| Modification Notes |
ADAMTS (a disintegrin and metalloproteinase domain with Thrombospondin type 1 modules) proteins comprise a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS family members contain an N-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a C-terminus that contains a varying number of thrombospondin type 1 (TSP-1) motifs. ADAMTS-5 (A disintegrin and metalloproteinase with thrombospondin motifs 5), also known as ADAMTS11 or ADMP2, is a 930 amino acid secreted protein that localizes to the extracellular matrix and contains one disintegrin domain, one peptidase M12B domain and two TSP type-1 domains. Expressed at low levels in heart, brain, bladder, cervix and placental tissue, ADAMTS-5 uses zinc as a cofactor to catalyze the cleavage of aggregan (a cartilage proteoglycan) and is thought to be involved in aggregan turnover, specifically in the destruction of aggregan in arthritic diseases. Due to its involvement in aggregan degradation, ADAMTS-5 is thought to play a role in the pathogenesis of osteoarthritis. The ADAMTS-5 precursor is processed by furin endopeptidase to yield a smaller, active form of the expressed protein. |
