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Originally published In Press as doi:10.1074/jbc.M200658200 on February 22, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21149-21157, June 14, 2002
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Reconstituted Discoidal ApoE-Phospholipid Particles Are Ligands for the Scavenger Receptor BI
THE AMINO-TERMINAL 1-165 DOMAIN OF ApoE SUFFICES FOR RECEPTOR BINDING*

Xiaoping LiDagger , Horng-Yuan KanDagger , Sophia LavrentiadouDagger , Monty Krieger§, and Vassilis ZannisDagger

From the Dagger  Section of Molecular Genetics, Whitaker Cardiovascular Institute, Departments of Medicine and Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118 and the § Biology Department, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

The high density lipoprotein receptor, scavenger receptor class B type I (SR-BI), recognizes lipid-bound apolipoprotein A-I (apoA-I) and other apolipoproteins. Here, we have used large scale cultures of apoE-expressing cells to purify apoE and prepare apoE containing reconstituted discoidal 1-palmitoyl-2-oleoyl-L-phosphatidylcholine (POPC)-apoE particles. These particles have been used to examine their binding to wild-type and mutant forms of SR-BI expressed in transfected ldlA-7 cells. Specific binding to SR-BI was determined by subtracting from the total binding, nonspecific values measured using either control untransfected ldlA-7 cells or by inhibiting SR-BI-mediated binding with a high titer antireceptor-blocking antibody. POPC-apoE particles generated using apoE2, apoE3, apoE4, or the carboxyl-terminally truncated forms apoE165, apoE202, apoE229, and apoE259 all bound tightly to wild-type SR-BI with similar affinities (Kd = 35-45 µg/ml). Binding was nearly abolished in a cell line expressing the ldlA (Q402R/Q418R) double mutant form of SR-BI that is unable to bind native high density lipoprotein but binds low density lipoprotein normally. The findings establish that apoE is a ligand for SR-BI and that the receptor binding domain is located in the amino-terminal 1-165-region of the protein. SR-BI-apoE interactions may contribute to cholesterol homeostasis in tissues and cells expressing SR-BI that are accessible to apoE-containing lipoproteins.

* This work was supported by National Institutes of Health Grants HL48739 and HL68216 (to V. Z.) and HL41484 and HL52212 (to M. K.) and the Alzheimer's Association Grant IIRG-002220 (to V. Z.).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. Tel.: 617-638-5085; Fax: 617-638-5141; Email: vzannis@bu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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