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Papers In Press, published online ahead of print January 16, 2004
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Department of Internal Medicine, University of Kentucky, Lexington, KY 40536
Corresponding Author: dvwest1{at}uky.edu
The class B scavenger receptors SR-BI and CD36 exhibit a broad ligand binding specificity. SR-BI is well characterized as a HDL receptor that mediates selective cholesteryl ester uptake from HDL. CD36, a receptor for oxidized LDL, also binds HDL and mediates selective cholesteryl ester uptake although much less efficiently than SR-BI. Apolipoprotein A-II (apoA-II), the second most abundant HDL protein, is considered to be pro-atherogenic but the underlying mechanisms are unclear. We previously showed that apolipoprotein A-II modulates SR-BI-dependent binding and selective uptake of cholesteryl ester from reconstituted HDL. To investigate the effect of apoA-II in naturally occurring HDL on these processes, we compared HDL without apoA-II (from apoA-II null mice) to HDLs containing differing amounts of apoA-II (from C57BL/6 mice and transgenic mice expressing a mouse apoA-II transgene). The level of apoA-II in HDL was inversely correlated with HDL binding and selective cholesteryl ester uptake by both scavenger receptors, particularly CD36. Interestingly, for HDL lacking apoA-II the efficiency with which CD36 mediated selective uptake reached a similar level to that of SR-BI. These results demonstrate that apoA-II exerts a marked effect on HDL binding and selective lipid uptake by the class B scavenger receptors and establishes a potentially important relationship between apoA-II and CD36.
Revised on December 24, 2003
Accepted on January 14, 2004
ApoA-II modulates the association of HDL with class B scavenger receptors SR-BI and CD36
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