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Blood, 15 October 2003, Vol. 102, No. 8, pp. 2901-2909. Prepublished online as a Blood First Edition Paper on June 26, 2003; DOI 10.1182/blood-2002-12-3702. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-12-3702v1 102/8/2901    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 Boilard, E. Articles by Surette, M. E. Search for Related Content PubMed PubMed Citation Articles by Boilard, E. Articles by Surette, M. E. Related Collections Apoptosis Cytoskeleton Immunobiology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Identification of an autoantigen on the surface of apoptotic human T cells as a new protein interacting with inflammatory group IIA phospholipase A2 Eric Boilard, Sylvain G. Bourgoin, Chantale Bernatchez, and Marc E. Surette From the Centre de Recherche en Rhumatologie et Immunologie, Centre de Recherche du Centre Hospitalier Universitaire de Québec, Pavillon Centre Hospitalier de l'Université Laval (CHUL) and Faculté de Médecine, Université Laval, QC, Canada; and Pilot Therapeutics, Charleston, SC. One of the most studied secreted phospholipases A2 (sPLA2), the group IIA sPLA2, is found at high levels in inflammatory fluids of patients with autoimmune diseases. A characteristic of group IIA sPLA2 is its preference for negatively charged phospholipids, which become exposed on the extracellular leaflet of apoptotic cell membranes. We recently showed that low molecular weight heparan sulfate proteoglycans (HSPGs) and uncharacterized detergent-insoluble binding site(s) contribute to the enhanced binding of human group IIA PLA2 (hGIIA) to apoptotic human T cells. Using matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry we now identify vimentin as the major HSPG-independent binding protein of hGIIA on apoptotic primary T lymphocytes. Vimentin is partially exposed on the surface of apoptotic T cells and binds hGIIA via its rod domain in a calcium-independent manner. Studies with hGIIA mutants showed that specific motifs in the interfacial binding surface are involved in the interaction with vimentin. The sPLA2 inhibitor LY311727, but not heparin, inhibited this interaction. In contrast, heparin but not LY311727 abrogated the binding of hGIIA to cellular HSPGs. Importantly, vimentin does not inhibit the catalytic activity of hGIIA. Altogether, the results show that vimentin, in conjunction with HSPGs, contributes to the enhanced binding of hGIIA to apoptotic T cells. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. A. Hill, D. A. Bell, W. Brintnell, D. Yue, B. Wehrli, A. M. Jevnikar, D. M. Lee, W. Hueber, W. H. Robinson, and E. Cairns Arthritis induced by posttranslationally modified (citrullinated) fibrinogen in DR4-IE transgenic mice J. Exp. Med., April 14, 2008; 205(4): 967 - 979. [Abstract] [Full Text] [PDF] A. Lanemo Myhrinder, E. Hellqvist, E. Sidorova, A. Soderberg, H. Baxendale, C. Dahle, K. Willander, G. Tobin, E. Backman, O. Soderberg, et al. 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Griffioen Gene expression of tumor angiogenesis dissected: specific targeting of colon cancer angiogenic vasculature Blood, October 1, 2006; 108(7): 2339 - 2348. [Abstract] [Full Text] [PDF] P.-L. Wu, S.-C. Lee, C.-C. Chuang, S. Mori, N. Akakura, W.-g. Wu, and Y. Takada Non-cytotoxic Cobra Cardiotoxin A5 Binds to {alpha}vbeta3 Integrin and Inhibits Bone Resorption: IDENTIFICATION OF CARDIOTOXINS AS NON-RGD INTEGRIN-BINDING PROTEINS OF THE Ly-6 FAMILY J. Biol. Chem., March 24, 2006; 281(12): 7937 - 7945. [Abstract] [Full Text] [PDF] E. Moisan and D. Girard Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis J. Leukoc. Biol., March 1, 2006; 79(3): 489 - 498. [Abstract] [Full Text] [PDF]

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