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Papers In Press, published online ahead of print July 1, 2004
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Lipoprotein and Atherosclerosis Group, University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4E9
Corresponding Author: gvass{at}ottawaheart.ca
Previous reports attributed CETP-mediated HDL cholesteryl ester (CE) selective uptake to the CETP-mediated transfer of CE from HDL to newly secreted apolipoprotein B-containing lipoproteins, which are then internalized by the LDL-receptor (LDL-R). CETP has also been implicated in the remodeling of HDL which renders it a better substrate for selective uptake by the scavenger receptor-BI (SR-BI). However, CETP-mediated selective uptake of HDL3-derived CE was not diminished in LDL-R null adipocytes, SR-BI null adipocytes; or in the presence of the receptor-associated protein (RAP). We found that monensin treatment or energy depletion of the SW872 liposarcoma cells with 2-deoxyglucose and NaN3 had no effect on CETP mediated selective uptake, demonstrating that endocytosis is not required. This is supported by data indicating that CETP transfers CE into a compartment where it can be extracted by unlabeled HDL. CETP could also mediate selective uptake of HDL3-derived triacylglycerol and phospholipid. The CETP-specific kinetics for triacylglycerol and CE uptake were similar and both reached saturation at about 5 µg/ml of HDL. In contrast, CETP-specific phospholipid uptake did not attain saturation at 5 µg/ml of HDL and was about 6-fold greater than the uptake of CE. We propose two possible mechanisms to account for the role of CETP in selective uptake.
Revised on June 2, 2004
Accepted on June 18, 2004
Role of cholesteryl ester transfer protein in selective uptake of high density lipoprotein cholesteryl esters by adipocytes
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