SEARCH:   Advanced

Prepublished online as a Blood First Edition Paper on June 21, 2002; DOI 10.1182/blood-2002-03-0770. This Article Full Text 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 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 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. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 October 2002, Vol. 100, No. 8, pp. 2832-2838 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The von Willebrand factor-reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974 John E. Pimanda, Douglas S. Annis, Mark Raftery, Deane F. Mosher, Colin N. Chesterman, and Philip J. Hogg From the Centre for Thrombosis and Vascular Research and Cytokine Research Unit, School of Medical Sciences, University of New South Wales and Department of Haematology, Prince of Wales Hospital, Sydney, Australia; and Section of Hematology, Department of Medicine, University of Wisconsin, Madison. 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 TSP family of extracellular glycoproteins consists of 5 members in vertebrates, TSP-1 through TSP-4 and TSP-5/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 Ca++-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 serine 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. © 2002 by The American Society of Hematology.   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. Sottrup-Jensen, L. C. Giudice, and C. Oxvig Proteinase Inhibition by Proform of Eosinophil Major Basic Protein (pro-MBP) Is a Multistep Process of Intra- and Intermolecular Disulfide Rearrangements J. Biol. Chem., March 18, 2005; 280(11): 9823 - 9832. [Abstract] [Full Text] [PDF] B.-l. A. Hannah, T. M. Misenheimer, M. M. Pranghofer, and D. F. Mosher A Polymorphism in Thrombospondin-1 Associated with Familial Premature Coronary Artery Disease Alters Ca2+ Binding J. Biol. Chem., December 10, 2004; 279(50): 51915 - 51922. [Abstract] [Full Text] [PDF] J. E. Pimanda, T. Ganderton, A. Maekawa, C. L. Yap, J. Lawler, G. Kershaw, C. N. Chesterman, and P. J. Hogg Role of Thrombospondin-1 in Control of von Willebrand Factor Multimer Size in Mice J. Biol. Chem., May 14, 2004; 279(20): 21439 - 21448. [Abstract] [Full Text] [PDF] J. E. Pimanda, A. Maekawa, T. Wind, J. Paxton, C. N. Chesterman, and P. J. Hogg Congenital thrombotic thrombocytopenic purpura in association with a mutation in the second CUB domain of ADAMTS13 Blood, January 15, 2004; 103(2): 627 - 629. [Abstract] [Full Text] [PDF] B.-l. A. Hannah, T. M. Misenheimer, D. S. Annis, and D. F. Mosher A Polymorphism in Thrombospondin-1 Associated with Familial Premature Coronary Heart Disease Causes a Local Change in Conformation of the Ca2+-binding Repeats J. Biol. Chem., March 7, 2003; 278(11): 8929 - 8934. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020