Reference : Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloprotei...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/11082
Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V
English
Colige, Alain mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. >]
Ruggiero, Florence [IFR128 BioSciences - Lyon, France > UMR CNRS 5086 > Institut de Biologie et Chimie des Protéines > >]
Vandenberghe, Isabel [Universiteit Gent - Ugent > > Laboratorium voor Eiwitbiochemie en Eiwitengineering > >]
Dubail, Johanne [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. >]
Kesteloot, Frédéric mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. > >]
Van Beeumen, Jozef [Universiteit Gent - Ugent > > Laboratorium voor Eiwitbiochemie en Eiwitengineering > >]
Beschin, Alain [Vrije Universiteit Brussel - VUB > Department of Cellular and Molecular Interactions, Flanders Interuniversity Institute for Biotechnology > Laboratorium voor Cellulaire en Moleculaire Immunologie > >]
Brys, Lea [Vrije Universiteit Brussel - VUB > Department of Cellular and Molecular Interactions, Flanders Interuniversity Institute for Biotechnology > Laboratorium voor Cellulaire en Moleculaire Immunologie > >]
Lapière, Charles M [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. > >]
Nusgens, Betty mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Département des sciences biomédicales et précliniques >]
14-Oct-2005
Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc
280
41
34397-34408
Yes (verified by ORBi)
International
0021-9258
Bethesda
[en] Processing of fibrillar collagens is required to generate collagen monomers able to self-assemble into elongated and cylindrical collagen fibrils. ADAMTS-2 belongs to the "A disintegrin and metalloproteinase with thrombospondin type 1 motifs" (ADAMTS) family. It is responsible for most of the processing of the aminopropeptide of type I procollagen in the skin, and it also cleaves type II and type III procollagens. ADAMTS are complex secreted enzymes that are implicated in various physiological and pathological processes. Despite accumulating evidence indicating that their activity is regulated by ancillary domains, additional information is required for a better understanding of the specific function of each domain. We have generated 17 different recombinant forms of bovine ADAMTS-2 and characterized their processing, activity, and cleavage specificity. The results indicated the following: (i) activation of the ADAMTS-2 zymogen involves several cleavages, by proprotein convertases and C-terminal processing, and generates at least seven distinct processed forms; (ii) the C-terminal domain negatively regulates enzyme activity, whereas two thrombospondin type 1 repeats are enhancer regulators; (iii) the 104-kDa form displays the highest aminoprocollagen peptidase activity on procollagen type I; (iv) ADAMTS-2 processes the aminopropeptide of alpha1 type V procollagen homotrimer at the end of the variable domain; and (v) the cleaved sequence (PA) is different from the previously described sites ((P/A)Q) for ADAMTS-2, redefining its cleavage specificity. This finding and the existence of multiple processed forms of ADAMTS-2 strongly suggest that ADAMTS-2 may be involved in function(s) other than processing of fibrillar procollagen types I-III.
http://hdl.handle.net/2268/11082
10.1074/jbc.M506458200

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