Identification of the proteoglycan binding site in apolipoprotein B48.

@article{Flood2002IdentificationOT,
  title={Identification of the proteoglycan binding site in apolipoprotein B48.},
  author={Christofer Flood and Maria Gustafsson and Paul E. Richardson and Stephen C. Harvey and Jere P. Segrest and Jan Bor{\'e}n},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 35},
  pages={32228-33}
}
An initial event in atherosclerosis is the retention of lipoproteins within the intima of the vessel wall. Previously we identified Site B (residues 3359-3369) in apolipoprotein (apo) B100 as the proteoglycan binding sequence in low density lipoproteins (LDLs) and showed that the atherogenicity of apoB-containing lipoproteins is linked to their affinity for artery wall proteoglycans. However, both apoB100- and apoB48-containing lipoproteins are equally atherogenic even though Site B lies in the… CONTINUE READING

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