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Isolation and characterization of human apolipoprotein M-containing lipoproteins

Christoffersen, Christina ; Nielsen, Lars Bo ; Axler, Olof LU ; Andersson, Astra LU ; Johnsen, Anders H. and Dahlbäck, Björn LU (2006) In Journal of Lipid Research 47(8). p.1833-1843
Abstract
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 immunoaffinity chromatography and compared with lipoproteins lacking apoM. The apoM-containing lipoproteins were predominantly of HDL size; similar to 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, paraoxonase 1, and apoB. ApoM-containing HDL (HDLapoM+) contained significantly more free cholesterol than HDL lacking apoM... (More)
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 immunoaffinity chromatography and compared with lipoproteins lacking apoM. The apoM-containing lipoproteins were predominantly of HDL size; similar to 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, paraoxonase 1, and apoB. ApoM-containing HDL (HDLapoM+) contained significantly more free cholesterol than HDL lacking apoM (HDLapoM-) (5.9 +/- 0.7% vs. 3.2 +/- 0.5%; P < 0.005) and was heterogeneous in size with both small and large particles. HDLapoM+ inhibited Cu2+-induced oxidation of LDL and stimulated 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 stimulates cholesterol efflux more efficiently than HDL lacking apoM. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cholesterol efflux, oxidation, apoM
in
Journal of Lipid Research
volume
47
issue
8
pages
1833 - 1843
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:16682745
  • wos:000240023100023
  • scopus:33747107812
  • pmid:16682745
ISSN
1539-7262
DOI
10.1194/jlr.M600055-JLR200
language
English
LU publication?
yes
id
bbd9f019-5762-445a-83c6-e6dff0da306e (old id 395091)
date added to LUP
2016-04-01 12:05:52
date last changed
2020-09-23 02:48:05
@article{bbd9f019-5762-445a-83c6-e6dff0da306e,
  abstract     = {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 immunoaffinity chromatography and compared with lipoproteins lacking apoM. The apoM-containing lipoproteins were predominantly of HDL size; similar to 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, paraoxonase 1, and apoB. ApoM-containing HDL (HDLapoM+) contained significantly more free cholesterol than HDL lacking apoM (HDLapoM-) (5.9 +/- 0.7% vs. 3.2 +/- 0.5%; P &lt; 0.005) and was heterogeneous in size with both small and large particles. HDLapoM+ inhibited Cu2+-induced oxidation of LDL and stimulated 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 stimulates cholesterol efflux more efficiently than HDL lacking apoM.},
  author       = {Christoffersen, Christina and Nielsen, Lars Bo and Axler, Olof and Andersson, Astra and Johnsen, Anders H. and Dahlbäck, Björn},
  issn         = {1539-7262},
  language     = {eng},
  number       = {8},
  pages        = {1833--1843},
  publisher    = {American Society for Biochemistry and Molecular Biology},
  series       = {Journal of Lipid Research},
  title        = {Isolation and characterization of human apolipoprotein M-containing lipoproteins},
  url          = {http://dx.doi.org/10.1194/jlr.M600055-JLR200},
  doi          = {10.1194/jlr.M600055-JLR200},
  volume       = {47},
  year         = {2006},
}