositol-specific phospholipase C liberated the complex of MT4-MMP and p68 ADAMTS4 from the cell membrane, but the p53 ADAMTS4 remained associated. Specific glycosaminoglycan lyase digestions, followed by product analyses using fluorescence-assisted carbohydrate electrophoresis and immunoprecipitation experiments, showed that the p53 form is associated with syndecan-1 through both chondroitin sulfate and heparan sulfate. We conclude that ADAMTS-4 activation in this cell system involves the coordinated activity of both glycosylphosphatidyl inositol-anchored MT4-MMP and the proteoglycan form of syndecan-1 on the cell surface.
Received for publication, November 4, 2003 , and in revised form, December 19, 2003.
* This work was supported by grants from the Shriners of North America and the Florida Chapter of the Arthritis Foundation (to J. D. S.), The Orthopaedic Research and Education Foundation (to G. G.), and by a grant from the National Office of The Arthritis Foundation (to A. P.). 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.
** To whom correspondence should be addressed: Shriners Hospital for Children, 12502 N. Pine Dr., Tampa, FL 33612-9499. Tel.: 813-972-2250; Fax: 813-975-7127; E-mail: jsandy{at}shctampa.usf.edu.
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