The binding of high density lipoproteins to isolated rat hepatocytes.
The binding of high density lipoproteins to isolated rat hepatocytes.
复制标题
高密度脂蛋白与离体大鼠肝细胞的结合。
DOI：
10.3109/00365518109092016
复制
发表时间：
1981
影响因子：
2.1
通讯作者：
T. Berg
中科院分区：
文献类型：
--
作者：
L. Ose;I. Røken;K. Norum;C. Drevon;T. Berg
The association of 125I-labelled rat high density lipoproteins (125-I-HDL) to suspended rat hepatocytes was studied at 4 degrees C. 125 I-HDL associated to isolated hepatocytes by two processes-one of high and one of low affinity. The cell-association of 125I-HDL exhibited saturation kinetics and was inhibited to varying degrees with both rat and human lipoproteins such as VLDL, LDL and HDL but not by lipoprotein deficient serum or asialo-fetuin. The cell-association of 125I-HDL did not require divalent cations and could be reduced by pronase treatment of the cells. The binding site was clearly different from the receptor for LDL in extrahepatic cells since heparin and apolipoprotein E did not compete and cholesterol ester labelled HDL. The number of binding sites for HDL at 4 degrees C was 2.2 X 10(6) per cell and the association constant (Ka) 8.2 X 10(6) (mol/l)-1. Experiments with HDL labelled with [3H] cholesterol by means of lecithin: cholesterol acyltransferase (LCAT, EC 2.3.1.43) in the cholesterol ester moiety suggested that the same mechanism was responsible for the cell-association of HDL prepared this way.
