Binding of apoA-IV-phospholipid complexes to plasma membranes of rat liver

Giancarlo Ghiselli, William L. Crump, Antonio Gotto

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Rat apoA-IV complexes with dimyristoyl phosphatidylcholine (apoA-IVDMPC) have been prepared and their ability to bind to purified rat liver plasma membranes investigated. Binding equilibrium at 37°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 (> 70%) by preincubating the membrane with pronase (18 μg/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.

Original languageEnglish (US)
Pages (from-to)122-128
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume139
Issue number1
DOIs
StatePublished - Aug 29 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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