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- W2024931792 abstract "The binding of asialofetuin(AF)-labeled liposomes (AF-liposomes) to isolated rat hepatocytes was examined at 4°C. AF-liposomes consisting of phosphatidylcholine, phosphatidic acid (PA) and cholesterol (molar ratio 6: 1: 3) rapidly bound to hepatocytes. A notable contribution of AF was demonstrated by the fact that the binding was inhibited by AF and dissociated by EDTA. An increase in the PA content of AF-liposomes enhanced the extent of their binding, whereas the extent of AF-mediated binding remained the same irrespective of the PA content. There were two classes of binding sites at which AF-liposomes bound to hepatocytes: a high-affinity site with an association constant of 6.45 × 109 M−1 and a low-affinity site with an association constant of 4.50 × 107 M−1, this value being compatible with that of control liposomes. Phosphatidylserine- or phosphatidylglycerol-containing liposomes bound to hepatocytes as did liposomes containing PA. The binding of stearylamine-containing liposomes or liposomes without charged lipid, however, was quite low. Thus, it is evident that AF-liposomes bind to hepatocytes through the high-affinity interaction between AF and asialoglycoprotein receptors and the low-affinity interaction that occurs as a result of liposomal negative charge." @default.
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- W2024931792 date "1991-01-01" @default.
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- W2024931792 title "Characteristics of the binding of asialofetuin-labeled liposomes to isolated rat hepatocytes" @default.
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- W2024931792 doi "https://doi.org/10.1016/0378-5173(91)90424-m" @default.
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