Oxidation of Low-Density Lipoprotein by Hypochlorite Causes Aggregation That is Mediated by Modification of Lysine Residues Rather Than Lipid Oxidation
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Peroxidation of low-density lipoprotein (LDL) lipid is generally thought to represent the initial step in a series of modification reactions that ultimately transform the protein moiety of the lipoprotein into a form recognized by receptors different from those that bind native LDL. Uptake of LDL via these alternative receptors can lead to the formation of lipid-laden cells, which are typical for the early stages of atherogenesis. We have studied the oxidative modification of LDL by hypochlorite (-OCl), a powerful oxidant produced from H2O2 and chloride via the action of myeloperoxidase which is released from activated neutrophils and monocytes. Exposure of LDL to reagent or enzymically generated -OCl at 4 or 37 degrees C resulted in immediate and preferential oxidation of amino acid residues of apolipoprotein B-100, the single protein associated with LDL. Lysine residues quantitatively represented the major target and, like tryptophan, were oxidized to approximately the same extent with reagent or enzymically generated -OCl. In contrast, LDL lipid oxidation was less favoured than protein oxidation, as judged by the amounts of lipid hydroperoxides, chlorohydrins, cholesterol or fatty acid oxidation products formed. Treatment with -OCl caused aggregation of LDL, as shown by an increased turbidity of the oxidized LDL solution and elution from a size-exclusion h.p.l.c. column of high-molecular-mass LDL complexes. Chemical modification of lysine residues before oxidation with -OCl prevented aggregation, while it enhanced the extent of lipid peroxidation. Treatment of LDL with -OCl also caused the formation of carbonyl groups and release of ammonia; both these modifications were inhibited by lysine-residue modification before oxidation. These results demonstrate that aggregation reactions are dependent on initial lysine oxidation by -OCl, followed by deamination and carbonyl formation, but do not involve lipid (per)oxidation. We propose that the observed -OCl-mediated aggregation of LDL is caused, at least in part, by cross-linking of apoproteins by Schiff-base formation independently of lipid peroxidation.
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Protein chlorination has been associated with structural changes of target proteins including fragmentation, crosslinking, aggregation, unfolding, and modulation of specific functions such as immunogenicity, enzymatic activity and ligand-receptor interaction.
“Protein chlorination has been associated with structural changes of target proteins including fragmentation, crosslinking, aggregation, unfolding, and modulation of specific functions such as immunogenicity, enzymatic activity and ligand-receptor interaction (48, 79).”
From Hypochlorous Acid: From Innate Immune Factor and Environmental Toxicant to Chemopreventive Agent Targeting Solar UV-Induced Skin Cancer (2022) · cites this paper as [79]
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- Authors
- Hazell, L. J., van den Berg, J. J. M., & Stocker, R.
- Affiliations
- The Heart Research Institute (AU)
- Children's Hospital Oakland Research Institute, Oakland, CA 94609, U.S.
- Corresponding author
- Stocker, R
- ORCID
- Stocker, R
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1994-08-15
- Volume
- 302
- Issue
- 1
- Pages
- 297-304
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1137223
- OpenAlex
- W2142527036
- Cited by
- 267
- References
- 44
- Citations by year
- 2025: 2 · 2024: 4 · 2023: 5 · 2022: 3 · 2021: 6 · 2020: 7 · 2019: 4 · 2018: 6 · 2017: 5 · 2016: 11 · 2015: 5 · 2014: 6 · 2013: 7 · 2012: 9
- FWCI
- 5.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Health and Human Services
- Tobacco-Related Disease Research Program
- National Institutes of Health (5r01dk034400-10)
- Medical Research Council
- National Health and Medical Research Council
- National Institute of Diabetes and Digestive and Kidney Diseases (P01DK032094, DK-34400, DK32094)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- LDL oxidation, hypochlorite, lysine oxidation, LDL aggregation, apolipoprotein B-100, lipid peroxidation, myeloperoxidase, atherogenesis, Schiff base formation, protein cross-linking, carbonyl formation, tryptophan oxidation, lipid hydroperoxides, neutrophils, monocytes
- MeSH terms
- Adult, Female, Humans, Hypochlorous Acid, Lipoproteins, LDL, Lysine, Male, Oxidation-Reduction
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