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• W2072477029 startingPage "1964" @default.
• W2072477029 abstract "Abstract Patients with antiphospholipid antibodies (APLAs) are at increased risk for arterial and venous thrombosis. Many APLAs associated with these events react with β2 glycoprotein I (β2GPI), and endothelial cell reactive antibodies that activate endothelial cells in a β2GPI-dependent manner occur commonly in these patients. We previously reported that β2GPI binds with high affinity to annexin A2 on the endothelial surface, though the relevance of this interaction to APLA/anti-β2GPI antibody–induced endothelial activation has not been determined. In this report, we confirm that anti-β2GPI antibodies activate endothelial cells in the presence of β2GPI, and demonstrate that anti–annexin A2 antibodies directly cause endothelial cell activation of a similar magnitude and with a similar time course. Moreover, bivalent anti–annexin A2 F(ab′)2 fragments also caused endothelial cell activation, whereas monomeric Fab fragments not only did not cause activation, but blocked activation induced by anti–annexin A2 antibodies and F(ab′)2 fragments, as well as that caused by anti-β2GPI antibodies in the presence of β2GPI. These observations suggest a novel pathway for endothelial activation induced by APLA/anti-β2GPI antibodies that is initiated by cross-linking or clustering of annexin A2 on the endothelial surface." @default.
• W2072477029 created "2016-06-24" @default.
• W2072477029 creator A5006247366 @default.
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• W2072477029 date "2005-03-01" @default.
• W2072477029 modified "2023-10-17" @default.
• W2072477029 title "Annexin A2 mediates endothelial cell activation by antiphospholipid/anti-β2 glycoprotein I antibodies" @default.
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• W2072477029 doi "https://doi.org/10.1182/blood-2004-05-1708" @default.
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