ArticleArchives of biochemistry and biophysics2025
Conformational features of guinea pig apolipoprotein E offer insights into functioning of human apolipoprotein E.
Article in Archives of biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Apolipoprotein (apo) E is a major cholesterol transport protein in the plasma and brain of humans, with the APOE ε4 allele (coding for R112) associated with a higher risk for cardiovascular and Alzheimer's diseases (CVD and AD, respectively) compared to APOE ε3 (coding for C112). The molecular basis underlying the link between APOE ε4 and CVD/AD is poorly understood. Here apoE from Cavia porcellus (guinea pig, GP), which is 72 % identical to human apoE4 but lacking residues 193-197 and 246-252, a feature noted in all hystricomorph apoE, was used as a model to understand the role of apoE4. Western blot with anti-human apoE antibody revealed cross reactivity with bacterially expressed recombinant GP apoE. GP apoE solubilized phospholipids far more efficiently than apoE3/E4 but promoted macrophage cholesterol efflux to a similar extent. The overall secondary structure and tetrameric organization of GP apoE were broadly similar to those of apoE3/E4. Guanidine HCl-induced denaturation revealed a biphasic unfolding pattern indicative of a two-domain architecture for GP apoE. Hydrogen-deuterium exchange coupled to mass spectrometry of GP apoE revealed mixed EX1/EX2 kinetics similar to that noted for apoE4, with peak broadening indicative of the presence of partially folded intermediate states. Limited proteolysis reveals more resistance to cleavage compared to apoE3/E4. Taken together, the findings suggest that the CT domain modulates the lipid-binding ability of apoE and attenuates the overall dynamics of the protein, which bears direct relevance in regulation of lipoprotein metabolism with implications in amyloid-related neurodegeneration.
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