Key result
Apolipoprotein A-II increases the thermodynamic stability of HDL alpha-helical structure, alters apoA-I conformation, and selectively inhibits lipid hydrolysis by hepatic lipase.
ApoA-II enhances the structural stability of HDL particles and modulates lipid metabolism by inhibiting hepatic lipase-mediated lipid hydrolysis.
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Hypothesis-generating for apoA-II in HDL metabolism; leaves open therapeutic relevance pending human studies.
Boucher et al. (2004) studied this question. Apolipoprotein A-II was evaluated on HDL structure, stability, and lipid hydrolysis. Apolipoprotein A-II increases the thermodynamic stability of HDL alpha-helical structure, alters apoA-I conformation, and selectively inhibits lipid hydrolysis by hepatic lipase.
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