| Literature DB >> 17923100 |
Taichi Yamamoto1, Hyung Won Choi, Robert O Ryan.
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.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17923100 PMCID: PMC2174959 DOI: 10.1016/j.ab.2007.09.005
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365