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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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Anionic phospholipids inhibit apolipoprotein E--low-density lipoprotein receptor interactions.

Taichi Yamamoto¹, Robert O Ryan

¹Center for Prevention of Obesity, Diabetes and Cardiovascular Disease, Children's Hospital, Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA.

Biochemical and Biophysical Research Communications

|January 30, 2007

Summary

The lipid composition of apolipoprotein E (apoE) particles significantly impacts their binding to the low-density lipoprotein receptor (LDLR). Specific phospholipids like DMPS inhibit LDLR binding, revealing lipid-dependent modulation of apoE-LDLR interactions.

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Area of Science:

Biochemistry
Molecular Biology
Lipid Metabolism

Background:

Apolipoprotein E (apoE) acts as a ligand for low-density lipoprotein receptors (LDLRs).
Lipid-free apoE is not recognized by LDLRs; lipid interaction induces conformational changes and receptor recognition.
The influence of lipid composition on apoE-LDLR binding remains unclear.

Purpose of the Study:

To investigate if the lipid composition of apoE-lipid complexes affects LDLR binding affinity.
To determine the role of specific phospholipids in modulating apoE's function as an LDLR ligand.

Main Methods:

Reconstitution of apoE3 N-terminal (NT) domain with various phospholipids, including dimyristoylphosphatidylcholine (DMPC), egg sphingomyelin, dimyristoylphosphatidylglycerol, and dimyristoylphosphatidylserine (DMPS).
Assessment of LDLR binding activity of these reconstituted lipoprotein particles.
Analysis of dose-dependent effects of DMPS on LDLR binding.

Main Results:

Maximal LDLR binding of apoE3-NT was observed at DMPC:apoE3-NT ratios greater than 2.5:1 (w/w).
Lipid particles with egg sphingomyelin were functional LDLR ligands.
Complexes with anionic phospholipids dimyristoylphosphatidylglycerol or DMPS showed no LDLR binding.
Increasing DMPS concentration in mixed DMPC/DMPS particles progressively inhibited LDLR binding.

Conclusions:

Lipid composition of apoE-lipid particles is a critical determinant of LDLR binding activity.
Beyond conformational changes, specific lipids can directly modulate the interaction between apoE and LDLR.
This finding has implications for understanding lipoprotein metabolism and receptor-mediated uptake.