Cited by 593Atherosclerosis and Cardiovascular DiseasesNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

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Presence of hypochlorite-modified proteins in human atherosclerotic lesions.

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Hazell, L J, Arnold, L, Flowers, D, Waeg, G, Malle, E, Stocker, R·1996·Journal of Clinical Investigation

DOI 10.1172/jci118576PMC PMC507214

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Abstract

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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Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
The pathogenesis of atherosclerosis: a perspective for the 1990s
Ross, R. (1993) · Nature · doi:10.1038/362801a0 · Cited by 10,618
Theory and Practice of Histological Techniques
Bancroft, J. D., & Gamble, M. (1990) · Cited by 6,948
Beyond Cholesterol
Epstein, F. H., Steinberg, D. I., Parthasarathy, S., Carew, T. E., Khoo, J. C., & Witztum, J. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198904063201407 · Cited by 6,425
Evidence for the presence of oxidatively modified low density lipoprotein in atherosclerotic lesions of rabbit and man.
Ylä‐Herttuala, S., Palinski, W., Rosenfeld, M. E., Parthasarathy, S., Carew, T. E., Butler, S. S., Witztum, J. L., & Steinberg, D. H. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114271 · Cited by 1,877
Low density lipoprotein undergoes oxidative modification in vivo.
Palinski, W., Rosenfeld, M. E., Ylä‐Herttuala, S., Gurtner, G. C., Socher, S. S., Butler, S. W., Parthasarathy, S., Carew, T. E., Steinberg, D. H., & Witztum, J. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.4.1372 · Cited by 1,514
The role of the monocyte in atherogenesis: I. Transition of blood-borne monocytes into foam cells in fatty lesions.
Rg, G. (1981) · PubMed Central · Cited by 1,314
A definition of initial, fatty streak, and intermediate lesions of atherosclerosis. A report from the Committee on Vascular Lesions of the Council on Arteriosclerosis, American Heart Association.
Stary, H. C., Chandler, A. B., Glagov, S. K., Guyton, J. R., Insull, W., Rosenfeld, M. E., Schaffer, S. A., Schwartz, C. J., Wagner, W. D., & Wissler, R. W. (1994) · Circulation · doi:10.1161/01.cir.89.5.2462 · Cited by 1,313
Autoantibody against oxidised LDL and progression of carotid atherosclerosis
Salonen, J. T., Korpela, H., Salonen, R., Nyyssönen, K., Ylä‐Herttuala, S., Yamamoto, R., Butler, S., Palinski, W., & Witztum, J. L. (1992) · The Lancet · doi:10.1016/0140-6736(92)90926-t · Cited by 1,311
Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269

Show all 39 references

Research works printed but not linked: 1

Adams, D.O., and T.A. Hamilton. 1992. Macrophages as destructive cells in host defense. In Inflammation: Basic principles and clinical correlates. J.I. Gallin, I.M. Goldstein, and R. Snyderman. Raven Press, New York. 637- 662.

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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: Malle, E
Stocker, R
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1996-03-15
Volume: 97
Issue: 6
Pages: 1535-1544
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci118576
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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Presence of hypochlorite-modified proteins in human atherosclerotic lesions.

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