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J. Biol. Chem., Vol. 279, Issue 2, 980-986, January 9, 2004

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Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1^*

Barry M. Steiglitz, Melvin Ayala, Karthikeyan Narayanan¶, Anne George¶, and Daniel S. Greenspan||

From the Departments of Biomolecular Chemistry and Pathology and Laboratory Medicine, University of Wisconsin, Madison, Wisconsin 53706 and the ^¶Department of Oral Biology, University of Illinois, Chicago, Illinois 60612

Bone morphogenetic protein-1 (BMP-1)/Tolloid-like metalloproteinases play key roles in formation of mammalian extracellular matrix (ECM), through the biosynthetic conversion of precursor proteins into their mature functional forms. These proteinases probably play a further role in formation of bone through activation of transforming growth factor -like BMPs. Dentin matrix protein-1 (DMP1), deposited into the ECM during assembly and involved in initiating mineralization of bones and teeth, is thought to undergo proteolysis in vivo to generate functional cleavage fragments found in extracts of mineralized tissues. Here, we have generated recombinant DMP1 and demonstrate that it is cleaved, to varying extents, by all four mammalian BMP-1/Tolloid-like proteinases, to generate fragments similar in size to those previously isolated from bone. Consistent with possible roles for the BMP-1/Tolloid-like proteinases in the physiological processing of DMP1, NH₂-terminal sequences of products generated by BMP-1 cleavage of DMP1 match those predicted from processing at the predicted DMP1 site that shows greatest cross-species conservation of sequences. Moreover, fibroblasts derived from mouse embryos homozygous null for genes encoding three of the four mammalian BMP-1/Tolloid-like proteinases appear to be deficient in processing of DMP1. Thus, a further role for BMP-1-Tolloid-like proteinases in formation of mineralized tissues is indicated, via proteolytic processing of DMP1.

Received for publication, September 12, 2003 , and in revised form, October 15, 2003.

^* This work was supported by National Institutes of Health (NIH) Grants AR47746 and GM63471 (to D. S. G.) and by NIH Predoctoral Training Grant T32 GM07215 in Molecular Biosciences (to B. M. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, University of Wisconsin, 1300 University Ave., Madison, WI 53706. Tel.: 608-262-4676; Fax: 608-262-6691; E-mail: dsgreens{at}wisc.edu.

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