This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene contains two disintegrin loops and three C-terminal TS motifs and has anti-angiogenic activity. The expression of this gene may be associated with various inflammatory processes as well as development of cancer cachexia. This gene is likely to be necessary for normal growth, fertility, and organ morphology and function.
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^Luque A, Carpizo DR, Iruela-Arispe ML (June 2003). "ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165". J. Biol. Chem.278 (26): 23656–65. doi:10.1074/jbc.M212964200. PMID12716911.
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Rodríguez-Manzaneque JC, Westling J, Thai SN, et al. (2002). "ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors". Biochem. Biophys. Res. Commun.293 (1): 501–8. doi:10.1016/S0006-291X(02)00254-1. PMID12054629.
Luque A, Carpizo DR, Iruela-Arispe ML (2003). "ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165". J. Biol. Chem.278 (26): 23656–65. doi:10.1074/jbc.M212964200. PMID12716911.
Russell DL, Doyle KM, Ochsner SA, et al. (2004). "Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation". J. Biol. Chem.278 (43): 42330–9. doi:10.1074/jbc.M300519200. PMID12907688.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet.36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
The MEROPS online database for peptidases and their inhibitors: M12.222