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Blood, 15 December 2005, Vol. 106, No. 13, pp. 4139-4145.
Prepublished online as a Blood First Edition Paper on September 1, 2005; DOI 10.1182/blood-2005-05-2029.
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Submitted May 23, 2005
Accepted July 25, 2005
Role of the CUB-1 domain in docking ADAMTS-13 to unusually large Von Willebrand factor in flowing blood
Zhenyin Tao, Yuandong Peng, Laticia Nolasco, Santiago Cal, Carlos Lopez-Otin, Renhao Li, Joel L Moake, Jose A Lopez, and Jing-fei Dong*
Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, Houston, TX, USA
Department of Biochemistry and Molecular Biology, University of Oviedo, Oviedo, Spain
Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX, USA
* Corresponding author; email: jfdong{at}bcm.tmc.edu.
The metalloprotease ADAMTS-13 converts the hyper-reactive unusually large (UL) forms of von Willebrand factor (VWF) that are newly released from endothelial cells into less active plasma forms by cleaving a peptide bond in the VWF A2 domain. Familial or acquired deficiency of this metalloprotease leads to the thrombotic disorder, thrombotic thrombocytopenic purpura (TTP). ADAMTS-13 belongs to the ADAMTS metalloprotease family, but, unlike other members, it also contains two C-terminal CUB domains (Complement component Clr/Cls, Uegf, and Bone morphogenic protein 1). Mutations in the CUB region have been found in congenital TTP, but deletion of the region did not impair enzyme activity in conventional in vitro assays. We investigated the functions of the CUB domain in ADAMTS-13 activity under flow conditions. We found that recombinant CUB-1 and CUB-1+2 polypeptides and synthetic peptides derived from the CUB-1 partially blocked the cleavage of ULVWF by ADAMTS-13 on the surface of endothelial cells under flow. The polypeptide bound immobilized and soluble forms of ULVWF, and blocked the adhesion of ADAMTS-13-coated beads to immobilized ULVWF under flow. These results suggest that the CUB-1 domain may serve as the docking site for ADAMTS-13 to bind ULVWF under flow, a critical step to initiate ULVWF proteolysis.
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