A disintegrin and metalloproteinase with thrombospondin motifs protein (ADAMTS protein)

A disintegrin and metalloproteinase with thrombospondin motifs proteins (ADAMTS proteins) are a family of extracellular, multidomain zinc-dependent protease enzymes consisting of at least 19 members in humans[1][3]. They participate in the processing of extracellular matrix components by cleaving proteoglycans and procollagens, as well as processing von Willebrand factor, impacting blood coagulation homeostasis[1][3]. ADAMTS enzymes are key regulators of tissue remodeling, angiogenesis, cell proliferation, cell migration, and inflammation, with individual proteins implicated in a range of physiological and pathological processes, including arthritis, cardiovascular disease, cancer, neurologic and connective tissue disorders, and thrombotic thrombocytopenic purpura (via ADAMTS13)[1][2][3][4][6]. Some members serve as candidate therapeutic targets, notably ADAMTS13, which is modulated by approved antibodies in the treatment of thrombotic microangiopathies. Dietary, genetic, or pharmacological perturbation of these proteases can yield both beneficial and adverse outcomes, requiring careful biomarker monitoring and assessment of safety in clinical development[1][2][6].

Other names

ADAMTS proteaseADAMTS enzymeA disintegrin and metalloproteinase with thrombospondin motifsADAMTS family

Inhibition of proteolytic activity (e.g., caplacizumab blocks ADAMTS13 binding to von Willebrand factor)