ADAMTSs (a disintegrin and metalloprotease with thrombospondin type 1 motifs) constitute a family of extracellular proteases which are implicated in cleaving the protein versican. The process of bone development was divided into the beginning of osteogenesis, woven bone, and lamellar bone stages. Versican protein was abundant in the woven bone matrix, but decreased in the lamellar bone matrix. Versican mRNA was prominent in some osteoblasts with corresponding localization of the cognate protein. The temporal and spatial mRNA expression pattern of ADAMTS1, 4, and 5 was comparable with that of versican. These results suggest that woven bone rich in versican alters into lamellar bone containing little versican during bone development in both mandibles and hind limbs, where some osteoblasts may be involved in production as well as degradation of versican, by secreting ADAMTS1, 4, and 5.
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