La apolipoprote铆na A-II altera la composici贸n apolipoproteica de HDL y su capacidad para activar la lipoprote铆na lipasa
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摘要

Introduction

Apolipoprotein (apo)A-II is the second most abundant HDL protein but its function remains largely unknown. Studies in humans and genetically-modified mice have demonstrated a role for apoA-II in triglyceride metabolism. The main objective of this study was to evaluate the relationship between apoA-II and HDL apolipoprotein composition, as well as HDL-mediated lipoprotein lipase (LPL) coactivation and plasma triglyceride concentration.

Methods

Eleven-hour fasting blood samples were taken from 32 healthy volunteers. Anthropometric data and lipid and apolipoprotein parameters were analyzed. HDL isolated by ultracentrifugation was incubated in the presence of a triolein-based emulsion and bovine LPL. In 14 of these volunteers, an additional blood sample was taken 3 h after breakfast.

Results

ApoA-II concentration was directly correlated with plasma triglycerides (R=0.55, p<0.05) and inversely correlated with the HDL-apoC-II+apoE/apoC-III ratio (R=鈭?.43, p<0.05). ApoA-II was also inversely correlated with HDL-mediated LPL coactivation (R=鈭?.35, p<0.05). ApoA-II concentration was directly correlated with plasma triglycerides 3 h after the fat-loading test (R=0.58, p<0.05).

Conclusion

These results show that HDL-apoA-II levels play a crucial role in triglyceride catabolism and suggest that, at least in part, this is due to modulation of LPL activity.

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