ADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc Metalloproteases

By T. Hurskainen, S. Hirohata, M. Seldin, S. Apte. 1999

We report the primary structure of three novel, putative zinc metalloproteases designated ADAM-TS5, ADAM-TS6, and ADAM-TS7. All have a similar domain organization, comprising a preproregion, a reprolysin-type catalytic domain, a disintegrin-like domain, a thrombospondin type-1 (TS) module, a cysteine-rich domain, a spacer domain without cysteine residues, and a COOH-terminal TS module. These genes are differentially regulated during mouse embryogenesis and in adult tissues, with Adamts5 highly expressed in the peri-implantation period in embryo and trophoblast. These proteins are similar to four other cognate gene products, defining a distinct family of human reprolysin-like metalloproteases, the ADAM-TS family. The other members of the family are ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino-propeptide processing enzyme (PCINP, ADAM-TS2), and proteins predicted by the KIAA0366 andKIAA0688 genes (ADAM-TS3 and ADAM-TS4). Individual ADAM-TS members differ in the number of COOH-terminal TS modules, and some have unique COOH-terminal domains. The ADAM-TS genes are dispersed in human and mouse genomes.

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Citations in the corpus

Knockout of Adamts7, A Novel CAD Locus in Humans, Reduces Atherosclerosis in Mice (2015, background): “ADAMTS7 is a member of the ADAMTS family of secreted zinc metalloproteases with characteristic protein domain composition, including at least 1 thrombospondin type I repeat.(6,7) These proteins have highly homologous N-terminal protein domain structure and organization, but the C-terminal halves var”
Biochemistry and physiological functions of ADAMTS7 metalloprotease (2013, background): “This suggests that ADAMTS7 is most likely not a redundant enzyme in the family, and it, like ADAMTS13, probably possesses one or several unique substrates.”
ADAM 23/MDC3, a Human Disintegrin That Promotes Cell Adhesion via Interaction with the αvβ3 Integrin through an RGD-independent Mechanism (2000, unknown): “The modular structure of members of the recently described ADAM-TS subfamily containing thrombospondin-1 repeats is shown by Hurskainen et al. (1999). the structure of the actin cytoskeleton in NB100 cells adherent to either ADAM 23 or fibronectin (Figure 4, E–”