Re-uptake of nascent low-density lipoproteins by HepG2 cells

Biochim Biophys Acta. 1993 Jun 12;1168(2):199-204. doi: 10.1016/0005-2760(93)90125-s.


The kinetics and specificity of the interaction of nascent HepG2 LDL with the HepG2 LDL receptor were examined. 125I-Labeled HepG2 LDL and plasma LDL were bound by HepG2 cells in a specific and saturable manner at 4 degrees C. Competition studies with HepG2 LDL and plasma LDL indicated that both ligands bound to the same receptor. Scatchard analyses of the specific 4 degrees C-binding data revealed a Kd of 75 nM for HepG2 LDL and a Kd of 30 nM for plasma LDL suggesting that HepG2 LDL bind less efficiently to the HepG2 LDL receptor than plasma LDL. Binding, internalization and degradation studies carried out at 37 degrees C indicated that HepG2 cells are capable of catabolizing their own nascent LDL; however, under normal experimental conditions re-uptake of nascent LDL is quantitatively insignificant.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding, Competitive
  • Cell Line / metabolism
  • Humans
  • Iodine Radioisotopes
  • Lipoproteins, LDL / blood
  • Lipoproteins, LDL / isolation & purification
  • Lipoproteins, LDL / metabolism*
  • Particle Size
  • Receptors, LDL / metabolism*


  • Iodine Radioisotopes
  • Lipoproteins, LDL
  • Receptors, LDL