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Apolipoprotein E-binding proteins isolated from dog and human liver.

U Beisiegel1, W Weber, J R Havinga

  • 1Medizinische Kernklinik and Poliklinik, Universitätskrankenhaus Eppendorf, Hamburg, Federal Republic of Germany.

Arteriosclerosis (Dallas, Tex.)
|May 1, 1988
PubMed
Summary

Researchers identified new proteins in liver cells that bind to apolipoprotein E (apo E) lipoproteins. These findings expand our understanding of apo E metabolism beyond the known apo B,E(LDL) receptor.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Lipid Metabolism

Background:

  • Chylomicron remnant catabolism is primarily mediated by apolipoprotein E (apo E) binding to hepatic lipoprotein receptors.
  • Previous research identified the apo B,E(LDL) receptor and a unique apo E-binding protein in liver tissue.

Purpose of the Study:

  • To further characterize the apo E-binding fraction isolated from liver.
  • To identify and investigate novel proteins involved in apo E-containing lipoprotein binding.

Main Methods:

  • Ligand blot analysis to assess protein-lipoprotein interactions.
  • Characterization of apo E-binding proteins using techniques like SDS-PAGE and Western blotting.
  • Generation of monoclonal antibodies for protein identification.

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Main Results:

  • The apo E-binding fraction contained at least three proteins with high-affinity binding to apo E lipoproteins.
  • A 56-kDa protein band was identified as subunits of F1-ATPase.
  • A novel 59-kDa apo E-binding protein was identified, exhibiting calcium-dependent and -independent binding properties.
  • The 59-kDa protein recognized various forms of apo E (apo E-2, apo E-3, apo E-4) and both lipid-free and lipid-bound apo E.

Conclusions:

  • Liver cells possess multiple apo E-binding proteins beyond the apo B,E(LDL) receptor.
  • The 56-kDa and 59-kDa proteins are present in normal human liver and in individuals lacking the apo B,E(LDL) receptor.
  • The physiological significance of these newly identified apo E-binding proteins in apo E metabolism requires further investigation.