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Presence of hypochlorite-modified proteins in human atherosclerotic lesions.
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Oxidation of LDL may contribute to atherogenesis, though the nature of the in vivo oxidant(s) remains obscure. Myeloperoxidase, the enzyme responsible for hypochlorous acid/hypochlorite (HOCl) production in vivo, is present in active form in human atherosclerotic lesions, and HOCl aggregates and transforms LDL into a high-uptake form for macrophages in vitro. Here we demonstrate HOCl-modified proteins in human lesions using an mAb raised against HOCl-modified LDL that recognizes HOCl-oxidized proteins but does not cross-react with Cu2+-, malondialdehyde-, or 4-hydroxynonenal-modified LDL. This antibody detected significantly more material in advanced atherosclerotic lesions than normal arteries, even though azide and methionine were included during sample work-up to inhibit myeloperoxidase and to scavenge HOCl. The epitope(s) recognized was predominantly cell associated and present in monocyte/macrophages, smooth muscle, and endothelial cells. The intima and cholesterol clefts stained more heavily than the center of the thickened vessels; adventitial staining was apparent in some cases. Immunostaining was also detected in a very early lesion from an accident victim, beside healthy areas that were unreactive. LDL oxidized by HOCl in vitro, but not native LDL, effectively competed with the epitopes in lesions for antibody binding. Density centrifugation of plaque homogenates and Western blot analysis showed that, in the apo B-containing lipoprotein fraction, the mAb recognized protein(s) of molecular mass greater than apo B, similar to those produced during oxidation of LDL with HOCl in vitro. Three major proteins were recognized by the anti-HOCl-modified protein antibody but not by an anti-apo B antibody in the apo B-free fraction. Together, these results demonstrate HOCl-oxidized proteins in human atherosclerotic lesions, implicating this oxidant in LDL modification in vivo.
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“Macrophage localization in the atherosclerotic plaque leads to detectable MPO activity and products of HOCl oxidation (213, 414).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [414]
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Metadata
- Authors
- Hazell, L. J., Arnold, L., Flowers, D., Waeg, G., Malle, E., & Stocker, R.
- Affiliations
- The Heart Research Institute (AU)
- The University of Sydney (AU)
- University of Graz (AT)
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 1996-03-15
- Volume
- 97
- Issue
- 6
- Pages
- 1535-1544
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC507214
- OpenAlex
- W2118480498
- Cited by
- 592
- References
- 39
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 14 · 2023: 14 · 2022: 19 · 2021: 12 · 2020: 18 · 2019: 20 · 2018: 26 · 2017: 16 · 2016: 12 · 2015: 17 · 2014: 15 · 2013: 13 · 2012: 16
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart Foundation of Australia
- Austrian Science Fund
- Medical Research Council
- National Health and Medical Research Council
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- hypochlorite, myeloperoxidase, atherosclerosis, LDL oxidation, oxidized LDL, atherosclerotic plaque, macrophages, smooth muscle cells, endothelial cells, oxidizing agents, atherogenesis
- MeSH terms
- Arteriosclerosis, Humans, Hypochlorous Acid, Immunohistochemistry, Lipoproteins, LDL, Oxidation-Reduction, Proteins
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