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ADAMTS-2 is an extracellular metalloproteinase responsible for cleaving the N-propeptides of procollagens I-III; an activity necessary for the formation of collagenous ECM (extracellular matrix). The four TIMPs (tissue inhibitors of metalloproteinases) regulate the activities of matrix metalloproteinases, which are involved in degrading ECM components. Here we delineate the abilities of the TIMPs to affect biosynthetic processing of procollagens. TIMP-1, -2 and -4 show no inhibitory activity towards ADAMTS-2, in addition none of the TIMPs showed inhibitory activity towards bone morphogenetic protein 1, which is responsible for cleaving procollagen C-propeptides. In contrast, TIMP-3 is demonstrated to inhibit ADAMTS-2 in vitro with apparent Ki values of 160 and 602 nM, in the presence of heparin or without respectively; and TIMP-3 is shown to inhibit procollagen processing by cells.

Type

Journal article

Journal

The Biochemical journal

Publication Date

09/2006

Volume

398

Pages

515 - 519

Addresses

Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison, WI 53706, USA.

Keywords

Cells, Cultured, Fibroblasts, Animals, Mice, Metalloendopeptidases, Procollagen N-Endopeptidase, Bone Morphogenetic Proteins, Tissue Inhibitor of Metalloproteinases, Tissue Inhibitor of Metalloproteinase-1, Tissue Inhibitor of Metalloproteinase-2, Tissue Inhibitor of Metalloproteinase-3, Protein Binding, ADAM Proteins, Bone Morphogenetic Protein 1