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High density lipoprotein binding by rat Fu5AH hepatoma cells is not related to cholesterol content
Journal article   Peer reviewed

High density lipoprotein binding by rat Fu5AH hepatoma cells is not related to cholesterol content

Betty A. Gottlieb, Julian B. Marsh and Maria Teresa Schultheis
Atherosclerosis, v 67(2), pp 251-259
1987
DOI: https://doi.org/10.1016/0021-9150(87)90286-3
PMID: 3118894
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Apolipoprotein A-I Cholesterol effects HDL binding Hepatoma cells
The binding of 125I-HDL obtained from nephrotic rats (HDL ne) containing only apo A-I and apo C, to rat hepatoma cells (Fu5AH) grown to confluency was studied under conditions which increased the free cholesterol or the cholesteryl ester content. The high affinity binding ( K d = 5nM) measured at 4°C was unchanged. This transformed cell line also exhibited greater specificity for rat HDL compared to human HDL than has been reported for other types of cultured cells. When the cells were allowed to internalize and degrade HDL ne at 37°C, the acid-soluble products were derived almost entirely from the breakdown of apo A-I. Competition experiments with an LDL fraction from nephrotic rat plasma (LDL ne) which contained 20% of apo A-I indicated that it was as effective as other rat HDL preparations in competing for the binding of HDL ne at 4°C, based on its content of apo A-I. Control experiments indicated that labeled apo A-I in HDL ne exchanged less than 1% when incubated with a 50-fold excess of unlabeled LDL ne for 2 h at 4°C. These results point to a critical role of cell type in HDL binding. They support the view that apo A-I is a ligand. The up-regulation of high affinity HDL binding by cholesterol which has been reported with cultured human fibroblasts and Hep G2 cells does not occur in the Fu5AH rat hepatoma cell line.

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Web of Science research areas
Cardiac & Cardiovascular Systems
Peripheral Vascular Disease
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