From Wikipedia, the free encyclopedia
Jump to: navigation, search

ADAMTS (A Disintegrin And Metalloproteinase with Thrombospondin Motifs) is a family of peptidases.[1] 19 members of this family have been identified in humans. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.[2] Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described.[3]

Family members are:

See also[edit]


  1. ^ Brocker, C; Vasiliou, V; Nebert, DW (Oct 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families.". Human Genomics 4 (1): 43–55. doi:10.1186/1479-7364-4-1-43. PMC 3500187. PMID 19951893. 
  2. ^ Apte, Suneel (2004). "A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family". The international Journal of Biochemistry and Cell Biology 15: 981–985. PMID 20036837. 
  3. ^ Cormier-Daire V, Le Goff C (2011). "The ADAMTS(L) family and human genetic disorders". Human Molecular Genetics 20 (R2): R163–R167. doi:10.1093/hmg/ddr361. PMID 21880666. 
  4. ^ METH-2 silencing and promoter hypermethylation in NSCLC