Abstract
Apolipoprotein E (apoE), an anti‐atherogenic apolipoprotein, plays a significant role in the metabolism of lipoproteins. It lowers plasma lipid levels by acting as a ligand for low‐density lipoprotein receptors (LDLr). ApoE mediates this function via essential lysine residues that interact with the LDLr. The objective of this project is to study the effect of oxidative stress (specifically acrolein) mediated in vitro modification on the structure and function of recombinant rat apoE. SDS‐PAGE and RP‐HPLC confirmed that the protein was purified to homogeneity with no signs of degradation. Acrolein modification of apoE was confirmed by Western blot. Guanidine HCl‐induced denaturation revealed that the overall fold of the modified protein was significantly altered. Modified apoE also demonstrated a decrease in heparin binding affinity and lipid binding ability. The LDLr binding ability of modified apoE was significantly impaired. Lastly, MALDI‐TOF/TOF MS analysis identified Lys82, 85, 86, 156 and 252 as likely modification sites by acrolein. Overall, we conclude that acrolein disrupts structural and functional integrity of apoE, which is likely to affect its role in maintaining plasma cholesterol homeostasis.
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