ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.