Abstract
Dermatosparaxis and Ehlers-Danlos syndrome type VIIC (EDS VIIC) are recessive, heritable disorders of domestic animals and humans, respectively. These phenotypes are primarily characterized by extreme fragility of the skin, and are marked by accumulation in skin of processing intermediates in the conversion of procollagen precursors into mature type I collagen monomers. The latter are capable of forming the fibrils that are the major structural components of dermis. This accumulation of precursors is due to a deficiency in skin in levels of a proteolytic activity that normally cleaves NH2-terminal peptide extensions (N-propeptides) from the procollagen precursors of collagen types I and II, the latter being the major collagen type of cartilage. In recent years, this procollagen N-proteinase activity has been demonstrated to be furnished by the metalloproteinase ADAMTS-2. Although the activity responsible for cleaving the type III procollagen N-propeptide has long been thought to be furnished by a different proteinase than that which cleaves the N-propeptides of procollagens I and II, recent evidence has shown ADAMTS-2 to have high levels of all three activities. Thus, a defect in ADAMTS-2 expression results in deficient procollagen III processing, which probably contributes to the Dermatosparaxis/EDS VIIC phenotype. ADAMTS-2 belongs to the recently described family of ADAMTS (A Disintegrin And Metalloproteinase with ThromboSpondin motifs), members of which are related by a common domain structure and sequence homologies. There are 19 known ADAMTS proteinases in vertebrates, and defects in a number of these are implicated as causal in diseases that include dermatosparaxis/EDS VIIC, osteoarthritis, inflammatory joint disease and thrombotic thrombocytopenic purpura. ADAMTS proteinases are also involved in growth, organogenesis and fertility in a broad spectrum of species that range from humans to worms.
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Greenspan, D.S., Wang, WM. (2005). Overview of ADAMTS Proteinases and ADAMTS 2. In: Hooper, N.M., Lendeckel, U. (eds) The ADAM Family of Proteases. Proteases in Biology and Disease, vol 4. Springer, Boston, MA. https://doi.org/10.1007/0-387-25151-0_12
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