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Receptor-mediated uptake of homologous low-density lipoproteins by isolated liver parenchymal cells of fetal rats

Summary

The binding and uptake of gold-labeled homologous, apolipoprotein E-free low-density lipoproteins (LDL) by isolated fetal rat liver parenchymal cells in suspension were studied ultrastructurally and morphometrically. Binding experiments using 125I-labeled LDL were also performed. After a 2-h preincubation in a lipoprotein-free medium and a subsequent 1-h postincubation in the presence of LDL-gold, fetal liver parenchymal cells exhibit a binding of 248±17 gold conjugates/100 μm plasma membrane and an uptake of 235±17 gold conjugates/100 μm2 cytoplasm. Compared with values obtained from freshly isolated nonpreincubated cells, these data correspond to a 15-fold and an 18-fold increase in total binding and uptake of LDL-gold, respectively. Competition experiments reveal that this increase is mainly a result of a 23-fold stimulation of specific binding and a 44-fold stimulation of receptor-mediated uptake of LDL-gold. The 125I-LDL binding experiments give a Kd value of 6.3×10-8 M and a maximum binding capacity of 17.3 fmol LDL/106 cells. Our data provide evidence, further to our in vivo studies, that fetal rat liver parenchymal cells possess high-affinity binding sites for native homologous apolipoprotein E-free LDL. These sites may correspond to B, E receptors of adult rat liver parenchymal cells.

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Dürer, U., Sommer, M., Franke, H. et al. Receptor-mediated uptake of homologous low-density lipoproteins by isolated liver parenchymal cells of fetal rats. Cell Tissue Res. 254, 203–208 (1988). https://doi.org/10.1007/BF00220035

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  • DOI: https://doi.org/10.1007/BF00220035

Key words

  • Fetal hepatocytes
  • Apo B, E receptors
  • Lipoproteins
  • Endocytosis
  • Rat (Wistar)