Recombinant Human ADAMTS13 protein

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ADAMTS13 also known as von Willebrand factor-cleaving protease (VWFCP) is a zinc-containing metalloprotease with a molecular mass of approximately 190 kDa. This protein belongs to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family and exhibits a complex structure with specific domains including a metalloprotease and a disintegrin-like domain. ADAMTS13 is produced mainly in the liver and circulates in the blood plasma. Research shows that it primarily facilitates the cleavage of von Willebrand factor (vWF) a large multimeric protein essential for blood clotting.

Biological function summary

ADAMTS13 plays a role in regulating the size and function of von Willebrand factor (vWF) ensuring proper hemostatic balance. The enzyme prevents the accumulation of ultra-large vWF multimers which can lead to spontaneous platelet aggregation and thrombus formation. Although ADAMTS13 acts independently its function is closely linked to the dynamics of vWF in response to vascular injury. Properly functioning ADAMTS13 aids in maintaining normal blood flow by preventing unnecessary clot formation in the bloodstream.

Pathways

ADAMTS13 is critical in the coagulation and hemostatic pathways. It operates by modulating the activity of vWF which plays an essential role in platelet adhesion and aggregation forming part of the coagulation cascade. A significant relationship exists between ADAMTS13 and vWF in these pathways as the protease controls vWF multimer size directly impacting clot formation. In the context of hemostatic balance ADAMTS13 intersects with factors like thrombin and fibrinogen which further contribute to clotting processes.

Associated diseases and disorders

ADAMTS13 deficiency or dysfunction is associated with thrombotic thrombocytopenic purpura (TTP) a rare but severe blood disorder. In TTP the reduced activity of ADAMTS13 leads to an over-accumulation of ultra-large vWF multimers resulting in excessive platelet aggregation and microvascular thrombosis. Another related condition is atypical hemolytic uremic syndrome (aHUS) where abnormal ADAMTS13 activity might exacerbate the disease pathology. Both disorders highlight the critical need for balanced ADAMTS13 function in maintaining vascular health and highlight its potential as a therapeutic target.