PMC

Evan Sadler

Structure of ADAMTS13. The primary translation product consists of 1427 amino acid residues. Motifs include a signal peptide (S), propeptide (P), metalloprotease (M), disintegrin (D), Cys-rich, spacer, CUB, and thrombospondin (TSP1) domains (1-8).

Pathogenesis of idiopathic TTP caused by ADAMTS13 deficiency. Multimeric VWF adheres to endothelial cells or to connective tissue exposed in the vessel wall. Platelets adhere to VWF through platelet membrane GPIb. In flowing blood, VWF in the platelet-rich thrombus is stretched and cleaved by ADAMTS13, limiting thrombus growth. If ADAMTS13 is absent, VWF-dependent platelet accumulation continues, eventually causing microvascular thrombosis and TTP.