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Prepublished online as a Blood First Edition Paper on June 21, 2002; DOI 10.1182/blood-2002-03-0770. This Article Full Text (PDF) All Versions of this Article: 2002-03-0770v1 100/8/2832    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 Pimanda, J. E Articles by Hogg, P. J Search for Related Content PubMed PubMed Citation Articles by Pimanda, J. E Articles by Hogg, P. J Social Bookmarking                   What's this? Submitted March 14, 2002 Accepted June 7, 2002 The von Willebrand factor-reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiolat position 974 John E Pimanda, Douglas S Annis, Mark Raftery, Deane F Mosher, Colin N Chesterman, and Philip J Hogg* Centre for Thrombosis and Vascular Research, University of New South Wales School of Medical Sciences, Sydney, NSW, Australia; Department of Haematology, Prince of Wales Hospital, Sydney, NSW, Australia Section of Hematology, University of Wisconsin Department of Medicine, Madison, WI, USA Cytokine Research Unit, University of New South Wales School of Medical Sciences, Sydney, NSW, Australia Department of Haematology, Prince of Wales Hospital, Sydney, NSW, Australia; Centre for Thrombosis and Vascular Research, University of New South Wales School of Medical Sciences, Sydney, NSW, Australia * Corresponding author; email: p.hogg{at}unsw.edu.au. Plasma von Willebrand factor (vWF) is a multimeric protein that mediates adhesion of platelets to sites of vascular injury, however only the very large vWF multimers are effective in promoting platelet adhesion in flowing blood. The multimeric size of vWF can be controlled by the glycoprotein, thrombospondin-1 (TSP-1), which facilitates reduction of the disulfide bonds that hold vWF multimers together. The thrombospondin family of extracellular glycoproteins consist of five members in vertebrates, TSP-1-4 and TSP5/COMP. TSP-1 and TSP-2 are structurally similar trimeric proteins composed of disulfide-linked 150-kDa monomers. Recombinant pieces of TSP-1 and TSP-2 incorporating combinations of domains that span the entire subunit were produced in insect cells and examined for vWF reductase activity. vWF reductase activity was present in the Ca2+-binding repeats and C-terminal sequence of TSP-1, but not of TSP-2. Alkylation of Cys974 in the C-terminal TSP-1 construct, which is a Ser in TSP-2, ablated vWF reductase activity. These results imply that the reductase function of TSP-1 centers around Cys974 in the C-terminal sequence. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Ahamed, H. H. Versteeg, M. Kerver, V. M. Chen, B. M. Mueller, P. J. Hogg, and W. Ruf Disulfide isomerization switches tissue factor from coagulation to cell signaling PNAS, September 19, 2006; 103(38): 13932 - 13937. [Abstract] [Full Text] [PDF] J. I. Zwicker, F. Peyvandi, R. Palla, R. Lombardi, M. T. Canciani, A. Cairo, D. Ardissino, L. Bernardinelli, K. A. Bauer, J. Lawler, et al. The thrombospondin-1 N700S polymorphism is associated with early myocardial infarction without altering von Willebrand factor multimer size Blood, August 15, 2006; 108(4): 1280 - 1283. [Abstract] [Full Text] [PDF] S. Glerup, H. B. Boldt, M. T. Overgaard, L. 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