Revisiting beta 2 glycoprotein I, the major autoantigen in the antiphospholipid syndrome

Beta 2 glycoprotein I [beta2GPI] is a single chain 50 kDa highly glycosylated glycoprotein at an approximate concentration of 4 micro M in cells. The abundance of this protein in plasma and its high state of preservation indicate the important role of this protein in mammalian. In addition, beta2GPI has a particular structure in the fifth domain, and is categorized as the major antigen recognized by autoantibodies present in antiphospholipid syndrome. Beta 2 glycoprotein I has been usually studied in the context of antiphospholipid antibody production. Complexes of beta2GPI/anti-beta2GPI antibodies have been examined in different coagulation and cell activation pathways. However, the function of beta2GPI, independent from the antibodies, has not been clearly determined. In this paper different features of beta2GPI including its structure, plasma concentration and its proposed in vitro and in vivo functions in clot formation and fibrinolysis along with anti-beta2GPI antibodies [Abs] are discussed. Their inhibitory or promotive effects are delineated in each facet

[Molecules and signaling pathways in transendothelial migration of leukocytes]

Transendothelial migration of leukocytes [diapedesis], have vital role in both the innate and adaptive immune responses. This process consists of overlapping steps, including: activation of leukocytes, formation of weak adhesions, and translocation along the endothelium followed by stronger adhesions resulting in transmigration of leukocytes. Although the surface molecules used by leukocytes and endothelial cells during diapedesis have been well characterized, the mechanisms by which they regulate this process is poorly understood. In this mini review we introduce some of the involved molecules and mechanisms that play roles in this process