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

Papers In Press, published online ahead of print June 21, 2004
J. Lipid Res., doi:10.1194/jlr.M400026-JLR200
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Submitted on January 23, 2004
Revised on April 19, 2004
Accepted on June 10, 2004

Remodeling of HDL remnants generated by scavenger receptor class B type I

Nancy R. Webb, Maria C. de Beer, Bela F. Asztalos, Nathan Whitaker, Deneys R. van der Westhuyzen, and Frederick C. de Beer

Internal Medicine, University of Kentucky, Lexington, KY 40536-0200

Corresponding Author: nrwebb1{at}uky.edu

SR-BI mediates the selective transfer of cholesteryl ester from HDL to cells. We previously established that SR-BI overexpressed in livers of apoA-I-deficient mice processes exogenous human HDL2 to incrementally smaller HDL particles. When mixed with normal mouse plasma either in vivo or ex vivo, SR-BI-generated HDL "remnants" rapidly remodel to form HDL-sized lipoproteins. In this study, we analyzed HDLs throughout the process of remnant formation and investigated the mechanism of conversion to larger particles. Upon interacting with SR-BI, alpha-migrating HDL2 is initially converted to a pre-alpha-migrating particle that is ultimately processed to a smaller alpha-migrating remnant. SR-BI does not appear to generate pre-beta-1 HDL particles. When incubated with isolated lipoprotein fractions, HDL remnants are converted to lipoprotein particles corresponding in size to the particle incubated with the remnant. Remnant conversion is not altered in phospholipid transfer protein (PLTP)-deficient mouse plasma or by the addition of purified PLTP. Although lecithin:cholesterol acyltransferase (LCAT)-deficient plasma promoted only partial conversion, this deficiency was due to the nature of HDL particles in LCAT-/- mice rather than a requirement for LCAT in the remodeling process. We conclude that HDL remnants, generated by SR-BI, are converted to larger particles by rapidly re-associating with existing HDL particles in an enzyme-independent manner.


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