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Originally published In Press as doi:10.1074/jbc.M004846200 on July 14, 2000

J. Biol. Chem., Vol. 275, Issue 39, 30504-30511, September 29, 2000
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Bone Morphogenetic Protein-1 Processes Probiglycan*

Ian C. ScottDagger , Yasutada ImamuraDagger , William N. Pappano§, James M. Troedel§, Anneliese D. Recklies, Peter J. Roughley||, and Daniel S. GreenspanDagger §**

From the Departments of Dagger  Pathology and Laboratory Medicine and § Biomolecular Chemistry University of Wisconsin, Madison, Wisconsin 53706 and the  Joint Diseases Laboratory and || Genetics Unit, Shriners Hospital for Children, and the Department of Surgery, McGill University, Montreal H3G 1A6, Quebec, Canada

Bone morphogenetic protein-1 (BMP-1) is a metalloprotease that plays important roles in regulating the deposition of fibrous extracellular matrix in vertebrates, including provision of the procollagen C-proteinase activity that processes the major fibrillar collagens I-III. Biglycan, a small leucine-rich proteoglycan, is a nonfibrillar extracellular matrix component with functions that include the positive regulation of bone formation. Biglycan is synthesized as a precursor with an NH2-terminal propeptide that is cleaved to yield the mature form found in vertebrate tissues. Here, we show that BMP-1 cleaves probiglycan at a single site, removing the propeptide and producing a biglycan molecule with an NH2 terminus identical to that of the mature form found in tissues. BMP-1-related proteases mammalian Tolloid and mammalian Tolloid-like 1 (mTLL-1) are shown to have low but detectable levels of probiglycan-cleaving activity. Comparison shows that wild type mouse embryo fibroblasts (MEFs) produce only fully processed biglycan, whereas MEFs derived from embryos homozygous null for the Bmp1 gene, which encodes both BMP-1 and mammalian Tolloid, produce predominantly unprocessed probiglycan, and MEFs homozygous null for both the Bmp1 gene and the mTLL-1 gene Tll1 produce only unprocessed probiglycan. Thus, all detectable probiglycan-processing activity in MEFs is accounted for by the products of these two genes.

* This work was supported by National Institutes of Health Grants AR43621 and GM46846 (to D. S. G.), by a grant from FibroGen Inc. (South San Francisco, CA) (to D. S. G.), and by grants from the Medical Research Council of Canada (to P. J. R.) and the Shriners of North America (to P. J. R. and A. D. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The 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. Tel.: 608-262-4676; Fax: 608-262-6691; E-mail: dsgreens@facstaff.wisc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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