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J. Lipid Res.
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A more recent version of this article appeared on June 1, 2003

Papers In Press, published online ahead of print April 1, 2003
J. Lipid Res., doi:10.1194/jlr.M200429-JLR200
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Submitted on November 4, 2002
Revised on March 24, 2003
Accepted on March 31, 2003

A quantitative analysis of apolipoprotein binding to scavenger receptor class B, type I (SR-BI): Multiple binding sites for lipid-free and lipid-associated apolipoproteins

Stephen T. Thuahnai, Sissel Lund-Katz, G.M. Anantharamaiah, David L. Williams, and Michael C. Phillips

GI/Nutrition, Children's Hospital of Philadelphia, Philadelphia, PA 19104-4318

Corresponding Author: phillipsmi{at}email.chop.edu

Competitive binding experiments were performed using Y1-BS1 adrenal cells to provide information about the interaction of HDL apolipoproteins (apo) with scavenger receptor class B, type 1 (SR-BI). Exchangeable apo A-I, A-II, E-2, E-3 and E-4 as phospholipid complexes bind like HDL3 to SR-BI via their multiple amphipathic alpha-helices; the concentrations required to reduce the binding of HDL3 to SR-BI by 50% (IC50) were similar and in the range 35-50 mg protein/ml. In the case of apo A-I, peptides corresponding to segments 1-85, 44-65, 44-87, 149-243 and 209-241 all had the same IC50 as each other (p=0.86) showing that a specific amino acid sequence in apo A-I is not responsible for the interaction with SR-BI. The distribution of charged residues in the amphipathic alpha-helix affects the interaction, with class A and Y helices binding better than class G* helices. Synthetic alpha-helical peptides composed of either L or D amino acids can bind equally to the receptor. Association with phospholipid increases the amount of apo binding to SR-BI without altering the affinity of binding. Lipid-free apo compete only partially with the binding of HDL to SR-BI whereas lipidated apo compete fully. These results are consistent with the existence of more than one type of apo binding site on SR-BI.


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