Bone morphogenetic proteins (BMPs) are bone-derived factors capable of
inducing ectopic bone formation. Unlike other BMPs, BMP-1 is not like
transforming growth factor-beta (TGF-beta), but it is the prototype o
f a family of putative proteases implicated in pattern formation durin
g development in diverse organisms. Although some members of this grou
p, such as Drosophila tolloid (TLD), are postulated to activate TGF-be
ta-like proteins, actual substrates are unknown, Procollagen C-protein
ase (PCP) cleaves the COOH-propeptides of procollagens I, II, and III
to yield the major fibrous components of vertebrate extracellular matr
ix. Here it is shown that BMP-1 and PCP are identical. This demonstrat
ion of enzymatic activity for a BMP-1/TLD-like protein links an enzyme
involved in matrix deposition to genes involved in pattern formation.