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Papers In Press, published online ahead of print September 5, 2002
School of Biological Sciences, University of Manchester, Manchester M13 9PT
Corresponding Author: laure.garrigue-antar{at}man.ac.uk
Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins. Sequence analysis suggests that BMP-1 has 6 potential N-linked glycosylation sites (i.e. NXS/T) namely: N91 (prodomain), N142 (metalloproteinase domain), N332 and N363 (CUB1 domain), N599 (CUB3 domain), and N726 in the C-terminal specific domain. In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except N726 presumably because proline occurs immediately C-terminal of threonine in the consensus sequence. Recombinant BMP-1 molecules lacking all glycosylation sites or the 3 CUB-specific sites were not secreted. BMP-1 lacking CUB glycosylation was translocated to the proteasome for degradation. BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase (PCP) activity, but N332Q and N599Q exhibited a slower rate of cleavage. BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation. The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
J. Biol. Chem, 10.1074/jbc.M207342200
Submitted on July 22, 2002
Revised on September 3, 2002
Accepted on September 5, 2002
Post-translational modification of bone morphogenetic protein (BMP)-1 is required for secretion and stability of the protein
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