ADAMTS

ADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes.{{cite journal|last=Brocker|first=C|author2=Vasiliou, V|author3= Nebert, DW|title=Evolutionary divergence and functions of the ADAM and ADAMTS gene families.|journal=Human Genomics|date=Oct 2009|volume=4|issue=1|pages=43–55|pmid=19951893|pmc=3500187|doi=10.1186/1479-7364-4-1-43|doi-access=free}} 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997.{{cite journal|last1=Porter|first1=Sarah|last2=Clark|first2=Ian M.|last3=Kevorkian|first3=Lara|last4=Edwards|first4=Dylan R.|title=The ADAMTS metalloproteinases|journal=Biochemical Journal|date=15 February 2005|volume=386|issue=1|pages=15–27|doi=10.1042/BJ20040424|pmid=15554875|pmc=1134762}} 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.{{cite journal|last=Apte|first=Suneel|title=A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family|journal=The International Journal of Biochemistry & Cell Biology|year=2004|pages=981–985|pmid=20036837|volume=15|issue=6|doi=10.1016/j.biocel.2004.01.014}}{{Cite journal

| last1 = Kelwick

| first1 = Richard

| last2 = Desanlis

| first2 = Ines

| last3 = Wheeler

| first3 = Grant N

| last4 = Edwards

| first4 = Dylan R

| date = 2015-05-30

| title = The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family

| journal = Genome Biology

| language = En

| volume = 16

| issue = 1

| pages = 113

| doi = 10.1186/s13059-015-0676-3

| pmc = 4448532

| pmid = 26025392

| doi-access = free

}} Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described.{{cite journal|last=Cormier-Daire V|first=Le Goff C|title=The ADAMTS(L) family and human genetic disorders|journal=Human Molecular Genetics|year=2011|pages=R163–R167|pmid=21880666|volume=20|doi=10.1093/hmg/ddr361|issue=R2|doi-access=free}} 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.