n-3, but not n-6 lipid particle uptake requires cell surface anchoring

Biochem Biophys Res Commun. 2010 Feb 5;392(2):135-9. doi: 10.1016/j.bbrc.2009.12.164. Epub 2010 Jan 7.


Omega-3 (n-3) fatty acids are emerging as bioactive agents protective against cardiovascular disease. However, their cellular delivery pathways are poorly defined. Here we questioned whether the uptake of n-3 triglyceride-rich particles (TGRP) is mediated by cell surface proteoglycans (PG) using LDL receptor (LDLR)+/+ and LDLR-/- cell models. LDLR+/+ but not LDLR-/- cells showed higher n-6 over n-3 TGRP uptake. Removal of cell surface proteins and receptors by pronase markedly enhanced the uptake of n-3 but not n-6 TGRP. Lactoferrin blockage of apoE-mediated pathways decreased the uptake of n-6 TGRP by up to 85% (p<0.05) but had insignificant effect on n-3 TGRP uptake. PG removal by sodium chlorate in LDLR+/+ cells substantially reduced n-3 TGRP uptake but had little effect on n-6 TGRP uptake. Thus, while n-6 TGRP uptake is preferentially mediated by LDLR-dependent pathways, the uptake of n-3 TGRP depends more on PG and non-LDLR cell surface anchoring.

MeSH terms

  • Cell Line
  • Cell Membrane / metabolism*
  • Fatty Acids, Omega-3 / metabolism*
  • Fatty Acids, Omega-6 / metabolism*
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Humans
  • Lactoferrin / pharmacology
  • Proteoglycans / metabolism
  • Receptors, LDL / genetics
  • Receptors, LDL / metabolism*
  • Triglycerides / metabolism*
  • alpha-Macroglobulins / pharmacology


  • Fatty Acids, Omega-3
  • Fatty Acids, Omega-6
  • Proteoglycans
  • Receptors, LDL
  • Triglycerides
  • alpha-Macroglobulins
  • Lactoferrin