ADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes. Nineteen members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan, making them key remodeling enzymes of the extracellular matrix. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described. Most cases of thrombotic thrombocytopenic purpura arise from autoantibody-mediated inhibition of ADAMTS13.
Like ADAMs, the name of the ADAMTS family refers to its disintegrin and metalloproteinase activity, and in the case of ADAMTS, the presence of a thrombospondin motif.
ADAMTS family members
ADAMTS1 (or METH-1), an antiangiogenic ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 (=ADAMTS11) ADAMTS6 ADAMTS7 ADAMTS8 (or METH-2), an antiangiogenicMETH-2 silencing and promoter hypermethylation in NSCLC ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13 ADAMTS14 ADAMTS15 ADAMTS16 ADAMTS17 ADAMTS18 ADAMTS19 ADAMTS20
See also A disintegrin and metalloproteinase (ADAM) family ADAMTSL family (ADAMTS-like proteins)
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