A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAMTS7)

A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAMTS7) is a secreted zinc-dependent metalloproteinase that plays a central role in the remodeling of the extracellular matrix, particularly through proteolytic cleavage of cartilage oligomeric matrix protein (COMP) and other substrates[1][2][3][5]. ADAMTS7 promotes vascular smooth muscle cell migration and neointimal formation in the vasculature, contributing to atherosclerotic plaque development and is genetically associated with increased coronary artery disease risk[2][3][4]. In joint tissues, it is implicated in matrix degradation observed in arthritic disorders, including rheumatoid arthritis[2][3]. ADAMTS7 activity is also linked to disc degeneration and generalized inflammatory changes[2][3]. The enzyme is considered a promising therapeutic target for cardiovascular and arthritic diseases, with inhibition of its metalloproteinase activity being investigated as a potential medical intervention[4]. Genetic loss-of-function or hypomorphic variants are protective for atherosclerosis and may represent natural models for therapy design[4]. There are currently no approved drugs directly targeting ADAMTS7, though it is under consideration as a novel drug target[2][3][4].

Other names

ADAMTS-7ADAM-TS7DKFZp434H204COMPasea disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 7ADAMTS7 preproprotein

Inhibition of metalloproteinase activity (proposed as therapeutic mechanism in cardiovascular and arthritic diseases) Potential use of genetic variants resulting in reduced enzyme secretion/activity as protective mechanisms