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Blood, 15 February 2005, Vol. 105, No. 4, pp. 1540-1545. Prepublished online as a Blood First Edition Paper on October 26, 2004; DOI 10.1182/blood-2004-09-3387. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-09-3387v1 105/4/1540    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 de Laat, B. Articles by de Groot, P. G. Search for Related Content PubMed PubMed Citation Articles by de Laat, B. Articles by de Groot, P. G. Related Collections Hemostasis, Thrombosis, and Vascular Biology Free Research Articles Clinical Trials and Observations Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY IgG antibodies that recognize epitope Gly40-Arg43 in domain I of 2–glycoprotein I cause LAC, and their presence correlates strongly with thrombosis Bas de Laat, Ronald H. W. M. Derksen, Rolf T. Urbanus, and Philip G. de Groot From the Departments of Haematology and Rheumatology and Clinical Immunology, University Medical Centre, Utrecht, the Netherlands. Anti–2–glycoprotein I antibodies are known to have a heterogeneous reactivity against 2–glycoprotein I. We performed this study to characterize the epitope on 2–glycoprotein I to which pathologic anti–2–glycoprotein I antibodies are directed. Plasma samples from 198 patients with various systemic autoimmune diseases were tested for the presence of lupus anticoagulant and anti–2–glycoprotein I immunoglobulin G (IgG) antibodies. The reactivity of the anti–2–glycoprotein I–positive samples was further tested by coating recombinant full-length 2–glycoprotein I and 8 deletion mutants of 2–glycoprotein I onto hydrophilic and hydrophobic enzyme-linked immunosorbent assay (ELISA) plates. Full-length 2–glycoprotein I with point mutations in domain I at positions 8, 40, and 43 were used in inhibition experiments. Fifty-two patients with anti–2–glycoprotein I IgG antibodies could be divided into 2 patterns. Type A antibodies only recognize domain I when coated onto hydrophobic plates; they do not recognize domain I coated onto hydrophilic plates. Type B antibodies have heterogeneous reactivity for all domains. Type A antibodies recognize the epitope around amino acids Gly40-Arg43 and cause lupus anticoagulant activity. In contrast to type B antibodies, those of type A strongly correlated with thrombosis. In conclusion, antibodies directed at domain I (epitope comprising Gly40 and Arg43) have lupus anticoagulant activity and strongly associate with thrombosis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: The cryptic path from epitope to clot: a story of 2 domains? Mark A. Vickers and Mike Greaves Blood 2005 105: 1371-1372. [Full Text] [PDF] This article has been cited by other articles: Z Rotar, B Rozman, P. de Groot, M Sanmarco, Y Shoenfeld, P. Meroni, R Cervera, V Pengo, R Cimaz, T Avcin, et al. Sixth meeting of the European Forum on antiphospholipid antibodies. How to improve the understanding of the antiphospholipid syndrome? Lupus, January 1, 2009; 18(1): 53 - 60. 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Rand Correlation between antiphospholipid antibodies that recognize domain I of {beta}2-glycoprotein I and a reduction in the anticoagulant activity of annexin A5 Blood, February 15, 2007; 109(4): 1490 - 1494. [Abstract] [Full Text] [PDF] B. Giannakopoulos, F. Passam, S. Rahgozar, and S. A. Krilis Current concepts on the pathogenesis of the antiphospholipid syndrome Blood, January 15, 2007; 109(2): 422 - 430. [Abstract] [Full Text] [PDF] J. H. Rand The Antiphospholipid Syndrome Hematology, January 1, 2007; 2007(1): 136 - 142. [Abstract] [Full Text] [PDF] J Swadzba, M Sanak, T Iwaniec, S Dziedzina, and J Musial Valine/Leucine247 polymorphism of {beta}2-glycoprotein I in patients with antiphospholipid syndrome: lack of association with anti-{beta}2-glycoprotein I antibodies Lupus, April 1, 2006; 15(4): 218 - 222. [Abstract] [PDF] B. de Laat, R. H. W. M. Derksen, M. van Lummel, M. T. T. Pennings, and P. G. de Groot Pathogenic anti-beta2-glycoprotein I antibodies recognize domain I of beta2-glycoprotein I only after a conformational change Blood, March 1, 2006; 107(5): 1916 - 1924. [Abstract] [Full Text] [PDF] O. Safa, C. T. Esmon, and N. L. Esmon Inhibition of APC anticoagulant activity on oxidized phospholipid by anti-{beta}2-glycoprotein I monoclonal antibodies Blood, September 1, 2005; 106(5): 1629 - 1635. [Abstract] [Full Text] [PDF]

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