Send to

Choose Destination
Matrix Biol. 2007 Sep;26(7):508-23. Epub 2007 May 18.

The bone morphogenetic protein 1/Tolloid-like metalloproteinases.

Author information

Program in Molecular and Cellular Pharmacology, University of Wisconsin, Madison, WI 53706, USA.


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 the 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 beta (TGFbeta)-like proteins BMP2, BMP4 (vertebrates) and decapentaplegic (arthropods). More recently, it has become apparent that the BMP1/TLD-like proteinases are activators of a broader subset of the TGFbeta superfamily of proteins, with implications that these proteinases may be key in orchestrating the formation of ECM with growth factor activation and BMP signaling in morphogenetic processes.

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center