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

ADAMTS13 (A disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13) is a zinc-dependent metalloprotease primarily synthesized in the liver that circulates in the plasma. Its primary biological function is the proteolytic cleavage of ultra-large von Willebrand factor (UL-VWF) multimers at the Tyr1605-Met1606 bond within the VWF A2 domain [UniProt]. By reducing the size of these multimers, ADAMTS13 prevents the spontaneous adhesion and aggregation of platelets, thereby maintaining microvascular patency [PubMed]. A severe deficiency in ADAMTS13 activity (typically <10%) leads to thrombotic thrombocytopenic purpura (TTP), a life-threatening condition marked by widespread microvascular thrombosis, hemolytic anemia, and organ failure [NIH]. TTP can be congenital (Upshaw-Schulman syndrome) due to genetic mutations or acquired via autoantibodies that inhibit the enzyme or accelerate its clearance [StatPearls]. Therapeutic management involves restoring enzyme activity through plasma exchange or the administration of recombinant human ADAMTS13 (e.g., Adzynma), which is the first approved enzyme replacement therapy for congenital TTP [FDA]. Beyond TTP, ADAMTS13 is being investigated for its potential role in modulating thrombosis and inflammation in conditions such as stroke and myocardial infarction [PubMed].

Other names

von Willebrand factor-cleaving proteaseVWFCPvWF-CPC9orf8

Enzyme replacement therapy to restore the proteolytic cleavage of ultra-large von Willebrand factor (VWF) multimers at the Tyr1605-Met1606 bond.