BACKGROUND
The metalloprotease ADAMTS13 regulates the platelet adhesion by von Willebrand factor (VWF) by severing large, prothrombotic VWF-Platelet aggregates. Genetic or autoimmune deficiency of ADAMTS13 impairs this regulatory mechanism causing thrombotic thrombocytopenic purpura (TTP), a rare fatal blood clotting disorder characterized by microangiopathic hemolytic anemia, thrombocytopenia, and deposition of microthrombi in small blood vessels. Assaying ADAMTS13 activity is very important in TTP diagnosis because it is the only test that confirms the presence of the disease. However, ADAMTS13 assays are slow to run and can be skewed by other enzymatic activity. There is a need for an improvement on ADAMTS13 assays from both medical and research perspectives.
SUMMARY OF TECHNOLOGY
Researchers at OSU have developed a multiplex-based assay to characterize ADAMTS13 properties and function. This next generation of assays function for both diagnostic purposes and to characterize the function of this enzyme. Several substrate variants based on novel substrates previously developed by the group enable the characterization of ADAMTS13 properties and function as well as diagnosis, making it a strong research tool. This assay can be developed for effectively any vertebrate, lending investigative power of this enzyme into more traditional biomedical animal systems.
POTENTIAL AREAS OF APPLICATION
MAIN ADVANTAGES
STAGE OF DEVELOPMENT