Abstract

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 [(3)H]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.

Highlights

  • Tor family, SR-BI binds multiple ligands with high affinity, including high (HDL), low (LDL), and very low density lipoproteins, oxidized LDL, acetylated LDL, and anionic phospholipids (1, 14 –17)

  • Panels A–C of Fig. 1 shows the amount of [3H]cholesterol associated with the ldlA7-SRBI and the control ldlA7 cells after the cells were incubated with the indicated amounts of radiolabeled HDL or LDL

  • A new observation made in this paper is that SR-BI transferred more free cholesterol than cholesteryl esters to cells from either LDL or HDL

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Summary

Introduction

Tor family, SR-BI binds multiple ligands with high affinity, including high (HDL), low (LDL), and very low density lipoproteins, oxidized LDL, acetylated LDL, and anionic phospholipids (1, 14 –17). Panels A–C of Fig. 1 shows the amount of [3H]cholesterol associated with the ldlA7-SRBI and the control ldlA7 cells after the cells were incubated with the indicated amounts of radiolabeled HDL or LDL.

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