Binding of apoA-IV-phospholipid complexes to plasma membranes of rat liver Academic Article Article uri icon


MeSH Major

  • Obesity
  • Thinness
  • Weight Gain


  • Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IV-DMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated. Binding equilibrium at 37 degrees C was reached in 30 minutes. Saturation binding experiments and subsequent analysis of the results with Scatchard plots gave results consistent with the presence of a single saturable binding site. DMPC or POPC unilamellar vesicles could not compete with apoA-IV-DMPC for binding; apoA-I-DMPC competed only partially. ApoE-poor HDL effectively competed with apoA-IV-DMPC. The fact that binding could be greatly reduced (greater than 70%) by preincubating the membrane with pronase (18 micrograms/ml), supports the conclusion that a membrane protein is involved in binding. Based on these results, we speculate that the rapid catabolism of apoA-IV in plasma may be mediated by a specific uptake mechanism in the liver. The implications of these results support the hypothesis that apoA-IV is involved in reverse cholesterol transport.

publication date

  • August 29, 1986



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/S0006-291X(86)80088-2

PubMed ID

  • 3767949

Additional Document Info

start page

  • 122

end page

  • 8


  • 139


  • 1