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Blood. 117(25), 6939-6947. Agar C, de Groot PG, Marquart JA & Meijers JCM. (2011b) Evolutionary conservation of the LPS binding site of beta2-glycoprotein I. Thromb Haemost. In press. Arad A, Proulle V, Furie RA, Furie BC & Furie B. (2011) β₂-Glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model. Blood. 117(12), 3453-3459. Bevers EM & Galli M. (1990) Beta 2-glycoprotein I for binding of anticardiolipin antibodies to cardiolipin.

Electron microscopy analysis of β2GPI. , 2010). Analysis of EM pictures showed that more than 99% of plasma β2GPI was in a closed conformation. These observations suggested that plasma β2GPI circulates in a circular (closed) conformation, whereas after interaction with antibodies β2GPI undergoes a major conformational change into a fishhook-like (open) structure. , 1996). When antibodies toward β2GPI were added to plasma, clotting times prolonged in a β2GPI-dependent way. This effect of anti–β2GPI antibodies is known as lupus anticoagulant (LA) activity.

It is difficult to discriminate whether DR loci contribute to this genetic susceptibility more than DQ loci, because they are in strong linkage disequilibrium. 4. Prothrombotic risk factors in antiphospholipid syndrome Antiphospholipid antibodies (aPL) are related to thrombosis in APS and thromboses are, together with obstetric complications, the main clinical manifestations of APS. Numerous pathophysiological mechanisms have been suggested to explain thrombotic events in APS, in both arterial and venous territories, involving cellular mechanisms, plasma coagulation regulatory proteins, and fibrinolysis.

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