Disintegrin and metalloprotease with thrombospondin motifs 13 (ADAMTS13)

ADAMTS13 (Disintegrin and metalloprotease with thrombospondin motifs 13, abbreviated as ADAMTS13) is a secreted zinc metalloprotease essential for hemostasis. Its main function is to cleave the A2 domain of von Willebrand factor (vWF), a blood glycoprotein pivotal in platelet adhesion during vascular injury. This cleavage prevents the accumulation of ultra-large vWF multimers that otherwise promote inappropriate platelet clumping and microvascular thrombosis. Deficiency or inhibition of ADAMTS13 activity, whether congenital or acquired, can cause thrombotic thrombocytopenic purpura (TTP)—a life-threatening disorder characterized by widespread small vessel clotting. ADAMTS13 is structurally complex, with multiple domains including a metalloprotease domain, disintegrin-like domain, thrombospondin repeats, cysteine-rich regions, a spacer, and unique CUB domains which fine-tune its activity. Therapies aim to restore normal function via plasma or recombinant protein replacement, or modulate vWF function in related disorders

Other names

von Willebrand factor–cleaving protease (VWFCP)ADAMTS-13 proteaseUpshaw-Schulman syndrome-associated protease

Therapeutic replacement (supplementing ADAMTS13 activity in deficiency/TTP)\nModulation of vWF-mediated platelet adhesion and clot formation