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• W1525426017 startingPage "339" @default.
• W1525426017 abstract "Summary. Recombinant coagulation factor VIIa (rFVIIa), which is widely used for treatment of bleeding episodes in haemophilia patients with inhibitors, is cleared from the circulation relatively fast with a plasma half-life of 2–4 h. PEGylation is an established and clinically proven strategy for prolonging the circulatory life-time of bio-therapeutic proteins. The aim of this study was to investigate the effect of glycoPEGylation of rFVIIa on rFVIIa binding to its cellular receptors and its subsequent internalization. rFVIIa and glycoPEGylated rFVIIa were labeled with 125I and the radio-iodinated proteins were used to monitor rFVIIa binding and uptake in endothelial cells and fibroblasts. FVIIa-TF activity at the cell surface was analyzed by a factor X activation assay. Modification of rFVIIa with PEG impaired rFVIIa binding to both endothelial cell protein C receptor and tissue factor (TF) on cell surfaces. The internalization of PEGylated rFVIIa in endothelial cells and fibroblasts was markedly lower compared to the internalization of rFVIIa in these cells. PEGylated rFVIIa was able to activate factor X on TF expressing cell surfaces at a rate similar to that of unmodified rFVIIa when the cells were not subjected to multiple washings to remove the free ligand. General effects such as steric hindrance or changes in electrostatic binding properties of the modified rFVIIa to its receptors are probably responsible for this impairment rather than a loss of specific recognition of the receptors, which could explain near normal activation of factor X by glycoPEGylated rFVIIa on TF expressing cells while its uptake is reduced." @default.
• W1525426017 created "2016-06-24" @default.
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• W1525426017 date "2009-10-21" @default.
• W1525426017 modified "2023-10-18" @default.
• W1525426017 title "Effect of glycoPEGylation on factor VIIa binding and internalization" @default.
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• W1525426017 doi "https://doi.org/10.1111/j.1365-2516.2009.02121.x" @default.
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