Abstract
In order to investigate the relationship of lipid and apolipoprotein composition to cholesterol esterification in lipoproteins containing apolipoprotein (apo) A-IV, apo A-containing lipoprotein particles were isolated from fresh human plasma using a system of sequential immunoaffinity chromatography. Plasma was first depleted of apo B- and apo E-containing lipoproteins. Four major subpopulations of apo A-containing lipoprotein particles were separated: Lp A-I, Lp A-I : A-II, Lp A-IV and Lp A-I : A-IV : A-II. Lp A-IV and Lp A-I : A-IV : A-II contained less total lipid, less cholesterol and more triacylglycerol than Lp A-I and Lp A-I : A-II. Lp A-IV and Lp A-I : A-IV : A-II contained more sphingomyelin and less phosphatidylcholine than Lp A-I and Lp A-I : A-II and were richer in (16:0 + 18:0) saturated fatty acids. Among these isolated lipoprotein particles, Lp A-IV contained the highest lecithin : cholesterol acyltransferase (LCAT) activity per μg of protein. Cholesterol esterification rates were 2.6 ± 0.5, 5.3 ± 0.4 and 0.8 ± 0.2 μmol of cholesterol per hour per mg of lipoproteins for Lp A-IV, Lp A-I and Lp A-I : A-II, respectively. The apolipoprotein and lipid composition and LCAT activity of Lp A-IV suggest that this lipoprotein may be a source of cholesterol esterification in plasma.
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