Apolipoprotein E isoform-specific binding to the low-density lipoprotein receptor |
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Authors: | Yamamoto Taichi Choi Hyung Won Ryan Robert O |
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Institution: | Center for Prevention of Obesity, Diabetes, and Cardiovascular Disease, Children's Hospital Oakland Research Institute, Oakland, CA 94609, USA. |
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Abstract: | Apolipoprotein E (apoE) is a ligand for members of the low-density lipoprotein receptor (LDLR) family and functions in plasma cholesterol homeostasis. A fluorescence-based assay has been employed in molecular studies of receptor-ligand interactions. Competition experiments revealed isoform-specific differences in binding of lipid-associated apoE N terminal (NT) domain to a recombinant soluble LDLR (sLDLR). In a similar manner, lipid--associated-but not lipid-free--full-length apoE3 showed binding activity to sLDLR. The molecular chaperone, receptor-associated protein, inhibited apoE3-NT-phospholipid complex binding to sLDLR. Kinetic studies of apoE3-NT-phospholipid complex interaction with sLDLR revealed time-dependent effects of apoE-NT isoform binding to sLDLR. The results reveal a discerning method for study of the molecular basis of ligand interactions that likely influence receptor function in maintenance of whole body cholesterol homeostasis. |
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Keywords: | Apolipoprotein Receptor Fluorescence Energy transfer Isoform |
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