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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M300358-JLR200 on April 21, 2004

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Journal of Lipid Research, Vol. 45, 1256-1265, July 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology

Cross-inhibition of SR-BI- and ABCA1-mediated cholesterol transport by the small molecules BLT-4 and glyburide

Thomas J. F. Nieland*,{dagger},§, Angeliki Chroni**, Michael L. Fitzgerald{dagger}{dagger}, Zoltan Maliga{dagger},§, Vassilis I. Zannis**, Tomas Kirchhausen{dagger} and Monty Krieger1,*

* Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139
{dagger} Department of Cell Biology, Harvard Medical School, and The CBR Institute for Biomedical Research, Inc., Boston, MA 02115-5701
** Molecular Genetics, Whitaker Cardiovascular Institute, Department of Medicine and Biochemistry, Boston University School of Medicine, Boston, MA 02118
{dagger}{dagger} Lipid Metabolism Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114
§ Harvard Institute for Chemistry and Cell Biology, Seeley G. Mudd 604, Boston, MA 02115

1 To whom correspondence should be addressed. e-mail: krieger{at}mit.edu

Scavenger receptor class B type I (SR-BI) and ABCA1 are structurally dissimilar cell surface proteins that play key roles in HDL metabolism. SR-BI is a receptor that binds HDL with high affinity and mediates both the selective lipid uptake of cholesteryl esters from lipid-rich HDL to cells and the efflux of unesterified cholesterol from cells to HDL. ABCA1 mediates the efflux of unesterified cholesterol and phospholipids from cells to lipid-poor apolipoprotein A-I (apoA-I). The activities of ABCA1 and other ATP binding cassette superfamily members are inhibited by the drug glyburide, and SR-BI-mediated lipid transport is blocked by small molecule inhibitors called BLTs . Here, we show that one BLT, [1-(2-methoxy-phenyl)-3-naphthalen-2-yl-urea] (BLT-4), blocked ABCA1-mediated cholesterol efflux to lipid-poor apoA-I at a potency similar to that for its inhibition of SR-BI (IC50 ~ 55–60 µM). Reciprocally, glyburide blocked SR-BI-mediated selective lipid uptake and efflux at a potency similar to that for its inhibition of ABCA1 (IC50 ~275–300 µM). As is the case with BLTs, glyburide increased the apparent affinity of HDL binding to SR-BI.

The reciprocal inhibition of SR-BI and ABCA1 by BLT-4 and glyburide raises the possibility that these proteins may share similar or common steps in their mechanisms of lipid transport.

Abbreviations: ABC, ATP binding cassette; apoA-I, apolipoprotein A-I; BLT, small molecules that block lipid transport; COE, cholesteryl oleyl ether; DSP, dithiobis (succinimidyl propionate); Kd, dissociation constant; SR-BI, scavenger receptor class B type I; SUR, sulfonylurea receptor

Supplementary key words scavenger receptor class B type I • ATP binding cassette transporter A1 • blockers of lipid transport


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