Isolation and characterization of human apolipoprotein M-containing lipoproteins
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/395091
- author
- Christoffersen, Christina ; Nielsen, Lars Bo ; Axler, Olof LU ; Andersson, Astra LU ; Johnsen, Anders H. and Dahlbäck, Björn LU
- organization
- publishing date
- 2006
- 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
- 2022-04-29 00:39:45
@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 < 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}}, keywords = {{cholesterol efflux; oxidation; apoM}}, 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}}, }