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  • Title: Interaction of apolipoprotein B-containing lipoprotein secreted by Hep G2 cells with receptors for low-density lipoprotein.
    Author: Fuki IV, Menschikov GB, Menschikowski M, Adamova IYu, Repin VS.
    Journal: Biochim Biophys Acta; 1991 Nov 05; 1086(2):237-40. PubMed ID: 1657183.
    Abstract:
    Radioligand and immunoenzymatic techniques were used to characterize the receptor binding properties of apolipoprotein B-containing lipoprotein produced by HepG2 cell line (H-LpB). It was found that compared to plasma low-density lipoprotein (LDL), the interaction of H-LpB nonseparated from conditioned medium with normal fibroblasts was 6-8-times lower and only slightly exceeded the nonspecific binding of LDL modified by malondialdehyde, while the uptake of the indicated lipoproteins by LDL receptor-negative strain of fibroblasts were identical. The uptake of H-LpB by normal fibroblasts increased 1.5-2-times after isolation from the culture medium by immunoaffinity chromatography. The effect of isolation could be explained by the finding that apolipoprotein E-containing lipoprotein secreted by HepG2 cells effectively competed for the binding with LDL-receptors. The obtained results suggest that H-LpB produced by HepG2 cells is poorly recognized by the LDL-receptors.
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