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Human apolipoprotein H (apoH, also designated b2-glycoprotein I, activated protein C binding protein or APC inhibitor) is a five-domain plasma membrane-adhesion protein that is rich in sialic acid linked a to galactose or N-acetylgal-actosamine. apoH has been implicated in a variety of physiological pathways, including blood coagulation and the immune response. apoH is a cofactor for the binding of serum auto-antibodies from antiphospholipid syndrome, and is correlated with thrombosis, lupus erythematosus and recurrent fetal loss. In addition, apoH is also implicated in the clearance of apoptotic bodies from the circulation. The apoH gene is located on human chromosome 17q24.2. apoH is synthesized by hepatocytes and is present in blood associated with plasma lipoproteins. apoH displays a genetically determined structural polymorphism including three alleles (apoH*1, apoH*2 and apoH*3). apoH can inhibit the translocation of cholesterol from extracellular pools to macrophages, which reduces the cellular accumulation of cholesterol, suggesting that apoH may play an important role in the prevention of atherosclerosis.
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