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Papers In Press, published online ahead of print November 4, 2002
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Submitted on July 3, 2002
Centre for Thrombosis and Vascular Research, University of New South Wales, School of Medical Sciences, UNSW Sydney, NSW 2052
Corresponding Author: r.stocker{at}unsw.edu.au
Atherosclerosis is commonly considered to be a state of heightened oxidative stress. Oxidized low-density lipoprotein (ox-LDL) is present in human atherosclerotic lesions and also used as marker for coronary artery disease. The present study investigated specific chemical changes occurring to apolipoprotein A-I (apoA-I) and A-II, as isolated high-density lipoproteins (HDL) and human plasma undergo oxidation. Such studies may be important, as in human lesions lipids associated with HDL are as oxidized as those associated with LDL. We show here that during mild, chemically induced oxidation of HDL and plasma, or autoxidation of plasma, Met residues in both of HDL's two major apolipoproteins become selectively and consecutively oxidized to their respective Met sulfoxide (MetO) forms that can be separately readily by reversed phase HPLC. Autoxidation is prevented completely by placing plasma at -20 °C, whereas metal chelators and butylated hydroxytoluene only offer partial protection. Independent of the oxidation conditions tested, apoA-I and apoA-II (dimer) with two MetO residues accumulate over time and are relatively stable oxidation products. Compared to controls, serum samples from subjects with the endothelial cell nitric oxide synthase a/b genotype that is associated with increased coronary artery disease, contained increased concentrations of apoA-I with two MetO residues. Our results demonstrate that during the early stages of plasma oxidation, oxidation of HDL-associated apolipoproteins is limited to chemically defined modifications. The results suggest that some of these specifically oxidized forms of apoA-I and apoA-II may be useful markers of in vivo HDL oxidation, and hence potentially atherosclerosis.
Revised on October 9, 2002
Accepted on October 25, 2002
Characterization of specifically oxidized apolipoproteins in mildly oxidized high-density lipoprotein
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