Selective uptake of HDL cholesterol ester by human fat cells.

In humans, high-density lipoprotein (HDL)-cholesterol ester turnover exceeds that of HDL apoproteins by severalfold or more, suggesting an independent catabolic fate of these constituents. The present study investigated the cellular uptake and dissociation of HDL labeled in its apoproteins with 125I and in its cholesterol ester with [3H]cholesteryl palmityl ether, a nonhydrolyzable cholesterol ester analogue. Approximately 50% of cell-associated 125I-HDL2 and 125I-HDL3 was released from prelabeled adipose cells by incubating the latter in the presence or absence of unlabeled lipoproteins for 2 h. The uptake of HDL-cholesterol ester by human fat cells as reflected by [3H]cholesteryl palmityl ether was 5-18 times greater than that predicted from the uptake of 125I-HDL2 and 125I-HDL3 and was irreversible. Analysis of dissociated 125I-HDL3 demonstrated changes to both higher and lower density fractions compared with the starting material. There was a high correlation between the cellular uptake of HDL3-cholesterol ester and HDL3-apoprotein uptakes (r = 0.90, P less than 0.01), suggesting that HDL-cholesterol ester uptake requires a specific apoprotein interaction or binding step. The selective uptake and retention of HDL-cholesterol ester by isolated adipocytes implies that human fat tissue may play a role in regulating the lipid composition of plasma HDL.