A disintegrin and metalloproteinase with thrombospondin motifs 9 is an enzyme that in humans is encoded by the ADAMTS9gene.[5][6]
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) 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. Members of the ADAMTS family have been implicated in the cleavage of proteoglycans, the control of organ shape during development, and the inhibition of angiogenesis. This gene is localized to chromosome 3p14.3-p14.2, an area known to be lost in hereditary renal tumors.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Clark ME, Kelner GS, Turbeville LA, Boyer A, Arden KC, Maki RA (Sep 2000). "ADAMTS9, a novel member of the ADAM-TS/ metallospondin gene family". Genomics. 67 (3): 343–50. doi:10.1006/geno.2000.6246. PMID10936055.
Cross NA, Chandrasekharan S, Jokonya N, et al. (2005). "The expression and regulation of ADAMTS-1, -4, -5, -9, and -15, and TIMP-3 by TGFbeta1 in prostate cells: relevance to the accumulation of versican". Prostate. 63 (3): 269–75. doi:10.1002/pros.20182. PMID15599946. S2CID24137815.
Zeng W, Corcoran C, Collins-Racie LA, et al. (2006). "Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5, -9, -16 and -18". Biochim. Biophys. Acta. 1760 (3): 517–24. doi:10.1016/j.bbagen.2006.01.013. PMID16507336.
