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The Phosphatidylserine–β2-Glycoprotein I complex is formed when β2GPI binds to phosphatidylserine exposed on the surface of apoptotic or activated cells. This complex exposes new antigenic epitopes, making it a target for autoantibodies in patients with antiphospholipid syndrome (APS). The presence of such antibodies has major clinical implications, as it leads to inappropriate activation of coagulation and complement systems, thereby increasing the risk of thrombosis and pregnancy complications. β2GPI itself is a highly versatile plasma protein that regulates immune homeostasis and hemostasis and can undergo structural transitions upon binding to anionic phospholipids like phosphatidylserine. The PS–β2GPI complex is a critical target for both diagnosis and potential therapeutic intervention in APS, and its immune recognition significantly contributes to the pathogenesis of thrombosis and inflammation seen in these patients.
Reduction of autoantibody binding to the complex; Suppression of the immune response against β2GPI; Inhibition of downstream coagulation or complement pathways activated by the complex
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