Dynamic properties of human high density lipoprotein apoproteins

J. Shepherd, J. R. Patsch, C. J. Packard, Antonio Gotto, O. D. Taunton

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


This study was designed to identify a method for the measurement of human high density lipoprotein subfraction (HDL 2 and HDL 3) metabolism. Apolipoproteins A-I, A-II, and C, the major HDL apoproteins, were radioiodinated and incorporated individually into HDL 2 and HDL 3 in vitro. Using a double label technique, the turnover of apoA-I in HDL 2 and HDL 3 was measured simultaneously in a normal male. The apoprotein exchanged rapidly between the two subfractions evidenced by equilibration of their apoA-I specific activity. Radiolabeled apoA-II, incorporated into the subfractions, showed a similar exchange in vitro. Incubation of 131I-labeled very low density lipoproteins (VLDL) with HDL or its subfractions resulted in transfer of C proteins from VLDL to the HDL moiety. The extent of transfer was dependent on the HDL subfraction present; 50% of the VLDL apoC was transferred to HDL 3, while the transfer to total HDL and HDL 2 was 69% and 78%, respectively. ApoC also exchanged between HDL 2 and HDL 3, again showing a preference for the former and suggesting a primary metabolic relationship between VLDL and HDL 2. Overall, the study indicates that apoA-I, apoA-II, and the C proteins exist in equilibrium between HDL 2 and HDL 3. This phenomenon precludes their use as probes for HDL subfraction metabolism in humans.

Original languageEnglish (US)
Pages (from-to)383-389
Number of pages7
JournalJournal of lipid research
Issue number3
StatePublished - 1978

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology


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