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| Content Provider | PubMed Central |
|---|---|
| Author | Hopkins, Delana R. Keles, Sunduz Greenspan, Daniel S. |
| Abstract | A decade ago, bone morphogenetic protein 1 (BMP1) was shown to provide the activity necessary for proteolytic removal of the C-propeptides of procollagens I–III: precursors of the major fibrillar collagens. Subsequent studies have shown BMP1 to be the prototype of a small group of extracellular metalloproteinases that play manifold roles in regulating formation of the extracellular matrix (ECM). Soon after initial cloning of BMP1, genetic studies showed the related Drosophila proteinase Tolloid (TLD) to be necessary for formation of the dorsal-ventral axis in early embryogenesis. It is now clear that the BMP1/TLD-like proteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of transforming growth factor β (TGFβ)-like proteins BMP2, BMP4 (vertebrates) and decapentaplegic (arthropods). More recently, it has become apparent that the BMP1/TLD-like proteinases are key activators of a broader subset of the TGFβ superfamily of proteins, with implications that these proteinases may be key in orchestrating formation of ECM with growth factor activation and BMP signaling in morphogenetic processes. |
| Related Links | http://dx.doi.org/10.1016/j.matbio.2007.05.004 |
| Ending Page | 523 |
| Page Count | 16 |
| Starting Page | 508 |
| File Format | |
| ISSN | 0945053X |
| e-ISSN | 15691802 |
| Journal | Matrix biology : journal of the International Society for Matrix Biology |
| Issue Number | 7 |
| Volume Number | 26 |
| Language | English |
| Publisher Date | 2007-09-01 |
| Access Restriction | Open |
| Subject Keyword | Molecular Biology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology |
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