Factor VIII efficient and specific non-covalent binding to PEGylated liposomes enables prolongation of its circulation time and haemostatic efficacy.

Haemophilia A is a bleeding disorder caused by the lack of factor VIII (FVIII). We report the prolongation of exogenous FVIII circulation time and haemostatic efficacy by its formulation with PEGylated liposomes (PEGLip). FVIII binds non-covalently but with high affinity in a specific mode with the external surface of PEGLip neither losing its activity nor its binding to von Willebrand Factor.

Antigen of erythroblast (Ag-Eb): a membrane protein that may be an erythroid-specific transferrin receptor.

Only a limited number of erythroid cell surface markers have been described in the literature. Ag-Eb was originally described as an erythroid-specific cell surface glycoprotein and could be used as an erythroid differentiation marker, but more recent studies suggest this localization is more widespread. From the data summarized in this review, it is hypothesized that Ag-Eb is a member of a subset of the transferrin receptor family and that it functions together with these receptors in the uptake and metabolism of iron, particularly at histo-hematic barriers.