J. Lipid Res.
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A more recent version of this article appeared on July 1, 2004

Papers In Press, published online ahead of print April 21, 2004
J. Lipid Res., doi:10.1194/jlr.M300358-JLR200
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Submitted on August 21, 2003
Revised on February 13, 2004
Accepted on March 31, 2004

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

Thomas J.F. Nieland, Angeliki Chroni, Michael L. Fitzgerald, Zoltan Maliga, Vassilis I. Zannis, Tomas Kirchhausen, and Monty Krieger

Biology, Massachusetts Institute of Technology, Cambridge, MA 02139

Corresponding Author: krieger{at}mit.edu

Scavenger receptor, class B, type I (SR-BI) and ATP binding cassette transporter A1 (ABCA1) are structurally dissimilar cell surface proteins that play key roles in high density lipoprotein (HDL) metabolism. SR-BI is a receptor that binds HDL with high affinity and mediates both selective lipid uptake of cholesteryl esters from lipid-rich HDL to cells and efflux of unesterified cholesterol from cells to HDL. ABCA1 mediates efflux of unesterified cholesterol and phospholipids from cells to lipid-poor apoA-I. The activities of ABCA1 and other ABC 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, 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 BLT’s, 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.


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