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. 2006 Apr;26(4):891-6.
doi: 10.1161/01.ATV.0000203512.01007.3d. Epub 2006 Jan 12.

Lipoprotein lipase bound to apolipoprotein B lipoproteins accelerates clearance of postprandial lipoproteins in humans

Chunyu Zheng  1 , Susan J Murdoch, John D Brunzell, Frank M Sacks
Affiliations

Lipoprotein lipase bound to apolipoprotein B lipoproteins accelerates clearance of postprandial lipoproteins in humans

Chunyu Zheng et al. Arterioscler Thromb Vasc Biol. 2006 Apr.

Abstract

Objective: Experiments in cells and animal models show that lipoprotein lipase (LpL) bound to apolipoprotein (apo)B lipoproteins enhances their uptake by receptor mediated pathways. It is unknown whether this pathway is important in humans.

Methods and results: ApoB lipoproteins with LpL were isolated from normal subjects after oral fat loading by immunoaffinity chromatography and were further separated into apoB100 and apoB48 lipoproteins. Postprandially, apoB lipoproteins with LpL had significantly greater increases (4- to 10-fold) and faster rates of clearance (5- to 8-fold) percentage-wise than those without LpL. apoB lipoproteins with LpL had enhanced clearance regardless of whether they also contained apoE. LpL was particularly important for the clearance of apoB48 lipoproteins, of which 25% (range, 11% to 31%) could be removed from circulation together with LpL during the postprandial state. apoB lipoproteins with LpL were larger in size and were enriched in triglyceride, cholesterol, and apoE compared with those without LpL. However, neither size nor apoE content explained the faster clearance rates of LpL-containing lipoproteins.

Conclusions: Plasma LpL may act like an apolipoprotein to enhance the clearance of apoB lipoproteins in humans, a mechanism particularly important for intestinal lipoproteins in the postprandial state.

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Figures

Figure 1
Figure 1
Particle size distribution. Diameters of lipoproteins were measured from electron microscopy in the following LpL+ and LpL− fractions: total apoB, light VLDL, dense VLDL and IDL. 100 lipoprotein particles were selected randomly for each fraction from each of 2 subjects.
Figure 2
Figure 2
Postprandial response of apoB and triglyceride. LpL+ and LpL− fractions were obtained from anti-LpL chromatography, and were further separated into TRL and LDL. Dual Y-axes are used: left-side axes correspond to values of LpL+; right-side axes correspond to LpL−. Data points represent mean±SEM of 9 subjects.
Figure 3
Figure 3
Postprandial response of apoB48 containing and apoB100 containing lipoproteins with LpL or without LpL. Plasma was fractionated first by anti-LpL immuno-affinity chromatography into LpL+ and LpL−, and was further fractionated by anti-apoB100 and ultracentrifugation into apoB100 and apoB48. Data points represent mean±SEM of 9 subjects.
Figure 4
Figure 4
Postprandial response of LpL+ fractions and LpL− light VLDL (A) apoB in LpL+ TRL and LpL− light VLDL (Sf>60); (B) apoB in LpL+ LDL and LpL− light VLDL; (C) apoB48 in LpL+ apoB lipoproteins and LpL− light VLDL; (D) apoB100 in LpL+ apoB lipoproteins and LpL− light VLDL.
Figure 5
Figure 5
Postprandial response of TRL according to contents of LpL and apoE. Plasma was fractionated first by anti-LpL immuno-affinity chromatography into LpL+ and LpL- fractions, and was further fractionated by anti-apoE immuno-affinity chromatography into apoE+ and apoE−. TRL was prepared by ultracentrifugation.
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