Article (Scientific journals)
Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3.
Colige, Alain; Vandenberghe, Isabel; Thiry, Marc et al.
2002In Journal of Biological Chemistry, 277 (8), p. 5756-66
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Keywords :
5' Untranslated Regions/genetics; ADAM Proteins; Amino Acid Sequence; Animals; Catalytic Domain; Collagen/ultrastructure; Collagen Type II/genetics; DNA Primers; DNA, Complementary; Ehlers-Danlos Syndrome/genetics; Humans; Metalloendopeptidases/deficiency/genetics; Mice; Mice, Knockout; Molecular Sequence Data; Peptide Fragments; Polymerase Chain Reaction; Procollagen N-Endopeptidase/deficiency/genetics; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Skin/enzymology; Substrate Specificity; Tendons/enzymology
Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Colige, Alain ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Laboratoire des tissus conjonctifs
Vandenberghe, Isabel;  University of Ghent > Laboratory of Protein Biochemistry and Protein Engineering
Thiry, Marc  ;  Université de Liège - ULiège > Département des sciences de la vie > Biologie cellulaire
Lambert, Charles ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Laboratoire des tissus conjonctifs
Van Beeumen, Jozef;  University of Ghent > Laboratory of Protein Biochemistry and Protein Engineering
Li, Shi-Wu;  Tulane University, Louisiana, USA > Health Sciences Center > Center for Gene Therapy
Prockop, Darwin J;  University of Tulane, Louisiana, USA > Health Sciences Center > Center for Gene Therapy
Lapiere, Charles M
Nusgens, Betty ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Laboratoire de Biologie des Tissus Conjonctifs
Language :
English
Title :
Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3.
Publication date :
2002
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, Baltimore, United States - Maryland
Volume :
277
Issue :
8
Pages :
5756-66
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 07 May 2010

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