The ADAMTS metalloproteinases

Biochem J. 2005 Feb 15;386(Pt 1):15-27. doi: 10.1042/BJ20040424.


The ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) are a group of proteases that are found both in mammals and invertebrates. Since the prototype ADAMTS-1 was first described in 1997, there has been a rapidly expanding body of literature describing this gene family and the proteins they encode. The complete human family has 19 ADAMTS genes, together with three members of a newly identified subgroup, the ADAMTSL (ADAMTS-like) proteins, which have several domains in common with the ADAMTSs. The ADAMTSs are extracellular, multidomain enzymes whose known functions include: (i) collagen processing as procollagen N-proteinase; (ii) cleavage of the matrix proteoglycans aggrecan, versican and brevican; (iii) inhibition of angiogenesis; and (iv) blood coagulation homoeostasis as the von Willebrand factor cleaving protease. Roles in organogenesis, inflammation and fertility are also apparent. Recently, some ADAMTS genes have been found to show altered expression in arthritis and various cancers. This review highlights progress in understanding the structural organization and functional roles of the ADAMTSs in normal and pathological conditions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Angiogenesis Inhibitors / physiology
  • Animals
  • Cloning, Molecular
  • Extracellular Matrix Proteins / metabolism
  • Forecasting
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Metalloendopeptidases / biosynthesis
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / classification
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / physiology*
  • Multigene Family
  • Neoplasm Proteins / biosynthesis
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / physiology
  • Protease Inhibitors / pharmacology
  • Protein Structure, Tertiary
  • Rats
  • Substrate Specificity
  • Terminology as Topic


  • Angiogenesis Inhibitors
  • Extracellular Matrix Proteins
  • Neoplasm Proteins
  • Protease Inhibitors
  • Metalloendopeptidases