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ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) are multidomain extracellular proteinases, containing at least one thrombospondin type-1 repeat [1]. The enzymes are involved in processing of extracellular matrix proteins and proteins in the circulation. ADAMTS5 was first purified from bovine nasal cartilage conditioned media and human ADAMTS5 cDNA was cloned from a human liver cDNA library [2]. ADAMTS5 consists of a prodomain, a catalytic domain, a disintegrin domain, a thrombospondin type-1 motif, a Cys-rich region followed by a spacer sequence and thrombospondin submotifs. The prodomain is most likely cleaved-off by a furin-type enzyme before ADAMTS5 is released from cells.

ADAMTS5 is expressed constitutively in synovium [3] and it degrades aggrecan, the major proteoglycan of articular cartilage [4]. Like ADAMTS4, another member of the ADAMTS-family, ADAMTS5 cleaves aggrecan at 5 sites [4]. Four cleavage sites are located in the chondroitin sulfate-rich region between aggrecan globular domains G2 and G3, while one site is contained in the rod-shaped polypeptide between globular domains G1 and G2. In addition, ADAMTS5 cleaves one more site in the chondroitin sulfate-rich region that is not cleaved by ADAMTS4 [4]

ADAMTS5 is inhibited by TIMP 3 [5,6] and ?2-macroglobulin [7].