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Some antiphospholipid antibodies bind to hemostasis and fibrinolysis proteases and promote thrombosis

Department of Medicine, Division of Rheumatology, University of California at Los Angeles, Los Angeles, CA pochen{at}mednet.ucla.edu

CD Yang

Division of Rheumatology, Ren Ji hospital, Jiaotong University, Shanghai, China

K Ede

Department of Medicine, Division of Rheumatology, University of California at Los Angeles, Los Angeles, CA

CC Wu

Department of Medicine, Division of Rheumatology, University of California at Los Angeles, Los Angeles, CA

JD FitzGerald

Department of Medicine, Division of Rheumatology, University of California at Los Angeles, Los Angeles, CA

JM Grossman

Department of Medicine, Division of Rheumatology, University of California at Los Angeles, Los Angeles, CA

It is generally accepted that the major autoantigen for antiphospholipid antibodies (aPL) is β₂glycoprotein I (β₂GPI). Interestingly, some aPL bind to β₂GPI and the homologous enzymatic domains of several proteases involved in hemostasis and fibrinolysis, and correspondingly hinder anticoagulant regulation and resolution of clots. These findings are consistent with several early findings of aPL and provide a new perspective about some aPL in terms of their binding specificities and related functional properties in promoting thrombosis. In addition, homologous enzymatic domains of the involved proteases share conformation epitope(s) with β₂GPI, thus providing a possible structural basis for some non-mutually exclusive mechanisms of aPL-mediated thrombosis.

Key Words: Antiphospholipid antibodies • coagulation • fibrinolysis • serine protease

Lupus, Vol. 17, No. 10, 916-921 (2008)
DOI: 10.1177/0961203308092805


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