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J Biol Chem, Vol. 274, Issue 46, 32692-32698, November 12, 1999
From the Departments of Internal Medicine and Molecular Genetics,
University of Texas Southwestern Medical Center,
Dallas, Texas 75235
The scavenger receptor-BI (SR-BI) delivers
sterols from circulating lipoproteins to tissues, but the relative
potency of individual lipoproteins and the transported cholesterol has
not been studied in detail. In this study, we used Chinese hamster
ovary cells that express recombinant mouse SR-BI but have no functional
low density lipoprotein (LDL) receptors (ldlA7-SRBI cells) to compare the fate of lipids transferred from high or low density lipoproteins to
cells by SR-BI. HDL and LDL were equally effective in mediating the
transfer of [3H]cholesterol to cells. Only 5% of
the free cholesterol transferred to cells was esterified, in direct
contrast to the findings in the cells that express LDL receptors in
which 50% of the transported cholesterol was esterified. Almost all
the free cholesterol transferred from lipoproteins to cells was rapidly
excreted when the ldlA7-SRBI cells were switched to media containing
unlabeled lipoproteins. SR-BI expression was associated with an
increase in selective cholesteryl ester uptake from both lipoproteins,
but HDL was a more effective donor. HDL and LDL were equally effective
in delivering cholesterol to the intracellular regulatory pool via
SR-BI. These data indicate that SR-BI is able to exchange cholesterol
rapidly between lipoproteins and cell membranes and can mediate the
uptake of cholesteryl esters from both classes of lipoproteins.
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