My contribution, my dream – a look at the future of APS

We found, in 1994, that the epitope for anticardiolipin antibodies (aCL) developed when β2-glycoprotein I (β2GPI) was adsorbed on polyoxygenated polystyrene plates. We also found, in 2009, that the cleaved form of β2GPI (nicked β2GPI) was bound to angiostatin 4.5 and attenuated its antiangiogenic property. We described in 2000 that antiprothrombin antibodies were bound to prothrombin exposed to immobilized phosphatidylserine (aPS/PT) and more than 95% of antiphospholipid syndrome patients who were positive for aPS/PT had lupus anticoagulant. We demonstrated that in the cells stimulated by human monoclonal anti-β2GPI antibodies, p38 mitogen-activated protein kinase phosphorylation was observed in the presence of β2GPI. Furthermore, we found that complement activation was essential for thrombus formation in patients with the antiphospholipid syndrome in vivo.