ADAMTS

ADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes.[1] 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997.[2] 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.[3][4] Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described.[5]

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

See also

References

  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 3500187Freely accessible. PMID 19951893.
  2. ↑ Porter, Sarah; Clark, Ian M.; Kevorkian, Lara; Edwards, Dylan R. (15 February 2005). "The ADAMTS metalloproteinases". Biochemical Journal. 386 (1): 15–27. doi:10.1042/BJ20040424.
  3. ↑ 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.
  4. ↑ Kelwick, Richard; Desanlis, Ines; Wheeler, Grant N; Edwards, Dylan R (2015-05-30). "The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family". Genome Biology. 16 (1). doi:10.1186/s13059-015-0676-3. PMC 4448532Freely accessible. PMID 26025392.
  5. ↑ 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.
  6. ↑ METH-2 silencing and promoter hypermethylation in NSCLC
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