Abstract
ADAMTS13 (a disintegrin-like metalloprotease domain with thrombospondin type 1 motif,
member 13) is a protease of crucial importance in the regulation of the size of von
Willebrand factor multimers. Very low ADAMTS13 activity levels result in thrombotic
thrombocytopenic purpura, a rare and life-threatening disease. The mechanisms involved
can either be acquired (immune-mediated thrombotic thrombocytopenic purpura [iTTP])
or congenital (cTTP, Upshaw–Schulman syndrome) caused by the autosomal recessive inheritance
of disease-causing variants (DCVs) located along the ADAMTS13 gene, which is located in chromosome 9q34. Apart from its role in TTP, and as a regulator
of microthrombosis, ADAMTS13 has begun to be identified as a prognostic and/or diagnostic
marker of other diseases, such as those related to inflammatory processes, liver damage,
metastasis of malignancies, sepsis, and different disorders related to angiogenesis.
Since its first description almost 100 years ago, the improvement of laboratory tests
and the description of novel DCVs along the ADAMTS13 gene have contributed to a better and faster diagnosis of patients under critical
conditions. The ability of ADAMTS13 to dissolve platelet aggregates in vitro and its
antithrombotic properties makes recombinant human ADAMTS13 treatment a potential therapeutic
approach targeting not only patients with cTTP but also other medical conditions.
Keywords
ADAMTS13 - thrombotic thrombocytopenic purpura - Upshaw–Schulman syndrome - genotypic
studies - phenotypic studies
