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Originally published In Press as doi:10.1074/jbc.M105601200 on December 7, 2001

J. Biol. Chem., Vol. 277, Issue 8, 5756-5766, February 22, 2002
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Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3*

Alain ColigeDagger §, Isabel Vandenberghe, Marc Thiry||**, Charles A. LambertDagger , Jozef Van Beeumen, Shi-Wu LiDagger Dagger , Darwin J. ProckopDagger Dagger , Charles M. LapièreDagger , and Betty V. NusgensDagger §§

From the Dagger  Laboratory of Connective Tissues Biology, Experimental Cancerology Research Center, Tour de Pathologie (B23/3), University of Liège, B-4000 Liège, Belgium, the  Laboratory of Protein Biochemistry and Protein Engineering, University of Gent, K. L. Ledeganckstraat 35, 9000 Gent, Belgium, the || Laboratoire de Biologie cellulaire et tissulaire, University of Liège, 4020 Liège, Belgium, and the Dagger Dagger  Center for Gene Therapy, Tulane University Health Sciences Center, New Orleans, Louisiana 70112

The processing of amino- and carboxyl-propeptides of fibrillar collagens is required to generate collagen monomers that correctly assemble into fibrils. Mutations in the ADAMTS2 gene, the aminopropeptidase of procollagen I and II, result in the accumulation of non-fully processed type I procollagen, causing human Ehlers-Danlos syndrome type VIIC and animal dermatosparaxis. In this study, we show that the aminopropeptide of type I procollagen can be cleaved in vivo in absence of ADAMTS-2 activity and that this processing is performed at the cleavage site for ADAMTS-2. In an attempt to identify the enzyme responsible for this alternative aminoprocollagen peptidase activity, we have cloned the cDNA and determined the primary structure of human and mouse ADAMTS-14, a novel ADAMTS displaying striking homologies with ADAMTS-2 and -3. The structure of the human gene, which maps to 10q21.3, and the mechanisms of generation of the various transcripts are described. The existence of two sites of initiation of transcription, in two different promoter contexts, suggests that transcripts resulting from these two sites can be differently regulated. The tissue distribution of ADAMTS-14, the regulation of the gene expression by various cytokines and the activity of the recombinant enzyme are evaluated. The potential function of ADAMTS-14 as a physiological aminoprocollagen peptidase in vivo is discussed.

* 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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF366351.

§ Research associate of the Belgian Fonds National de la Recherche Scientifique and supported by Belgian National Fonds National de la Recherche Scientifique Grant 1.5.131.01 and the Fonds Special pour la Recherche Grant 1165003.

** Research associate of the Belgian Fonds National de la Recherche Scientifique.

§§ To whom correspondence should be addressed: Laboratory of Connective Tissues Biology, Tour de Pathologie (B23/3), University of Liège, B-4000 Liège, Belgium. Tel.: 32-4-3662456; Fax: 32-4-3662457; E-mail: LCTB@ulg.ac.be.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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