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von Willebrand factor, ADAMTS-13, and thrombotic thrombocytopenic purpura.

Authors: Moake, JL 
Citation: Moake JL Semin Hematol. 2004 Jan;41(1):4-14.
Pubmed: (View Article at PubMed) PMID:14727254

Thrombotic thrombocytopenic purpura (TTP) is a severe, occlusive, microvascular "thrombotic microangiopathy" characterized by systemic platelet aggregation, organ ischemia, profound thrombocytopenia, and erythrocyte fragmentation. Failure to degrade "unusually large" (UL) von Willebrand factor (VWF) multimers as they are secreted from endothelial cells probably causes most cases of familial TTP, acquired idiopathic TTP, thienopyridine-related TTP, and pregnancy-associated TTP. The emphasis in this review is the pathophysiology of familial and acquired idiopathic TTP. In each of these entities, there is a severe defect in the function of a plasma enzyme, VWF-cleaving metalloprotease (ADAMTS-13), that normally cleaves hyper-reactive ULVWF multimers into smaller and less adhesive VWF forms. In familial TTP, mutations in the ADAMTS13 gene cause absent or severely reduced plasma VWF-cleaving metalloprotease activity. Acquired idiopathic TTP, in contrast, is the result in many patients of the production of autoantibodies that inhibit the function of ADAMTS-13. Established, evolving, and some of the unresolved issues in TTP pathophysiology will be summarized.


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CRRD Object Information
CRRD ID: 1580644
Created: 2006-08-18
Species: All species
Last Modified: 2006-08-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.