Net transfer of phosphatidylcholine from plasma low density lipoproteins to sphingomyelin-apolipoprotein A-II complexes by bovine liver and human plasma phospholipid exchange proteins

David B. Wilson, Jeff L. Ellsworth, Richard L. Jackson

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Bovine liver phosphatidylcholine exchange protein facilitated the net transfer of dipalmitoyl phosphatidyl[N-methyl-14C]cholme from radiolabeled low density lipoproteins (LDL) to complexes of sphingomyelin and apolipoprotein A-II. Transfer of the radiolabeled phosphatidylcholine was dependent on temperature and incubation time, as well as the ratio of LDL to sphingomyelinapolipoprotein A-II. When unlabeled LDL was incubated with sphingomyelinapolipoprotein A-II complex containing [N-methyl-14C]sphingomyelin, negligible amounts of the radiolabel were transferred to the LDL, implying that the transfer of phosphatidylcholine to the sphingomyelin-apolipoprotein A-II complex was not coupled with a return of sphingomyelin to the LDL. Bovine liver phosphatidylcholine exchange protein also facilitated the net transfer of dipalmitoyl phosphatidyl[N-methyl-14C]choline from sonicated vesicles of 1-palmitoyl-2-palmitoleoyl phosphatidylcholine to sphingomyelin-apolipoprotein A-II complex. Dansyl phosphatidylethanolamine incorporated in the donor vesicles was not transferred to the sphingomyelin-apolipoprotein A-II complex, indicating that phospholipid transfer was not due to a disruption of the vesicles and subsequent fusion of vesicle remnants with the sphingomyelin-apolipoprotein A-II complex. Bovine liver phosphatidylcholine exchange protein did not transfer dipalmitoyl phosphatidyl[N-methyl-14C]choline or [3H]cholesteryl esters from high density lipoproteins (HDL) to sonicated vesicles of sphingomyelin. Fluorescence polarization studies showed that relative to the sphingomyelin-apolipoprotein A-II complexes, the sphingomyelin vesicles have a rigid structure which may account for this lack of transfer of the phosphatidyl[14C]choline. Phospholipid exchange protein(s) isolated from human plasma also facilitated the net transfer of dipalmitoyl phosphatidyl[14C]choline from LDL to sphingomyelin-apolipoprotein A-II complexes.

Original languageEnglish
Pages (from-to)550-561
Number of pages12
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume620
Issue number3
DOIs
StatePublished - Dec 5 1980

Keywords

  • Apolipoprotein A-II
  • LDL
  • Phosphatidylcholine transfer
  • Phospholipid exchange protein
  • Sphingomyelin

Fingerprint

Dive into the research topics of 'Net transfer of phosphatidylcholine from plasma low density lipoproteins to sphingomyelin-apolipoprotein A-II complexes by bovine liver and human plasma phospholipid exchange proteins'. Together they form a unique fingerprint.

Cite this