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Blood, 1 March 2005, Vol. 105, No. 5, pp. 1964-1969.
Prepublished online as a Blood First Edition Paper on October 7, 2004; DOI 10.1182/blood-2004-05-1708.
 Previous Article | Next Article 
Submitted May 5, 2004
Accepted September 24, 2004
Annexin A2 mediates endothelial cell activation by antiphospholipid/anti- 2-Glycoprotein I antibodies
Jianwei Zhang and Keith R McCrae*
Department of Medicine,Hematology-Oncology Division, Case Western Reserve University School of Medicine, Cleveland, OH, USA
* Corresponding author; email: kxm71{at}po.cwru.edu.
Patients with antiphospholipid antibodies (APLA) are at increased risk for arterial and venous thrombosis. Many APLA associated with these events react with  2-glycoprotein I (2GPI), and endothelial cell reactive antibodies that activate endothelial cells in a 2GPI-dependent manner occur commonly in these patients. We previously reported that 2GPI binds with high affinity to annexin A2 on the endothelial surface, though the relevance of this interaction to APLA/anti-2GPI antibody induced endothelial activation has not been determined. In this report, we confirm that anti-2GPI antibodies activate endothelial cells in the presence of 2GPI, 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, while 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-2GPI antibodies in the presence of 2GPI. These observations suggest a novel pathway for endothelial activation induced by APLA/anti-2GPI antibodies that is initiated by cross-linking or clustering of annexin II on the endothelial surface.
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