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Identification of autoantibodies in human plasma recognizing an apoB-100 LDL receptor binding site peptide

Nordin Fredrikson, Gunilla LU ; Berglund, Göran LU ; Alm, Ragnar LU ; Nilsson, Jan-Åke LU ; Shah, Prediman K. and Nilsson, Jan LU (2006) In Journal of Lipid Research 47(9). p.2049-2054
Abstract
The aim of this study was to test the hypothesis that autoantibodies recognize amino acid sequences in the LDL receptor binding region of apolipoprotein B-100 (apoB-100). Autoantibodies against an unmodified or malondialdehyde (MDA)-modified LDL receptor binding site peptide were determined by ELISA in baseline plasma samples of 78 cases with coronary events and 149 matched controls recruited from the prospective Malmo Diet Cancer Study. IgG and IgM recognizing this peptide were detected in all subjects but did not differ between cases and controls. Inverse associations were observed between IgG against the native binding site and plasma oxidized LDL (r = -0.21, P < 0.005), but there were no significant associations with total or LDL... (More)
The aim of this study was to test the hypothesis that autoantibodies recognize amino acid sequences in the LDL receptor binding region of apolipoprotein B-100 (apoB-100). Autoantibodies against an unmodified or malondialdehyde (MDA)-modified LDL receptor binding site peptide were determined by ELISA in baseline plasma samples of 78 cases with coronary events and 149 matched controls recruited from the prospective Malmo Diet Cancer Study. IgG and IgM recognizing this peptide were detected in all subjects but did not differ between cases and controls. Inverse associations were observed between IgG against the native binding site and plasma oxidized LDL (r = -0.21, P < 0.005), but there were no significant associations with total or LDL cholesterol levels. In univariate analyses, inverse associations were found between baseline carotid intima-media thickness and IgG against the MDA-modified binding site (r = -0.14, P < 0.05), but this association was lost when controlling for other major cardiovascular risk factors. Specificity studies demonstrated that the binding of autoantibodies to these sequences could be inhibited by oxidized but not by native LDL. Autoantibodies recognizing the LDL receptor binding site in apoB-100 are frequently expressed. Their association with plasma oxidized LDL suggests that they have been generated in response to breakdown products of LDL oxidation, but their influence on cholesterol metabolism and the development of atherosclerosis appears limited. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
apolipoprotein B-100, atherosclerosis, low density lipoprotein
in
Journal of Lipid Research
volume
47
issue
9
pages
2049 - 2054
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:16809787
  • wos:000240351800018
  • scopus:33748752424
ISSN
1539-7262
DOI
10.1194/jlr.M600217-JLR200
language
English
LU publication?
yes
id
06c60789-e2e8-4ce1-847f-250a8dc1950d (old id 394070)
date added to LUP
2007-10-02 21:28:56
date last changed
2019-02-20 04:35:20
@article{06c60789-e2e8-4ce1-847f-250a8dc1950d,
  abstract     = {The aim of this study was to test the hypothesis that autoantibodies recognize amino acid sequences in the LDL receptor binding region of apolipoprotein B-100 (apoB-100). Autoantibodies against an unmodified or malondialdehyde (MDA)-modified LDL receptor binding site peptide were determined by ELISA in baseline plasma samples of 78 cases with coronary events and 149 matched controls recruited from the prospective Malmo Diet Cancer Study. IgG and IgM recognizing this peptide were detected in all subjects but did not differ between cases and controls. Inverse associations were observed between IgG against the native binding site and plasma oxidized LDL (r = -0.21, P &lt; 0.005), but there were no significant associations with total or LDL cholesterol levels. In univariate analyses, inverse associations were found between baseline carotid intima-media thickness and IgG against the MDA-modified binding site (r = -0.14, P &lt; 0.05), but this association was lost when controlling for other major cardiovascular risk factors. Specificity studies demonstrated that the binding of autoantibodies to these sequences could be inhibited by oxidized but not by native LDL. Autoantibodies recognizing the LDL receptor binding site in apoB-100 are frequently expressed. Their association with plasma oxidized LDL suggests that they have been generated in response to breakdown products of LDL oxidation, but their influence on cholesterol metabolism and the development of atherosclerosis appears limited.},
  author       = {Nordin Fredrikson, Gunilla and Berglund, Göran and Alm, Ragnar and Nilsson, Jan-Åke and Shah, Prediman K. and Nilsson, Jan},
  issn         = {1539-7262},
  keyword      = {apolipoprotein B-100,atherosclerosis,low density lipoprotein},
  language     = {eng},
  number       = {9},
  pages        = {2049--2054},
  publisher    = {American Society for Biochemistry and Molecular Biology},
  series       = {Journal of Lipid Research},
  title        = {Identification of autoantibodies in human plasma recognizing an apoB-100 LDL receptor binding site peptide},
  url          = {http://dx.doi.org/10.1194/jlr.M600217-JLR200},
  volume       = {47},
  year         = {2006},
}