Proteolytic cleavage of von Willebrand factor by ADAMTS-13 prevents uninvited clumping of blood platelets
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چکیده
منابع مشابه
ADAMTS‐13 and von Willebrand factor: a dynamic duo
von Willebrand factor (VWF) is a key player in hemostasis, acting as a carrier for factor VIII and capturing platelets at sites of vascular damage. To capture platelets, it must undergo conformational changes, both within its A1 domain and at the macromolecular level through A2 domain unfolding. Its size and this function are regulated by the metalloproteinase ADAMTS-13. Recently, it has been s...
متن کاملADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage.
A severe lack of von Willebrand factor-cleaving protease (VWF-CP) activity can cause thrombotic thrombocytopenic purpura (TTP). This protease was recently identified as a member of the ADAMTS family, ADAMTS-13. It consists of a preproregion, a metalloprotease domain, a disintegrin-like domain, a thrombospondin type-1 motif (Tsp1), a cysteine-rich domain, a spacer domain, additional Tsp1 repeats...
متن کاملCleavage of ultralarge multimers of von Willebrand factor by C-terminal-truncated mutants of ADAMTS-13 under flow.
A disintegrin-like and metalloprotease with thrombospondin type 1-motif 13 (ADAMTS-13) cleaves the A2 domain of von Willebrand factor (VWF), converting the ultralarge (UL) and hyperactive VWF multimers freshly released from endothelial cells to smaller and less active forms found in plasma. Recombinant ADAMTS-13 lacking the C-terminal region is active under static conditions, but its functions ...
متن کاملConformational quiescence of ADAMTS‐13 prevents proteolytic promiscuity
Essentials Recently, ADAMTS-13 has been shown to undergo substrate induced conformation activation. Conformational quiescence of ADAMTS-13 may serve to prevent off-target proteolysis in plasma. Conformationally active ADAMTS-13 variants are capable of proteolysing the Aα chain of fibrinogen. This should be considered as ADAMTS-13 variants are developed as potential therapeutic agents. Click to ...
متن کاملSialic acid prevents loss of large von Willebrand factor multimers by protecting against amino-terminal proteolytic cleavage.
Removal of sialic acid from the von Willebrand factor (vWF) subunit exposes additional cleavage sites in the amino-terminal region that are associated with loss of large multimers. The extent of large multimer loss was evaluated by examining the sites of subunit cleavage of native and carbohydrate-modified vWF after treatment with trypsin, chymotrypsin, or plasmin. In the presence of proteinase...
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ژورنال
عنوان ژورنال: Journal of Thrombosis and Haemostasis
سال: 2004
ISSN: 1538-7933,1538-7836
DOI: 10.1111/j.1538-7836.2004.00840.x