A disintegrin and metalloproteinase with a thrombospondin type 1 motif member 13 (ADAMTS13)

A disintegrin and metalloproteinase with a thrombospondin type 1 motif member 13 (ADAMTS13) is a circulating zinc-metalloprotease primarily synthesized in hepatic stellate cells (UniProt: P59510). Its essential physiological role is the regulation of hemostasis by cleaving ultra-large von Willebrand factor (UL-VWF) multimers at the Tyr1605-Met1606 bond within the VWF A2 domain (PubMed: 11564856). Without sufficient ADAMTS13 activity, these large multimers accumulate and spontaneously bind to platelets, leading to microvascular thrombosis and the life-threatening condition known as thrombotic thrombocytopenic purpura (TTP) (NIH: StatPearls NBK430721). Therapeutic interventions include the use of recombinant ADAMTS13 (Adzynma), which serves as an enzyme replacement therapy to restore normal VWF processing (FDA: Adzynma Approval 2023). Clinical management often involves monitoring ADAMTS13 activity levels and the presence of autoantibodies to guide treatment in both congenital and acquired forms of the disease (PubMed: 28115311). Beyond TTP, ADAMTS13 is being investigated for its potential role in other thrombotic and inflammatory conditions, such as stroke and myocardial infarction (PubMed: 28115311).

Other names

von Willebrand factor-cleaving proteaseVWFCPADAM-TS13

Enzyme replacement therapy to restore the cleavage of ultra-large von Willebrand factor multimers, preventing microvascular thrombosis.