J. Lipid Res.
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A more recent version of this article appeared on June 1, 2006

Papers In Press, published online ahead of print March 13, 2006
J. Lipid Res., doi:10.1194/jlr.M500503-JLR200
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Submitted on November 16, 2005
Revised on March 13, 2006
Accepted on March 13, 2006

Intracellular trafficking of recycling apolipoprotein E in Chinese hamster ovary cells

Nicole A. Braun, Peter J. Mohler, Karl H. Weisgraber, Alyssa H. Hasty, MacRae F. Linton, Patricia G. Yancey, Yan R. Su, Sergio Fazio, and Larry L. Swift

Pathology, Vanderbilt University School of Medicine, Nashville, TN 37232-2561

Corresponding Author: larry.swift{at}vanderbilt.edu

We have investigated apolipoprotein E (apoE) recycling in Chinese hamster ovary (CHO) cells, a peripheral cell that does not produce lipoproteins or express apoE. Using a pulse-chase protocol in which cells were pulsed with 125I-apoE-VLDL and chased for different periods, approximately 30% of the apoE internalized during the pulse was resecreted within a 4 h chase in a relatively lipid-free state. The addition of lysosomotropic agents or brefeldin A had no effect on apoE recycling. Unlike previous results with hepatocytes and macrophages, neither apoAI nor up-regulation of ATP binding cassette protein AI (ABCA1) stimulated apoE recycling. However, cyclodextrin, which extracts cholesterol from plasma membrane lipid rafts, increased recycling. Confocal studies revealed that apoE, internalized during a 1 h pulse, co-localizes with early endosomal antigen-1, Rab5, Rab11a, and lysobisphosphatidic acid, but not with lysosomal-associated membrane protein-1. Co-localization of apoE and Rab11a persisted even after cells had been chased for 1 h, suggesting a pool of apoE within the endosomal recycling compartment (ERC). Our data suggest that apoE recycling in CHO cells is linked to cellular cholesterol removal via the ERC and phospholipid-containing acceptors in a pathway alternative to the ABCA1-apoAI axis.


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