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Blood, 1 July 2005, Vol. 106, No. 1, pp. 141-143. Prepublished online as a Blood First Edition Paper on March 17, 2005; DOI 10.1182/blood-2004-11-4188. This Article Full Text (PDF) All Versions of this Article: 2004-11-4188v1 106/1/141    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Tao, Z. Articles by Dong, J.-f. Search for Related Content PubMed PubMed Citation Articles by Tao, Z. Articles by Dong, J.-f. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted November 16, 2004 Accepted March 5, 2005 Cleavage of ultra-large multimers of Von Willebrand factor by C-terminal truncated mutants of ADAMTS-13 under flow Zhenyin Tao, Yongtao Wang, Huiwei Choi, Aubrey Bernardo, Kenji Nishio, J E Sadler, Jose A Lopez, and Jing-fei Dong* Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, Houston, TX, USA Hematology Division, Department of Medicine, Washington University, St. Louis, MO, USA * Corresponding author; email: jfdong{at}bcm.tmc.edu. ADAMTS-13 cleaves the A2 domain of von Willebrand factor, converting the ultra-large (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 under flow conditions have not been determined. Here, we show that VWF-cleaving activity measured under flow was preserved in an ADAMTS-13 mutant lacking the 2nd to 8th TSP-1 motifs and the CUB domains, but was severely deficient in a mutant that was further truncated to remove the spacer domain. We also show that the mutant lacking the TSP-1 and CUB domains was hyperactive under flow, suggesting that the C-terminal region may negatively regulate ADAMTS-13 activity. The wild-type and the mutant without the spacer were more active in the presence of plasma, raising the possibility of ADAMTS-13 cofactors in plasma. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: R. de Groot, A. Bardhan, N. Ramroop, D. A. Lane, and J. T. B. Crawley Essential role of the disintegrin-like domain in ADAMTS13 function Blood, May 28, 2009; 113(22): 5609 - 5616. [Abstract] [Full Text] [PDF] F. Banno, A. K. Chauhan, K. Kokame, J. Yang, S. Miyata, D. D. Wagner, and T. 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Tsai An IAP retrotransposon in the mouse ADAMTS13 gene creates ADAMTS13 variant proteins that are less effective in cleaving von Willebrand factor multimers Blood, August 1, 2007; 110(3): 886 - 893. [Abstract] [Full Text] [PDF] C. Gendron, M. Kashiwagi, N. H. Lim, J. J. Enghild, I. B. Thogersen, C. Hughes, B. Caterson, and H. Nagase Proteolytic Activities of Human ADAMTS-5: COMPARATIVE STUDIES WITH ADAMTS-4 J. Biol. Chem., June 22, 2007; 282(25): 18294 - 18306. [Abstract] [Full Text] [PDF] D. Shang, X. W. Zheng, M. Niiya, and X. L. Zheng Apical sorting of ADAMTS13 in vascular endothelial cells and Madin-Darby canine kidney cells depends on the CUB domains and their association with lipid rafts Blood, October 1, 2006; 108(7): 2207 - 2215. [Abstract] [Full Text] [PDF] R. Donadelli, J. N. Orje, C. Capoferri, G. Remuzzi, and Z. M. Ruggeri Size regulation of von Willebrand factor-mediated platelet thrombi by ADAMTS13 in flowing blood Blood, March 1, 2006; 107(5): 1943 - 1950. [Abstract] [Full Text] [PDF] K. Soejima, H. Nakamura, M. Hirashima, W. Morikawa, C. Nozaki, and T. Nakagaki Analysis on the Molecular Species and Concentration of Circulating ADAMTS13 in Blood J. Biochem., January 1, 2006; 139(1): 147 - 154. [Abstract] [Full Text] [PDF] B. Plaimauer, J. Fuhrmann, G. Mohr, W. Wernhart, K. Bruno, S. Ferrari, C. Konetschny, G. Antoine, M. Rieger, and F. Scheiflinger Modulation of ADAMTS13 secretion and specific activity by a combination of common amino acid polymorphisms and a missense mutation Blood, January 1, 2006; 107(1): 118 - 125. [Abstract] [Full Text] [PDF] Z. Tao, Y. Peng, L. Nolasco, S. Cal, C. Lopez-Otin, R. Li, J. L. Moake, J. A. Lopez, and J.-f. Dong Recombinant CUB-1 domain polypeptide inhibits the cleavage of ULVWF strings by ADAMTS13 under flow conditions Blood, December 15, 2005; 106(13): 4139 - 4145. [Abstract] [Full Text] [PDF] J. Ai, P. Smith, S. Wang, P. Zhang, and X. L. Zheng The Proximal Carboxyl-terminal Domains of ADAMTS13 Determine Substrate Specificity and Are All Required for Cleavage of von Willebrand Factor J. Biol. Chem., August 19, 2005; 280(33): 29428 - 29434. [Abstract] [Full Text] [PDF]

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