Interactions of von Willebrand factor and ADAMTS13 in von Willebrand disease and thrombotic thrombocytopenic purpura
| Autor: | U. Budde, R. Schneppenheim |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
0301 basic medicine
congenital hereditary and neonatal diseases and abnormalities Thrombotic thrombocytopenic purpura ADAMTS13 Protein Disease 030204 cardiovascular system & hematology 03 medical and health sciences 0302 clinical medicine Von Willebrand factor hemic and lymphatic diseases Protein Interaction Mapping von Willebrand Factor Enhanced degradation Von Willebrand disease Animals Humans Medicine Platelet Blood Coagulation Hyaline Purpura Thrombotic Thrombocytopenic biology business.industry Models Cardiovascular Hematology medicine.disease ADAMTS13 ADAM Proteins von Willebrand Diseases 030104 developmental biology Immunology cardiovascular system biology.protein business Dimerization Biomarkers Protein Binding circulatory and respiratory physiology |
| Zdroj: | Hämostaseologie. 34:215-225 |
| ISSN: | 2567-5761 0720-9355 |
| DOI: | 10.5482/hamo-13-08-0045 |
| Popis: | SummaryThe function of von Willebrand factor (VWF), a huge multimeric protein and a key factor in platelet dependent primary haemostasis, is regulated by its specific protease ADAMTS13. The ADAMTS13 dependent degradation of VWF to its proteolytic fragments can be visualized as a characteristic so-called triplet structure of individual VWF oligomers by multimer analysis. Lack of VWF high molecular weight multimers (VWF-HMWM) or their pathologically enhanced degradation under - lies a particular type of von Willebrand disease, VWD type 2A with a significant bleeding tendency, and may also be observed in acquired von Willebrand syndrome due to cardiovascular disease. In these conditions multimer analysis is an obligatory and powerful tool for diagnosis of VWD. The opposite condition, the persistence of ultralarge VWF (UL-VWF) multimers may cause the microangiopathic life-threatening disorder thrombotic thrombocytopenic purpura (TTP). During the course of active TTP, UL-VWF is consumed in the hyaline thrombi formed in the microvasculature which will ultimately result in the loss of UL-VWF and VWF-HMWM. Therefore, VWF multimer analysis is not a valid tool to diagnose TTP in the active phase of disease but may be helpful for the diagnosis of TTP patients in remission. |
| Databáze: | OpenAIRE |
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