Apolipoprotein C-III displacement of apolipoprotein E from VLDL: effect ofparticle size

Citation
Ed. Breyer et al., Apolipoprotein C-III displacement of apolipoprotein E from VLDL: effect ofparticle size, J LIPID RES, 40(10), 1999, pp. 1875-1882
Citations number
45
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF LIPID RESEARCH
ISSN journal
00222275 → ACNP
Volume
40
Issue
10
Year of publication
1999
Pages
1875 - 1882
Database
ISI
SICI code
0022-2275(199910)40:10<1875:ACDOAE>2.0.ZU;2-J
Abstract
ApoC-III and apoE are important determinants of intravascular lipolysis and clearance of triglyceride-rich chylomicrons and VLDL from the blood plasma . Interactions of these two apolipoproteins were studied by adding purified human apoC-III to human plasma at levels observed in hypertriglyceridemic subjects and incubating under specific conditions (2 h, 37 degrees C), As p lasma concentrations of apoC-III protein were increased, the contents in bo th VLDL and HDL were also increased. Addition of apoC-III at concentrations up to four times the intrinsic concentration resulted in the decreasing in cremental binding of apoC-III to VLDL while HDL bound increasing amounts wi thout evidence of saturation. No changes were found in lipid content or in particle size of any lipoprotein in these experiments. However, distributio n of the intrinsic apoE in different lipoprotein particles changed markedly with displacement of apoE from VLDL to HDL, The fraction of VLDL apoE that was displaced from VLDL to HDL at these high apoC-III concentrations varie d among individuals from 20% to 100% its intrinsic level. The proportion of VLDL apoE that was tightly bound (0% to 80%) was found to be reproducible and to correlate with several indices of VLDL particle size. In the group o f subjects studied, strongly adherent apoE was essentially absent from VLDL particles having an average content of less than 50,000 molecules of trigl yceride.jlr Addition of apoC-III to plasma almost completely displaces apoE from small VLDL particles. Larger VLDL contain tightly bound apoE which ar e not displaced by increasing concentration of apoC-III.