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      Investigation of Serum Oxidized Low-Density Lipoprotein IgG Levels in Patients with Angiographically Defined Coronary Artery Disease

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          Abstract

          It has been suggested that antioxidized low-density lipoprotein (anti-oxLDL) antibodies play a role in the pathogenesis of atherosclerosis. The aim of this study was to measure serum ox-LDL IgG levels in 31 patients with angiographically defined coronary artery disease (CAD) (≥50% stenosis in at least one major coronary artery; CAD + group) and compare these levels with those of 32 subjects with <50% coronary stenosis (CAD group) and 24 healthy age- and sex-matched controls using ELISA. We did not find any significant difference between CAD +, CAD , and control groups in regard to oxLDL IgG levels ( P = 0.83). Serum oxLDL IgG levels did not differ between 1VD (one vessel disease), 2VD (2 vessels disease), and 3VD (3 vessels disease) subgroups of CAD + patients ( P = 0.20). Serum anti-oxLDL titers were only significantly correlated with LDL-C in the CAD + group ( P < 0.05) and waist and hip circumference ( P < 0.05 and P < 0.01, resp.) in the CAD group. In stepwise regression analysis, none of the conventional cardiovascular risk factors was associated with serum ox-LDL IgG levels. The present results suggest that serum levels of ox-LDL IgG are neither associated with the presence and severity of CAD nor with the conventional cardiovascular risk factors.

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          Most cited references 38

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          Prediction of Coronary Heart Disease Using Risk Factor Categories

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            Markers of Inflammation and Cardiovascular Disease

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              Evidence for the presence of oxidatively modified low density lipoprotein in atherosclerotic lesions of rabbit and man.

              Three lines of evidence are presented that low density lipoproteins gently extracted from human and rabbit atherosclerotic lesions (lesion LDL) greatly resembles LDL that has been oxidatively modified in vitro. First, lesion LDL showed many of the physical and chemical properties of oxidized LDL, properties that differ from those of plasma LDL: higher electrophoretic mobility, a higher density, higher free cholesterol content, and a higher proportion of sphingomyelin and lysophosphatidylcholine in the phospholipid fraction. A number of lower molecular weight fragments of apo B were found in lesion LDL, similar to in vitro oxidized LDL. Second, both the intact apo B and some of the apo B fragments of lesion LDL reacted in Western blots with antisera that recognize malondialdehyde-conjugated lysine and 4-hydroxynonenal lysine adducts, both of which are found in oxidized LDL; plasma LDL and LDL from normal human intima showed no such reactivity. Third, lesion LDL shared biological properties with oxidized LDL: compared with plasma LDL, lesion LDL produced much greater stimulation of cholesterol esterification and was degraded more rapidly by macrophages. Degradation of radiolabeled lesion LDL was competitively inhibited by unlabeled lesion LDL, by LDL oxidized with copper, by polyinosinic acid and by malondialdehyde-LDL, but not by native LDL, indicating uptake by the scavenger receptor(s). Finally, lesion LDL (but not normal intimal LDL or plasma LDL) was chemotactic for monocytes, as is oxidized LDL. These studies provide strong evidence that atherosclerotic lesions, both in man and in rabbit, contain oxidatively modified LDL.
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                Author and article information

                Journal
                Int J Vasc Med
                Int J Vasc Med
                IJVM
                International Journal of Vascular Medicine
                Hindawi Publishing Corporation
                2090-2824
                2090-2832
                2014
                3 February 2014
                : 2014
                Affiliations
                1Cardiovascular Research Center, Mashhad University of Medical Sciences, Mashhad, Iran
                2Department of Cardiology, Mashhad University of Medical Sciences, Mashhad, Iran
                3Student Research Committee, Biochemistry of Nutrition Research Center, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
                4Biochemistry of Nutrition Research Center, School of Medicine, Mashhad University of Medical Sciences, Mashhad 9177948564, Iran
                5Health Sciences Research Center, Department of Biostatistics and Epidemiology, School of Health, Mashhad University of Medical Sciences, Mashhad, Iran
                6Department of Clinical Biochemistry, Tehran University of Medical Sciences, Tehran, Iran
                7Biotechnology Research Center, Mashhad University of Medical Sciences, Mashhad, Iran
                Author notes
                *Majid Ghayour-Mobarhan: ghayourm@ 123456mums.ac.ir

                Academic Editor: Karlheinz Peter

                Article
                10.1155/2014/845960
                3930021
                Copyright © 2014 Mohsen Moohebati et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                Categories
                Research Article

                Cardiovascular Medicine

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