ADAM metallopeptidase with thrombospondin type 1 motif 6 (ADAMTS6)

ADAM metallopeptidase with thrombospondin type 1 motif 6 (ADAMTS6) is a secreted, catalytically active metalloproteinase of the ADAMTS family, characterized by a metalloprotease domain, disintegrin-like domain, and multiple thrombospondin type 1 repeats. ADAMTS6 modulates the extracellular matrix by cleaving specific proteins, especially impacting microfibril assembly and cell-cell junction integrity. Increased ADAMTS6 activity disrupts epithelial cell-cell junctions (tight and adherens junctions), reduces deposition of microfibrils (such as fibrillin-1 and fibronectin), and depletes cell surface heparan sulfate by proteolytic cleavage, including of syndecan-4. These actions influence tissue architecture and homeostasis, and aberrant expression or activity is associated with connective tissue abnormalities, including predisposition to hernias and possible roles in other connective tissue diseases[1][2][3][6].

Other names

ADAM-TS6ADAMTS-6ADAM-TS 6A disintegrin and metalloproteinase with thrombospondin motifs 6A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 6EC 3.4.24.82EC 3.4.24.-[2][3]

Proteolytic cleavage of extracellular matrix components. Disruption of cell surface heparan sulfate and associated proteoglycans (such as syndecan-4).