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Originally published In Press as doi:10.1074/jbc.M100228200 on February 9, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15832-15839, May 11, 2001
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Apolipoprotein A-II Modulates the Binding and Selective Lipid Uptake of Reconstituted High Density Lipoprotein by Scavenger Receptor BI*

Maria C. de BeerDagger , Diane M. Durbin§, Lei CaiDagger , Nichole Mirocha§, Ana Jonas§, Nancy R. WebbDagger , Frederick C. de BeerDagger , and Deneys R. van der WesthuyzenDagger

From the Dagger  Department of Internal Medicine, University of Kentucky Medical Center, Lexington, Kentucky 40536, the Department of Veterans Affair Medical Center, Lexington, Kentucky 40511, and the § Department of Biochemistry, College of Medicine at Urbana-Champaign, University of Illinois, Urbana, Illinois 61801

High density lipoprotein (HDL) represents a mixture of particles containing either apoA-I and apoA-II (LpA-I/A-II) or apoA-I without apoA-II (LpA-I). Differences in the function and metabolism of LpA-I and LpA-I/A-II have been reported, and studies in transgenic mice have suggested that apoA-II is pro-atherogenic in contrast to anti-atherogenic apoA-I. The molecular basis for these observations is unclear. The scavenger receptor BI (SR-BI) is an HDL receptor that plays a key role in HDL metabolism. In this study we investigated the abilities of apoA-I and apoA-II to mediate SR-BI-specific binding and selective uptake of cholesterol ester using reconstituted HDLs (rHDLs) that were homogeneous in size and apolipoprotein content. Particles were labeled in the protein (with 125I) and in the lipid (with [3H]cholesterol ether) components and SR-BI-specific events were analyzed in SR-BI-transfected Chinese hamster ovary cells. At 1 µg/ml apolipoprotein, SR-BI-mediated cell association of palmitoyloleoylphosphatidylcholine-containing AI-rHDL was significantly greater (3-fold) than that of AI/AII-rHDL, with a lower Kd and a higher Bmax for AI-rHDL as compared with AI/AII-rHDL. Unexpectedly, selective cholesterol ester uptake from AI/AII-rHDL was not compromised compared with AI-rHDL, despite decreased binding. The efficiency of selective cholesterol ester uptake in terms of SR-BI-associated rHDL was 4-5-fold greater for AI/AII-rHDL than AI-rHDL. These results are consistent with a two-step mechanism in which SR-BI binds ligand and then mediates selective cholesterol ester uptake with an efficiency dependent on the composition of the ligand. ApoA-II decreases binding but increases selective uptake. These findings show that apoA-II can exert a significant influence on selective cholesterol ester uptake by SR-BI and may consequently influence the metabolism and function of HDL, as well as the pathway of reverse cholesterol transport.

* This work was supported by National Institutes of Health Grants HL-59376 and HL-63763 (to D. R. vd W.) and HL-16059 (to A. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Internal Medicine, University of Kentucky Medical Center MN520, 800 Rose St., Lexington, KY 40536. Tel: 859-233-4511 (Ext. 4580); Fax: 859-323-5707; E-mail: dvwest1@pop.uky.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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