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Papers In Press, published online ahead of print May 8, 2006
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Clinical Biochemistry, KB3011, Rigshospitalet, University of Copenhagen, Copenhagen DK-2100
Corresponding Author: larsbo{at}rh.dk
Apolipoprotein M (apoM) is a novel apolipoprotein with unknown function. In this study, we established a method for isolating apoM-containing lipoproteins and studied their composition and the effect of apoM on HDL function. ApoM-containing lipoproteins were isolated from human plasma with immuno-affinity chromatography and compared with lipoproteins lacking apoM. The apoM-containing lipoproteins were predominantly of HDL size; ~ 5 % of the total HDL population contained apoM. Mass spectrometry showed that the apoM-containing lipoproteins also contained apoJ, apoA-I, apoA-II, apoC-I, apoC-II, apoC-III, PON1, and apoB. ApoM-containing HDL (HDLapoM+) contained significantly more free cholesterol than HDL lacking apoM (HDLapoM-) (5.9±0.7 % versus 3.2±0.5 %, p<0.005) and was heterogeneous in size with both small and large particles. HDLapoM+ inhibited Cu++-induced oxida-tion of LDL and stimulate cholesterol efflux from THP-1 foam cells more efficiently than HDLapoM-. In conclusion our results suggest that apoM is associated with a small heterogeneous subpopulation of HDL particles. Nevertheless, apoM designates a subpopulation of HDL that protects LDL against oxidation and stimulate cholesterol efflux more efficiently than HDL lacking apoM.
Revised on May 8, 2006
Accepted on May 8, 2006
Isolation and characterization of human apolipoprotein M-containing lipoproteins
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