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TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2.
- Source :
-
The Biochemical journal [Biochem J] 2006 Sep 15; Vol. 398 (3), pp. 515-9. - Publication Year :
- 2006
-
Abstract
- 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.
- Subjects :
- ADAMTS Proteins
ADAMTS4 Protein
Animals
Bone Morphogenetic Protein 1
Bone Morphogenetic Proteins metabolism
Cells, Cultured
Fibroblasts metabolism
Metalloendopeptidases metabolism
Mice
Protein Binding
Tissue Inhibitor of Metalloproteinase-1 genetics
Tissue Inhibitor of Metalloproteinase-1 metabolism
Tissue Inhibitor of Metalloproteinase-2 genetics
Tissue Inhibitor of Metalloproteinase-2 metabolism
Tissue Inhibitor of Metalloproteinase-3 genetics
Tissue Inhibitor of Metalloproteinases genetics
Tissue Inhibitor of Metalloproteinases metabolism
Tissue Inhibitor of Metalloproteinase-4
ADAM Proteins antagonists & inhibitors
Procollagen N-Endopeptidase antagonists & inhibitors
Tissue Inhibitor of Metalloproteinase-3 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1470-8728
- Volume :
- 398
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 16771712
- Full Text :
- https://doi.org/10.1042/BJ20060630