Cited by 1,269Atherosclerosis and Cardiovascular DiseasesNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

The DOI matches its Crossref record; 84 of the 88 references it cites were found in a registry or an index.

Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.

Open access

Daugherty, A, Dunn, J L, Rateri, D L, Heinecke, J W·1994·Journal of Clinical Investigation

DOI 10.1172/jci117342PMC PMC296328

Open this paper in CoChat — free account Open PDF

Abstract

Oxidatively modified lipoproteins have been implicated in atherogenesis, but the mechanisms that promote oxidation in vivo have not been identified. Myeloperoxidase, a heme protein secreted by activated macrophages, generates reactive intermediates that oxidize lipoproteins in vitro. To explore the potential role of myeloperoxidase in the development of atherosclerosis, we determined whether the enzyme was present in surgically excised human vascular tissue. In detergent extracts of atherosclerotic arteries subjected to Western blotting, a rabbit polyclonal antibody monospecific for myeloperoxidase detected a 56-kD protein, the predicted molecular mass of the heavy subunit. Both the immunoreactive protein and authentic myeloperoxidase bound to a lectin-affinity column; after elution with methyl mannoside their apparent molecular masses were indistinguishable by nondenaturing size-exclusion chromatography. Peroxidase activity in detergent extracts of atherosclerotic lesions likewise bound to a lectin column and eluted with methyl mannoside. Moreover, eluted peroxidase generated the cytotoxic oxidant hypochlorous acid (HOCl), indicating that enzymatically active myeloperoxidase was present in lesions. Patterns of immunostaining of arterial tissue with antihuman myeloperoxidase antibodies were similar to those produced by an antimacrophage antibody, and were especially prominent in the shoulder region of transitional lesions. Intense foci of myeloperoxidase immunostaining also appeared adjacent to cholesterol clefts in lipid-rich regions of advanced atherosclerotic lesions. These findings identify myeloperoxidase as a component of human vascular lesions. Because this heme protein can generate reactive species that damage lipids and proteins, myeloperoxidase may contribute to atherogenesis by catalyzing oxidative reactions in the vascular wall.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1172/jci117342

Cites

84 of 84 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
The pathogenesis of atherosclerosis: a perspective for the 1990s
Ross, R. (1993) · Nature · doi:10.1038/362801a0 · Cited by 10,618
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
The Pathogenesis of Atherosclerosis — An Update
Ross, R. (1986) · New England Journal of Medicine · doi:10.1056/nejm198602203140806 · Cited by 4,885
Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
Oxygen-Dependent Microbial Killing by Phagocytes
BABIOR, B. M. (1978) · New England Journal of Medicine · doi:10.1056/nejm197803232981205 · Cited by 2,483
Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition
Goldstein, J. L., Ho, Y. K., Basu, S. K., & Brown, M. S. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.1.333 · Cited by 2,447
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
Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids.
Steinbrecher, U. P., Parthasarathy, S., Leake, D. S., Witztum, J. L., & Steinberg, D. I. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3883 · Cited by 1,626
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

Flagged first, then by citations

Show all 88 references

4 of the 88 references couldn’t be matched to a known paper.

Sorted by citations

Items 101–200 of 999

Human Atherosclerotic Intima and Blood of Patients with Established Coronary Artery Disease Contain High Density Lipoprotein Damaged by Reactive Nitrogen Species
Pennathur, S., Bergt, C., Shao, B., Byun, J., Kassim, S. Y., Singh, P., Green, P. S., McDonald, T. O., Brunzell, J. D., Chait, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406762200 · Cited by 263
Self-citation
Oxidized Low Density Lipoprotein Induces Apoptosis in Cultured Human Umbilical Vein Endothelial Cells by Common and Unique Mechanisms
Harada‐Shiba, M., Kinoshita, M., KAMIDO, H., & Shimokado, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9681 · Cited by 261
Differences in innate immune response between man and mouse
Zschaler, J., Schlorke, D., & Arnhold, J. (2014) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2014011600 · Cited by 264
Neutrophils in the innate immune response.
Kobayashi, S. D., Voyich, J. M., Burlak, C., & DeLeo, F. R. (2005) · PubMed · Cited by 260
Human neutrophils employ chlorine gas as an oxidant during phagocytosis.
Hazen, S. L., Hsu, F., Mueller, D. M., Crowley, J., & Heinecke, J. W. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118914 · Cited by 258
Self-citation
Interactions Between Nitric Oxide and Lipid Oxidation Pathways: Implications for Vascular Disease
O’Donnell, V. B., & Freeman, B. A. (2001) · Circulation Research · doi:10.1161/01.res.88.1.12 · Cited by 257
Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
Fu, S., Davies, M. J., Stocker, R., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3330519 · Cited by 256
Discovery of the nitric oxide signaling pathway and targets for drug development
Nathan, S. B. (2009) · Frontiers in bioscience · doi:10.2741/3228 · Cited by 260
The Roles of Neutrophil-Derived Myeloperoxidase (MPO) in Diseases: The New Progress
Lin, W. C., Chen, H., Chen, X., & Guo, C. (2024) · Antioxidants · doi:10.3390/antiox13010132 · Cited by 290
Aggregation, fusion, and vesicle formation of modified low density lipoprotein particles: molecular mechanisms and effects on matrix interactions
Öörni, K., Pentikäinen, M. O., Ala-Korpela, M., & Kovanen, P. T. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31964-7 · Cited by 252
Lipoxygenase contributes to the oxidation of lipids in human atherosclerotic plaques.
Folcik, V. A., Nivar-Aristy, R. A., Krajewski, L. P., & Cathcart, M. K. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118062 · Cited by 252
Human myeloperoxidase in innate and acquired immunity
Arnhold, J., & Flemmig, J. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.04.008 · Cited by 254
Vascular Oxidative Stress: Impact and Therapeutic Approaches
Sena, C. M., Leandro, A., Azul, L., Seiça, R. M. F., & Perry, G. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01668 · Cited by 266
Immunohistochemical evidence for the myeloperoxidase/H2O2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochlorite‐modified proteins
Malle, E., Waeg, G., Schreiber, R., Gröne, E. F., Sattler, W., & Gröne, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01498.x · Cited by 245
The effects of neutrophil-generated hypochlorous acid and other hypohalous acids on host and pathogens
Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239
High Levels of Systemic Myeloperoxidase Are Associated With Coronary Plaque Erosion in Patients With Acute Coronary Syndromes
Ferrante, G., Nakano, M., Prati, F., Niccoli, G., Mallus, M. T., Ramazzotti, V., Montone, R. A., Kolodgie, F. D., Virmani, R., & Crea, F. (2010) · Circulation · doi:10.1161/circulationaha.110.955302 · Cited by 237
Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II
Marquez‐Curtis, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 237
Biosynthesis, processing, and sorting of human myeloperoxidase
Hansson, M., Olsson, I., & Nauseef, W. M. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.08.009 · Cited by 240
Development of the Lipid-Rich Core in Human Atherosclerosis
Guyton, J. R., & Klemp, K. F. (1996) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.16.1.4 · Cited by 236
A fast-responsive mitochondria-targeted fluorescent probe detecting endogenous hypochlorite in living RAW 264.7 cells and nude mouse
Xiao, H., Xin, K., Dou, H., Yin, G., Quan, Y., & Wang, R. (2014) · Chemical Communications · doi:10.1039/c4cc07411d · Cited by 234
Effect of a short-term diet and exercise intervention on oxidative stress, inflammation, MMP-9, and monocyte chemotactic activity in men with metabolic syndrome factors
Roberts, C. K., Won, D., Pruthi, S., Kurtovic, S., Sindhu, R. K., Vaziri, N. D., & Barnard, R. J. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01292.2005 · Cited by 240
The molecular mechanisms of the thrombotic complications of atherosclerosis
Libby, P. (2008) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2008.01965.x · Cited by 226
Formation of Nitric Oxide–Derived Oxidants by Myeloperoxidase in Monocytes
Hazen, S. L., Zhang, R., Shen, Z., Wu, W., Podrez, E. A., MacPherson, J. C., Schmitt, D. C., Mitra, S. N., Mukhopadhyay, C., Chen, Y., et al. (1999) · Circulation Research · doi:10.1161/01.res.85.10.950 · Cited by 226
Tyrosine 192 in Apolipoprotein A-I Is the Major Site of Nitration and Chlorination by Myeloperoxidase, but Only Chlorination Markedly Impairs ABCA1-dependent Cholesterol Transport
Shao, B., Bergt, C., Fu, X., Green, P., Voss, J. C., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411484200 · Cited by 227
Self-citation
Degradable Semiconducting Oligomer Amphiphile for Ratiometric Photoacoustic Imaging of Hypochlorite
Yin, C., Xu, Z. J., Fan, Q., Huang, W., & Pu, K. (2017) · ACS Nano · doi:10.1021/acsnano.7b01092 · Cited by 227
Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols
Hazen, S. L., Hsu, F. F., Duffin, K., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23080 · Cited by 221
Self-citation
Cocoa polyphenols and inflammatory mediators
Sies, H., SCHEWE, T., Heiß, C., & Kelm, M. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.1.304s · Cited by 224
Vascular Oxidant Stress and Inflammation in Hyperhomocysteinemia
Papatheodorou, L., & Weiss, N. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1750 · Cited by 227
Oxidative risk for atherothrombotic cardiovascular disease
Leopold, J. A., & Loscalzo, J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.009 · Cited by 218
pH Heterogeneity of human and rabbit atherosclerotic plaques; a new insight into detection of vulnerable plaque
Naghavi, M., John, R., Naguib, S., Siadaty, M. S., Grasu, R. M., Kurian, K. C., Winkle, W. B. V., Soller, B. R., Litovsky, S. H., Madjid, M., et al. (2002) · Atherosclerosis · doi:10.1016/s0021-9150(02)00018-7 · Cited by 212
Oxidative stress and cardiovascular disease: new insights
Pignatelli, P., Menichelli, D., Pastori, D., & Violi, F. (2018) · Kardiologia Polska · doi:10.5603/kp.a2018.0071 · Cited by 222
α2-Macroglobulin from Rheumatoid Arthritis Synovial Fluid: Functional Analysis Defines a Role for Oxidation in Inflammation
Wu, S. M., & Pizzo, S. V. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2408 · Cited by 210
Oxidative damage to extracellular matrix and its role in human pathologies
Rees, M. D., Kennett, E. C., Whitelock, J. M., & Davies, M. J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.016 · Cited by 207
Myeloperoxidase, modified lipoproteins, and atherogenesis
Nicholls, S. J., & Hazen, S. L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800086-jlr200 · Cited by 211
Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules
Eiserich, J. P., Patel, R. P., & O’Donnell, V. B. (1998) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(99)00002-3 · Cited by 211
Localization of Nitration and Chlorination Sites on Apolipoprotein A-I Catalyzed by Myeloperoxidase in Human Atheroma and Associated Oxidative Impairment in ABCA1-dependent Cholesterol Efflux from Macrophages
Zheng, L., Settle, M., Brubaker, G., Schmitt, D., Hazen, S. L., Smith, J. D., & Kinter, M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407019200 · Cited by 206
Dysfunctional HDL: A novel important diagnostic and therapeutic target in cardiovascular disease?
Otocka-Kmiecik, A., Mikhailidis, D. P., Nicholls, S. J., Davidson, M. H., Rysz, J., & Banach, M. (2012) · Progress in Lipid Research · doi:10.1016/j.plipres.2012.03.003 · Cited by 207
Myeloperoxidase produces nitrating oxidants in vivo
Gaut, J. P., Byun, J., Tran, H. D., Lauber, W. M., Carroll, J. A., Hotchkiss, R. S., Belaaouaj, A., & Heinecke, J. W. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15021 · Cited by 225
Self-citation
Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
Hawkins, C. L., & Davies, M. J. (1999) · Biochemical Journal · doi:10.1042/bj3400539 · Cited by 201
Heparins Increase Endothelial Nitric Oxide Bioavailability by Liberating Vessel-Immobilized Myeloperoxidase
Baldus, S. E., Rudolph, V., Roiss, M., Ito, W. D., Rudolph, T. K., Eiserich, J. P., Sydow, K., Lau, D., Szöcs, K., Klinke, A., et al. (2006) · Circulation · doi:10.1161/circulationaha.105.590083 · Cited by 198
Regulation and function of endothelial glycocalyx layer in vascular diseases
Sieve, I., Münster-Kühnel, A. K., & Hilfiker‐Kleiner, D. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.09.002 · Cited by 199
The role of oxidative stress in atherosclerosis.
Vogiatzi, G., Tousoulis, D., & Stefanadis, C. (2009) · PubMed · Cited by 197
Pathophysiological role of neutrophils in acute myocardial infarction
Carbone, F., Nencioni, A., Mach, F., Vuilleumier, N., & Montecucco, F. (2013) · Thrombosis and Haemostasis · doi:10.1160/th13-03-0211 · Cited by 204
Glutathione-Related Antioxidant Defenses in Human Atherosclerotic Plaques
Lapenna, D., de Gioia, S., Ciofani, G., Mezzetti, A., Ucchino, S., Calafiore, A. M., Napolitano, A. M., Ilio, C. D., & Cuccurullo, F. (1998) · Circulation · doi:10.1161/01.cir.97.19.1930 · Cited by 197
Accumulation of Myeloperoxidase-Positive Neutrophils in Atherosclerotic Lesions in LDLR −/− Mice
van Leeuwen, M., Gijbels, M. J., Duijvestijn, A. M., Smook, M., Mj, V. D. G., Heeringa, P., de Winther, M. P. J., & Tervaert, J. W. C. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.154807 · Cited by 195
Humans With Atherosclerosis Have Impaired ABCA1 Cholesterol Efflux and Enhanced High-Density Lipoprotein Oxidation by Myeloperoxidase
Shao, B., Tang, C., Sinha, A., Mayer, P. S., Davenport, G. D., Brot, N., Oda, M. N., Zhao, X.-Q., & Heinecke, J. W. (2014) · Circulation Research · doi:10.1161/circresaha.114.303454 · Cited by 201
Self-citation
Atherosclerosis, oxidative stress, and antioxidant protection in endothelium-derived relaxing factor action
Keaney, J. F., & Vita, J. A. (1995) · Progress in Cardiovascular Diseases · doi:10.1016/s0033-0620(05)80003-9 · Cited by 196
Inflammatory biomarkers for predicting cardiovascular disease
Stoner, L. R., Lucero, A. A., Palmer, B. R., Jones, L. M., Young, J. M., & Faulkner, J. (2013) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2013.05.070 · Cited by 196
Molecular and Cellular Imaging of Atherosclerosis
Jaffer, F. A., Libby, P., & Weissleder, R. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2006.01.029 · Cited by 201
The effects of oxidative stress on the development of atherosclerosis
Khosravi, M., Poursaleh, A., Ghasempour, G., Shaikhnia, F., & Najafi, M. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0397 · Cited by 195
Identification of α-Chloro Fatty Aldehydes and Unsaturated Lysophosphatidylcholine Molecular Species in Human Atherosclerotic Lesions
Thukkani, A. K., McHowat, J., Hsu, F.-F., Brennan, M.-L., Hazen, S. L., & Ford, D. A. (2003) · Circulation · doi:10.1161/01.cir.0000104564.01539.6a · Cited by 194
Endothelial Dysfunction: From Molecular Mechanisms to Measurement, Clinical Implications, and Therapeutic Opportunities
Brocq, M. L. L., Leslie, S. J., Milliken, P. H., & Megson, I. L. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.2013 · Cited by 196
Phagocyte-derived reactive species: salvation or suicide?
Halliwell, B. B. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.07.005 · Cited by 192
Myeloperoxidase Impairs ABCA1-dependent Cholesterol Efflux through Methionine Oxidation and Site-specific Tyrosine Chlorination of Apolipoprotein A-I
Shao, B., Oda, M. N., Bergt, C., Fu, X., Green, P. S., Brot, N., Oram, J. F., & Heinecke, J. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600011200 · Cited by 191
Self-citation
The roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture
Teng, N., Maghzal, G. J., Talib, J., Rashid, I., Lau, A. K., & Stocker, R. (2016) · Redox Report · doi:10.1080/13510002.2016.1256119 · Cited by 198
When and why a water-soluble antioxidant becomes pro-oxidant during copper-induced low-density lipoprotein oxidation: a study using uric acid
Bagnati, M., Perugini, C., Cau, C., Bordone, R. P., Albano, E., & Bellomo, G. (1999) · Biochemical Journal · doi:10.1042/bj3400143 · Cited by 190
Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I
Shao, B., Cavigiolio, G., Brot, N., Oda, M. N., & Heinecke, J. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802025105 · Cited by 189
Self-citation
New insights on oxidative stress in the artery wall
STOCKER, R., & KEANEY, J. F. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01370.x · Cited by 188
Antibodies against adhesion molecules reduce apoptosis after transient middle cerebral artery occlusion in rat brain
Chopp, M., Li, Y., Jiang, N., Zhang, R. L., & Prostak, J. (1996) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199607000-00007 · Cited by 185
Oxidative stress and endothelial dysfunction in vascular disease
Pennathur, S., & Heinecke, J. W. (2007) · Current Diabetes Reports · doi:10.1007/s11892-007-0041-3 · Cited by 187
Self-citation
The Role of Oxidative Stress–Altered Lipoprotein Structure and Function and Microinflammation on Cardiovascular Risk in Patients with Minor Renal Dysfunction
Kaysen, G. A., & Eiserich, J. P. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000111744.00916.e6 · Cited by 185
Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid
Malle, E., Marsche, G., Arnhold, J., & Davies, M. J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.03.024 · Cited by 184
Myeloperoxidase: An Oxidative Pathway for Generating Dysfunctional High-Density Lipoprotein
Shao, B., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx9003775 · Cited by 189
Self-citation
Glycolaldehyde, a reactive intermediate for advanced glycation end products, plays an important role in the generation of an active ligand for the macrophage scavenger receptor.
Nagai, R., Matsumoto, K., Ling, X., Suzuki, H., Araki, T., & Horiuchi, S. (2000) · Diabetes · doi:10.2337/diabetes.49.10.1714 · Cited by 184
Fluorescent Detection of Hypochlorous Acid from Turn‐On to FRET‐Based Ratiometry by a HOCl‐Mediated Cyclization Reaction
Yuan, L., Lin, W., Xie, Y., Chen, B., & Song, J. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201101918 · Cited by 181
Role of myeloperoxidase and oxidant formation in the extracellular environment in inflammation-induced tissue damage
Hawkins, C. L., & Davies, M. J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.007 · Cited by 184
Attenuation of diet‐induced atherosclerosis in rabbits with a highly selective 15‐lipoxygenase inhibitor lacking significant antioxidant properties
Sendobry, S. M., Cornicelli, J. A., Welch, K. A., Bocan, T. M. A., Tait, B. D., Trivedi, B. K., Colbry, N. L., Dyer, R. D., Feinmark, S. J., & Daugherty, A. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701007 · Cited by 175
Self-citation
A highly specific BODIPY-based probe localized in mitochondria for HClO imaging
Cheng, G., Fan, J., Sun, W. C., Sui, K., Jin, X., Wang, J., & Peng, X. (2013) · The Analyst · doi:10.1039/c3an01152f · Cited by 174
Human Neutrophils Employ the Myeloperoxidase-Hydrogen Peroxide-Chloride System to Oxidize α-Amino Acids to a Family of Reactive Aldehydes
Hazen, S. L., d'Avignon, A., Anderson, M. M., Hsu, F., & Heinecke, J. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4997 · Cited by 174
Self-citation
The Oxidation of Lipoproteins by Monocytes-Macrophages
Chisolm, G. M., Hazen, S. L., Fox, P. L., & Cathcart, M. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.25959 · Cited by 174
Myeloperoxidase Targets Apolipoprotein A-I, the Major High Density Lipoprotein Protein, for Site-Specific Oxidation in Human Atherosclerotic Lesions
Shao, B., Pennathur, S., & Heinecke, J. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.337345 · Cited by 170
Self-citation
Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases
Baldus, S. E., Eiserich, J. P., Brennan, M., Jackson, R. M., Alexander, C. B., & Freeman, B. Α. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00993-0 · Cited by 170
The HDL proteome: a marker–and perhaps mediator–of coronary artery disease
Heinecke, J. W. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800097-jlr200 · Cited by 170
Self-citation
Expression of Human Myeloperoxidase by Macrophages Promotes Atherosclerosis in Mice
McMillen, T. S., Heinecke, J. W., & LeBoeuf, R. C. (2005) · Circulation · doi:10.1161/circulationaha.104.516278 · Cited by 168
Self-citation
Oxidative stress: new approaches to diagnosis and prognosis in atherosclerosis
Heinecke, J. W. (2003) · The American Journal of Cardiology · doi:10.1016/s0002-9149(02)03145-4 · Cited by 168
Self-citation
EVIDENCE OF INFLAMMATORY CELL INVOLVEMENT IN BRAIN ARTERIOVENOUS MALFORMATIONS
Chen, Y., Zhu, W. P., Bollen, A. W., Lawton, M. T., Barbaro, N. M., Dowd, C. F., Hashimoto, T. N., Yang, G., & Young, W. L. (2008) · Neurosurgery · doi:10.1227/01.neu.0000312339.62339.fc · Cited by 166
Mechanisms for Oxidative Stress in Diabetic Cardiovascular Disease
Pennathur, S., & Heinecke, J. W. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1595 · Cited by 165
Self-citation
An Allelic Association Implicates Myeloperoxidase in the Etiology of Acute Promyelocytic Leukemia
Reynolds, W. F., Chang, E. L., Douer, D., Ball, E. D., & Kanda, V. (1997) · Blood · doi:10.1182/blood.v90.7.2730 · Cited by 164
NON‐CORONARY HEART DISEASE IN DIALYSIS PATIENTS: Hypertrophy and Fibrosis in the Cardiomyopathy of Uremia—Beyond Coronary Heart Disease
Groß, M.-L., & Ritz, E. (2008) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2008.00454.x · Cited by 161
Citrate anticoagulation abolishes degranulation of polymorphonuclear cells and platelets and reduces oxidative stress during haemodialysis
Gritters, M., Grooteman, M. P. C., Schoorl, M. G., Schoorl, M., Bartels, P. C. M., Scheffer, P. G., Teerlink, T., Schalkwijk, C. G., Spreeuwenberg, M. D., & Nubé, M. J. (2005) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfi069 · Cited by 163
Enzyme-Sensitive Magnetic Resonance Imaging Targeting Myeloperoxidase Identifies Active Inflammation in Experimental Rabbit Atherosclerotic Plaques
Ronald, J. A., Chen, J. W., Chen, Y., Hamilton, A. M., Rodríguez, E., Reynolds, F., Hegele, R. A., Rogers, K. A., Querol, M., Bogdanov, A. A., Jr., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.813998 · Cited by 164
A ratiometric fluorescent probe for in situ quantification of basal mitochondrial hypochlorite in cancer cells
Hou, J., Li, K., Yang, J. P., Yu, K., Liao, Y.-X., Ran, Y.-Z., Liu, Y., Zhou, X., & Yu, X. (2015) · Chemical Communications · doi:10.1039/c5cc01217a · Cited by 161
Protein Tyrosine Nitration in Cytokine-activated Murine Macrophages
Pfeiffer, S., Lass, A., Schmidt, K., & Mayer, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100585200 · Cited by 160
Distinct Infiltration of Neutrophils in Lesion Shoulders in ApoE−/− Mice
Rotzius, P., Thams, S., Soehnlein, O., Kenne, E. M., Tseng, C., Björkström, N. K., Malmberg, K., Lindbom, L., & Eriksson, E. E. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090480 · Cited by 159
Albumin mediates the transcytosis of myeloperoxidase by means of caveolae in endothelial cells
Tiruppathì, C., Naqvi, T., Wu, Y.-B., Vogel, S. M., Minshall, R. D., & Malik, A. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401712101 · Cited by 158
Mitochondria-targeted colorimetric and fluorescent probes for hypochlorite and their applications for in vivo imaging
Hou, J., Wu, M., Li, K., Yang, J. P., Yu, K., Xie, Y., & Yu, X. (2014) · Chemical Communications · doi:10.1039/c4cc02673j · Cited by 157
Dysfunctional HDL as a Diagnostic and Therapeutic Target
Smith, J. D. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.179226 · Cited by 157
Hypochlorous acid as a precursor of free radicals in living systems
Panasenko, O. M., Gorudko, I. V., & Av, S. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130075 · Cited by 159
The principal eosinophil peroxidase product, HOSCN, is a uniquely potent phagocyte oxidant inducer of endothelial cell tissue factor activity: a potential mechanism for thrombosis in eosinophilic inflammatory states
Wang, J.-G., Mahmud, S. A., Thompson, J. A., Geng, J.-G., Key, N. S., & Slungaard, A. (2005) · Blood · doi:10.1182/blood-2005-05-2152 · Cited by 159
The Dual Role of Myeloperoxidase in Immune Response
Arnhold, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218057 · Cited by 172
On the Role of Vitamin C and Other Antioxidants in Atherogenesis and Vascular Dysfunction
Frei, B. B. (1999) · Proceedings of The Society for Experimental Biology and Medicine · doi:10.1046/j.1525-1373.1999.d01-136.x · Cited by 158
Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences
Ehrenshaft, M., Deterding, L. J., & Mason, R. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.003 · Cited by 158
Cardiovascular disease and nutrient antioxidants: Role of low‐density lipoprotein oxidation
Frei, B. B. (1995) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399509527689 · Cited by 157
The Reactions of Hypochlorous Acid, the Reactive Oxygen Species Produced by Myeloperoxidase, With Lipids
Spickett, C. M., Jerlich, A., Panasenko, O. M., Arnhold, J., Pitt, A. R., Stelmaszyńska, T., & Schaur, R. J. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_3944 · Cited by 154
Lipoprotein Modification and Macrophage Uptake: Role of Pathologic Cholesterol Transport in Atherogenesis
Miller, Y. I., Choi, S.-H., Fang, L., & Tsimikas, S. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-8622-8_8 · Cited by 155
Imaging of Myeloperoxidase in Mice by Using Novel Amplifiable Paramagnetic Substrates
Chen, J. W., Querol, M., Bogdanov, A. A., Jr., & Weissleder, R. (2006) · Radiology · doi:10.1148/radiol.2402050994 · Cited by 154
Hypochlorous Acid Generated by Myeloperoxidase Modifies Adjacent Tryptophan and Glycine Residues in the Catalytic Domain of Matrix Metalloproteinase-7 (Matrilysin)
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304739200 · Cited by 152
Self-citation
Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment
Brennan, M., & Hazen, S. L. (2003) · Current Opinion in Lipidology · doi:10.1097/00041433-200308000-00003 · Cited by 153
Antioxidant Properties of Carotenoids In Vitro and In Vivo
Kiokias, S. N., & Gordon, M. H. (2004) · Food Reviews International · doi:10.1081/fri-120037155 · Cited by 152
Modulation of inflammatory mediators and pparγand nfκb expression by pravastatin in response to lipoproteins in human monocytes in vitro
Zelvyté, I., Dominaitiene, R., Crisby, M., & Janciauskiene, S. M. (2002) · Pharmacological Research · doi:10.1006/phrs.2001.0922 · Cited by 152

Authors: Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W.
Affiliations: Washington University in St. Louis (US)
ORCID: Daugherty, A
Rateri, D L
Heinecke, J W
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1994-07-01
Volume: 94
Issue: 1
Pages: 437-444
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci117342
PMC: PMC296328
OpenAlex: W2028257547
Cited by: 1,269
References: 88
Citations by year: 2026: 5 · 2025: 15 · 2024: 24 · 2023: 28 · 2022: 39 · 2021: 32 · 2020: 48 · 2019: 47 · 2018: 61 · 2017: 40 · 2016: 40 · 2015: 48 · 2014: 42 · 2013: 50 · 2012: 45
FWCI: 10.54
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health (5r01hd029920-05)
National Heart, Lung, and Blood Institute (HL-17646)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01 HD-29920)
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: myeloperoxidase, lipoprotein oxidation, atherosclerosis, atherosclerotic plaque, macrophages, hypochlorous acid, oxidized lipoproteins, atherogenesis, heme enzymes, cholesterol clefts, vascular wall
MeSH terms: Arteriosclerosis, Free Radicals, Humans, Hypochlorous Acid, Immunohistochemistry, Lipoproteins, Macrophages, Peroxidase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks