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Blood, 21 May 2009, Vol. 113, No. 21, pp. 5323-5329. Prepublished online as a Blood First Edition Paper on December 24, 2008; DOI 10.1182/blood-2008-07-169359. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2008-07-169359v1 113/21/5323    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Google Scholar Articles by Banno, F. Articles by Miyata, T. PubMed PubMed Citation Articles by Banno, F. Articles by Miyata, T. Related Collections Thrombosis and Hemostasis Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  THROMBOSIS AND HEMOSTASIS The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation Fumiaki Banno1, Anil K. Chauhan2,3, Koichi Kokame1, Jin Yang1, Shigeki Miyata4, Denisa D. Wagner2,3, and Toshiyuki Miyata1 1 Research Institute, National Cardiovascular Center, Suita, Japan; 2 Immune Disease Institute and 3 Department of Pathology, Harvard Medical School, Boston, MA; and 4 Division of Transfusion Medicine, National Cardiovascular Center, Suita, Japan ADAMTS13 is a multidomain protease that limits platelet thrombogenesis through the cleavage of von Willebrand factor (VWF). We previously identified 2 types of mouse Adamts13 gene: the 129/Sv-strain Adamts13 gene encodes the long-form ADAMTS13 having the same domains as human ADAMTS13, whereas the C57BL/6-strain Adamts13 gene encodes the short-form ADAMTS13 lacking the distal C-terminal domains. To assess the physiologic significance of the distal C-terminal domains of ADAMTS13, we generated and analyzed 129/Sv-genetic background congenic mice (Adamts13S/S) that carry the short-form ADAMTS13. Similar to wild-type 129/Sv mice (Adamts13L/L), Adamts13S/S did not have ultralarge VWF multimers in plasma, in contrast to 129/Sv-genetic background ADAMTS13-deficient mice (Adamts13–/–). However, in vitro thrombogenesis under flow at a shear rate of 5000 s–1 was accelerated in Adamts13S/S compared with Adamts13L/L. Both in vivo thrombus formation in ferric chloride–injured arterioles and thrombocytopenia induced by collagen plus epinephrine challenge were more dramatic in Adamts13S/S than in Adamts13L/L but less than in Adamts13–/–. These results suggested that the C-terminally truncated ADAMTS13 exhibited decreased activity in the cleavage of VWF under high shear rate. Role of the C-terminal domains may become increasingly important under prothrombotic conditions. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: ADAMTS13's tail tale Karen Vanhoorelbeke, Hendrik B. Feys, and Simon F. De Meyer Blood 2009 113: 5039-5040. [Full Text] [PDF] This article has been cited by other articles: S. Zanardelli, A. C. K. Chion, E. Groot, P. J. Lenting, T. A. J. McKinnon, M. A. Laffan, M. Tseng, and D. A. Lane A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF Blood, September 24, 2009; 114(13): 2819 - 2828. [Abstract] [Full Text] [PDF] K. Vanhoorelbeke, H. B. Feys, and S. F. De Meyer ADAMTS13's tail tale Blood, May 21, 2009; 113(21): 5039 - 5040. [Full Text] [PDF]

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