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 501–600 of 999

Myeloperoxidase: a potential therapeutic target for coronary artery disease
Chaikijurajai, T., & Tang, W. H. W. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1762177 · Cited by 53
Estrogen, neutrophils and oxidation
Chiang, K. T., Parthasarathy, S., & Santanam, N. (2004) · Life Sciences · doi:10.1016/j.lfs.2004.04.035 · Cited by 53
The Oxidative Modification Hypothesis of Atherogenesis
Tsimikas, S., & Witztum, J. L. (2000) · Developments in cardiovascular medicine · doi:10.1007/978-1-4615-4649-8_4 · Cited by 53
Concentrations of iron correlate with the extent of protein, but not lipid, oxidation in advanced human atherosclerotic lesions
Stanley, N., Stadler, N., Woods, A. A., Bannon, P. G., & Davies, M. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.031 · Cited by 51
Substituent Effects in BODIPY in Live Cell Imaging
Mulay, S. V., Yudhistira, T., Choi, M., Kim, Y., Kim, J., Jang, Y. J., Jon, S., & Churchill, D. G. (2016) · Chemistry - An Asian Journal · doi:10.1002/asia.201601400 · Cited by 52
The HDL cholesterol/apolipoprotein A-I ratio: an indicator of cardiovascular disease
Rhee, E., Byrne, C. D., & Sung, K. (2017) · Current Opinion in Endocrinology Diabetes and Obesity · doi:10.1097/med.0000000000000315 · Cited by 52
Reappraisal of Inflammatory Biomarkers in Heart Failure
Chaikijurajai, T., & Tang, W. H. W. (2020) · Current Heart Failure Reports · doi:10.1007/s11897-019-00450-1 · Cited by 54
Role of reactive oxygen species and Bax in oxidized low density lipoprotein-induced apoptosis of human monocytes
Ermak, N., Lacour, B., Drüeke, T. B., & Vicca, S. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.12.052 · Cited by 52
Isolevuglandins, a novel class of isoprostenoid derivatives, function as integrated sensors of oxidant stress and are generated by myeloperoxidase in vivo
Poliakov, E., Brennan, M., MacPherson, J. C., Zhang, R., Sha, W., Narine, L., Salomon, R. G., & Hazen, S. L. (2003) · The FASEB Journal · doi:10.1096/fj.03-0086com · Cited by 52
Thematic review series: The Immune System and Atherogenesis. Cytokine regulation of macrophage functions in atherogenesis
Daugherty, A., Webb, N. R., Rateri, D. L., & King, V. L. (2005) · Journal of Lipid Research · doi:10.1194/jlr.r500009-jlr200 · Cited by 51
Self-citation
Human Low Density Lipoprotein as a Target of Hypochlorite Generated by Myeloperoxidase
Jerlich, A., Fabjan, J. S., Tschabuschnig, S., Smirnova, A. V., Horáková, Ľ., Hayn, M., Auer, H., Guttenberger, H., Leis, H., Tatzber, F., et al. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00439-5 · Cited by 52
Chlorinated Phospholipids and Fatty Acids: (Patho)physiological Relevance, Potential Toxicity, and Analysis of Lipid Chlorohydrins
Schröter, J., & Schiller, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8386362 · Cited by 51
Low-density lipoprotein modified by myeloperoxidase oxidants induces endothelial dysfunction
Abdo, A. I., Rayner, B. S., van Reyk, D. M., & Hawkins, C. L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.08.004 · Cited by 51
A phenanthroimidazole-based fluorescent probe for hypochlorous acid with high selectivity and its bio-imaging in living cells
Zhao, Y. F., Li, H., Xue, Y., Ren, Y., & Han, T. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.10.092 · Cited by 51
Neutrophils and neutrophil extracellular traps in oral health and disease
Kim, T. S., & Moutsopoulos, N. M. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01219-w · Cited by 59
Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival
Wei, Y., Liu, X., Peyton, K. J., Wang, H., Johnson, F. K., Johnson, R. A., & Durante, W. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00536.2008 · Cited by 51
Clonal analysis of hematopoietic progenitor cells in the zebrafish
Stachura, D. L., Svoboda, O., Lau, R. P., Balla, K. M., Zon, L. I., Bartůněk, P., & Traver, D. J. (2011) · Blood · doi:10.1182/blood-2011-01-331199 · Cited by 53
Selective and Absolute Quantification of Endogenous Hypochlorous Acid with Quantum-Dot Conjugated Microbeads
Yang, Y., Lu, H.-H., Wang, W.-T., & Liau, I. (2011) · Analytical Chemistry · doi:10.1021/ac202077x · Cited by 51
The nitroxide radical TEMPOL prevents obesity, hyperlipidaemia, elevation of inflammatory cytokines, and modulates atherosclerotic plaque composition in apoE−/− mice
Kim, C. H. J., Mitchell, J. B., Bursill, C. A., Sowers, A. L., Thetford, A., Cook, J. A., van Reyk, D. M., & Davies, M. J. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.03.012 · Cited by 50
Oxidation of LDL by recombinant human 15-lipoxygenase: evidence for alpha-tocopherol-dependent oxidation of esterified core and surface lipids
Upston, J. M., Neužil, J., & Stocker, R. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37468-x · Cited by 51
Immunohistochemical Distribution and Quantitative Biochemical Detection of Advanced Glycation End Products in Fetal to Adult Rats and in Rats with Streptozotocin-Induced Diabetes
Ling, X., Nagai, R., Sakashita, N., Takeya, M., Horiuchi, S., & Takahashi, K. (2001) · Laboratory Investigation · doi:10.1038/labinvest.3780294 · Cited by 50
Neutrophil-Mediated Cardiac Damage After Acute Myocardial Infarction: Significance of Defining a New Target Cell Type for Developing Cardioprotective Drugs
Kazzi, M. E., Rayner, B. S., Chami, B., Dennis, J. M., Thomas, S. R., & Witting, P. K. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7928 · Cited by 53
Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin
Av, S., Ageeva, K. V., Cherkalina, O. S., Pulina, M. O., Zakharova, E. T., Prozorovskii, V. N., Aksenov, D. V., Vasilyev, V. B., & Panasenko, O. M. (2010) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2010.02.002 · Cited by 50
Triggering of inflammatory response by myeloperoxidase-oxidized LDLAn oral presentation of the data was given before the Congress of the Beligian Society of Internal Medicine.
Boudjeltia, K. Z., Legssyer, I., Antwerpen, P. V., Lema-Kisoka, R., Babar, S., Moguilevsky, N., Delrée, P., Ducobu, J., Remacle, C., Vanhaeverbeek, M., et al. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-061 · Cited by 50
High plasma thiocyanate levels modulate protein damage induced by myeloperoxidase and perturb measurement of 3-chlorotyrosine
Talib, J., Pattison, D. I., Harmer, J. A., Celermajer, D. S., & Davies, M. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.018 · Cited by 49
Hypochlorite-modified high-density lipoprotein acts as a sink for myeloperoxidase in vitro
Marsche, G., Furtmüller, P. G., Obinger, C., Sattler, W., & Malle, E. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn051 · Cited by 49
Vitamin C fails to protect amino acids and lipids from oxidation during acute inflammation
Gaut, J. P., Belaaouaj, A., Byun, J., Roberts, L. J., Maeda, N., Frei, B., & Heinecke, J. W. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.013 · Cited by 48
Self-citation
Metabolomics and ischaemic heart disease
Rasmiena, A. A., Ng, T. W., & Meikle, P. J. (2012) · Clinical Science · doi:10.1042/cs20120268 · Cited by 48
Monoclonal antibodies against LDL progressively oxidized by myeloperoxidase react with ApoB-100 protein moiety and human atherosclerotic lesions
Moguilevsky, N., Boudjeltia, K. Z., Babar, S., Delrée, P., Legssyer, I., Carpentier, Y., Vanhaeverbeek, M., & Ducobu, J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.220 · Cited by 48
The mechanism of the hypochlorite‐induced lipid peroxidation
Panasenko, O. M. (1997) · BioFactors · doi:10.1002/biof.5520060212 · Cited by 48
Bifunctional near-infrared fluorescent probe for the selective detection of bisulfite and hypochlorous acid in food, water samples and in vivo
Shang, Z., Meng, Q., Zhang, R., & Zhang, Z. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341783 · Cited by 45
Assessment of Myeloperoxidase Activity by the Conversion of Hydroethidine to 2-Chloroethidium
Maghzal, G. J., Cergol, K. M., Shengule, S. R., Suarna, C., Newington, D. L., Kettle, A. J., Payne, R. J., & Stocker, R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.539486 · Cited by 47
Contribution of Myeloperoxidase to Smoking-dependent Vascular Inflammation
Rudolph, T. K., Rudolph, V., & Baldus, S. E. (2008) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200807-063th · Cited by 46
Dual Functionality of Myeloperoxidase in Rotenone-Exposed Brain-Resident Immune Cells
Chang, C. Y., Song, M. J., Jeon, S., Yoon, H. J., Lee, D., Kim, I.-H., Suk, K., Choi, D., & Park, E. J. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.04.033 · Cited by 47
Dysfunctional High-Density Lipoprotein: An Innovative Target for Proteomics and Lipidomics
Salazar, J. J., Olivar, L. C., Ramos, E., Chávez-Castillo, M., Rojas, J., & Bermúdez, V. (2015) · Cholesterol · doi:10.1155/2015/296417 · Cited by 50
Preventing Protein Oxidation with Sugars: Scavenging of Hypohalous Acids by 5-Selenopyranose and 4-Selenofuranose Derivatives
Storkey, C., Pattison, D. I., White, J. M., Schiesser, C. H., & Davies, M. J. (2012) · Chemical Research in Toxicology · doi:10.1021/tx3003593 · Cited by 50
Mono- or di- naphthalimides as fluorophore to detect hypochlorous acid (HOCl) by ratiometric fluorescent signal and their biological application
Zhang, H., Huo, F., Zhang, Y., & Yin, C. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.04.155 · Cited by 47
The reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chloride
Abu‐Soud, H. M., Maitra, D., Byun, J., Souza, C. E. A., Banerjee, J., Saed, G. M., Diamond, M. P., Andreana, P. R., & Pennathur, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.496 · Cited by 47
Elevated levels of protein-bound p-hydroxyphenylacetaldehyde, an amino-acid-derived aldehyde generated by myeloperoxidase, are present in human fatty streaks, intermediate lesions and advanced atherosclerotic lesions
Hazen, S. L., Gaut, J. P., Crowley, J. R., Hsu, F., & Heinecke, J. W. (2000) · Biochemical Journal · doi:10.1042/bj3520693 · Cited by 47
Self-citation
Fragmentation of extracellular matrix by hypochlorous acid
Woods, A. A., & Davies, M. J. (2003) · Biochemical Journal · doi:10.1042/bj20030715 · Cited by 45
Critical evaluation of plasma and LDL oxidant-trapping potential in hemodialysis patients
Nguyen‐Khoa, T., Massy, Z. A., Witko‐Sarsat, V., Thévenin, M., Touam, M., Lambrey, G., Lacour, B., Drüeke, T. B., & Descamps‐Latscha, B. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00565.x · Cited by 46
Enhanced coronary vasoconstriction to oxidative stress product, 8-epi-prostaglandinF2α, in experimental hypercholesterolemia
Wilson, S. H. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00225-4 · Cited by 46
The Nitric Oxide Congener Nitrite Inhibits Myeloperoxidase/H2O2/ Cl−-mediated Modification of Low Density Lipoprotein
Carr, A. C., & Frei, B. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009082200 · Cited by 46
Hypochlorite-Modified LDL: Chemotactic Potential and Chemokine Induction in Human Monocytes
Woenckhaus, C., Kaufmann, A. M., Bußfeld, D., Gemsa, D., Sprenger, H., & Gröne, H. (1998) · Clinical Immunology and Immunopathology · doi:10.1006/clin.1997.4453 · Cited by 46
Discovery of AZD4831, a Mechanism-Based Irreversible Inhibitor of Myeloperoxidase, As a Potential Treatment for Heart Failure with Preserved Ejection Fraction
Inghardt, T., Antonsson, T., Ericsson, C., Hovdal, D., Johannesson, P., Johansson, C. A., Jurva, U., Kajanus, J., Kull, B., Michaëlsson, E., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02141 · Cited by 46
A ratiometric fluorescent probe for highly selective and sensitive detection of hypochlorite based on the oxidation of N-alkylpyridinium
Wang, L., Long, L., Zhou, L., Wu, Y., Zhang, C., Han, Z., Wang, J., & Da, Z. (2014) · RSC Advances · doi:10.1039/c4ra10633d · Cited by 45
Comparative reactivity of the myeloperoxidase-derived oxidants hypochlorous acid and hypothiocyanous acid with human coronary artery endothelial cells
Lloyd, M. M., Grima, M. A., Rayner, B. S., Hadfield, K. A., Davies, M. J., & Hawkins, C. L. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.007 · Cited by 45
Chlorinated lipid species in activated human neutrophils: lipid metabolites of 2-chlorohexadecanal
Anbukumar, D. S., Shornick, L. P., Albert, C. J., Steward, M., Zoeller, R. A., Neumann, W. L., & Ford, D. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m003673 · Cited by 45
Binding of myeloperoxidase to the extracellular matrix of smooth muscle cells and subsequent matrix modification
Cai, H., Chuang, C. Y., Hawkins, C. L., & Davies, M. J. (2020) · Scientific Reports · doi:10.1038/s41598-019-57299-6 · Cited by 45
Nanotechnology for Targeted Therapy of Atherosclerosis
Nasr, S. H., & Huang, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.755569 · Cited by 47
Glycation of low‐density lipoprotein results in the time‐dependent accumulation of cholesteryl esters and apolipoprotein B‐100 protein in primary human monocyte‐derived macrophages
Brown, B. E., Rashid, I., van Reyk, D. M., & Davies, M. J. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05699.x · Cited by 47
Comparison between copper-mediated and hypochlorite-mediated modifications of human low density lipoproteins evaluated by protein carbonyl formation
Yan, L., Lodge, J. K., Traber, M. G., Matsugo, S., & Packer, L. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37223-0 · Cited by 44
Chronic Renal Dysfunction as an Independent Risk Factor for the Development of Cardiovascular Disease
Varma, R., Garrick, R., McClung, J. A., & Frishman, W. H. (2005) · Cardiology in Review · doi:10.1097/01.crd.0000132600.45876.d0 · Cited by 44
Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I
Chan, G. K. L., Witkowski, A., Gantz, D., Zhang, T. O., Zanni, M. T., Jayaraman, S., & Cavigiolio, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.630442 · Cited by 44
A genotypic association implicates myeloperoxidase in the progression of hepatic fibrosis in chronic hepatitis C virus infection
Reynolds, W. F., Patel, K., Pianko, S., Blatt, L. M., Nicholas, J. J., & McHutchison, J. G. (2002) · Genes and Immunity · doi:10.1038/sj.gene.6363880 · Cited by 44
Polymorphic metabolizing genes and susceptibility to atherosclerosis among cigarette smokers
Salama, S. A., Au, W. W., Hunter, G. C., Sheahan, R. G., Badary, O. A., Abdel‐Naim, A. B., & Hamada, F. M. A. (2002) · Environmental and Molecular Mutagenesis · doi:10.1002/em.10106 · Cited by 44
Reagent or myeloperoxidase-generated hypochlorite affects discrete regions in lipid-free and lipid-associated human apolipoprotein A-I
Bergt, C., Oettl, K., Keller, W., Andreae, F., Leis, H. J., Malle, E., & Sattler, W. (2000) · Biochemical Journal · doi:10.1042/bj3460345 · Cited by 44
Assessing human health risk to endocrine disrupting chemicals: a focus on prenatal exposures and oxidative stress
Neier, K. E., Marchlewicz, E. H., Dolinoy, D. C., & Padmanabhan, V. (2015) · Endocrine Disruptors · doi:10.1080/23273747.2015.1069916 · Cited by 44
Neutrophil count improves the GRACE risk score prediction of clinical outcomes in patients with ST-elevation myocardial infarction
Zhang, S., Wan, Z., Zhang, Y., Fan, Y., Gu, W., Li, F., Meng, L., Zeng, X., Han, D., & Li, X. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.06.035 · Cited by 43
Hypochlorous Acid-Induced Heme Degradation from Lactoperoxidase as a Novel Mechanism of Free Iron Release and Tissue Injury in Inflammatory Diseases
Souza, C. E. A., Maitra, D., Saed, G. M., Diamond, M. P., Moura, A. A., Pennathur, S., & Abu‐Soud, H. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027641 · Cited by 43
Proatherogenic modification of LDL by surface-bound myeloperoxidase
Av, S., Kostevich, V. A., Runova, O. L., Gorudko, I. V., Vasilyev, V. B., Sn, C., & Panasenko, O. M. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2014.02.006 · Cited by 43
Myeloperoxidase inhibition in mice alters atherosclerotic lesion composition
Flach, R. J. R., Su, C., Bollinger, E., Cortes, C., Robertson, A. W., Opsahl, A., Coskran, T., Maresca, K. P., Keliher, E. J., Yates, P. D., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214150 · Cited by 43
Modulation of hypochlorous acid (HOCl) induced damage to vascular smooth muscle cells by thiocyanate and selenium analogues
Flouda, K., Gammelgaard, B., Davies, M. J., & Hawkins, C. L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101873 · Cited by 43
Anti-inflammatory agents and monoHER protect against DOX-induced cardiotoxicity and accumulation of CML in mice
Bruynzeel, A. M. E., Hassan, M. A. A. E., Schalkwijk, C., Berkhof, J. H., Bast, A., Niessen, H. W. M., & van der Vijgh, W. J. F. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603640 · Cited by 43
Myeloperoxidase polymorphisms in brain infarction. Association with infarct size and functional outcome
Hoy, A., Leininger‐Muller, B., Poirier, O., Siest, G., Gautier, M., Elbaz, A., Amarenco, P., & Visvikis‐Siest, S. (2003) · Atherosclerosis · doi:10.1016/s0021-9150(02)00041-2 · Cited by 43
Iron and LDL‐oxidation in atherogenesis.
Yuan, X., & Brunk, U. T. (1998) · Apmis · doi:10.1111/j.1699-0463.1998.tb00229.x · Cited by 43
Comparison of HOCl traps with myeloperoxidase inhibitors in prevention of low density lipoprotein oxidation
Jerlich, A., Fritz, G., Kharrazi, H., Hammel, M., Tschabuschnig, S., Glatter, O., & Schaur, R. J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00112-6 · Cited by 43
Myeloperoxidase Levels and Its Product 3-Chlorotyrosine Predict Chronic Kidney Disease Severity and Associated Coronary Artery Disease
Afshinnia, F., Zeng, L., Byun, J., Gadegbeku, C. A., Magnone, M. C., Whatling, C., Valastro, B., Kretzler, M., Pennathur, S., & Michigan Kidney Translational Core CPROBE Investigator Group (2017) · American Journal of Nephrology · doi:10.1159/000477766 · Cited by 43
Heart Fatty Acid-Binding Protein Offers Similar Diagnostic Performance to High-Sensitivity Troponin T in Emergency Room Patients Presenting With Chest Pain
Inoue, K., Suwa, S., Ohta, H., Itoh, S., Maruyama, S., Masuda, N., Sugita, M., & Daida, H. (2011) · Circulation Journal · doi:10.1253/circj.cj-11-0598 · Cited by 42
Kinetics of 3-Chlorotyrosine Formation and Loss due to Hypochlorous Acid and Chloramines
Curtis, M. P., Hicks, A. J., & Neidigh, J. W. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100380d · Cited by 43
A mitochondria-targeted near-infrared fluorescent probe with a large Stokes shift for real-time detection of hypochlorous acid
Jiao, X., Huang, K., He, S., Liu, C., Zhao, L., & Zeng, X. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob02583e · Cited by 42
HMG-CoA reductase inhibitor stabilizes rabbit atheroma by increasing basal NO and decreasing superoxide
Thakur, N. K., Hayashi, T., Sumi, D., Kano, H., Tsunekawa, T., & Iguchi, A. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.1.h75 · Cited by 42
Myeloperoxidase genetic polymorphisms modulate human neutrophil enzyme activity: Genetic determinants for atherosclerosis?
Chevrier, I., Trégouët, D., Massonnet-Castel, S., Beaune, P. H., & Loriot, M. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.10.012 · Cited by 42
Targeted Imaging in Atherosclerosis
Li, J., Wang, K., Pan, W., Li, N., & Tang, B. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02644 · Cited by 41
Effects of timed administration of doxycycline or methylprednisolone on post-myocardial infarction inflammation and left ventricular remodeling in the rat heart
Garcia, R. A., Go, K. V., & Villarreal, F. J. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-9379-0 · Cited by 41
A High Throughput Biochemical Fluorometric Method for Measuring Lipid Peroxidation in HDL
Kelesidis, T., Roberts, C. K., Huynh, D., Martínez-Maza, O., Currier, J. S., Reddy, S. T., & Yang, O. O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111716 · Cited by 41
Hypochlorite-promoted inhibition of photo-induced electron transfer in phenothiazine–borondipyrromethene donor–acceptor dyad: a cost-effective and metal-free “turn-on” fluorescent chemosensor for hypochlorite
Soni, D., Gangada, S., Duvva, N., Roy, T. K., Nimesh, S., Arya, G., Giribabu, L., & Chitta, R. K. (2017) · New Journal of Chemistry · doi:10.1039/c7nj00516d · Cited by 41
Bornyl acetate suppresses ox-LDL-induced attachment of THP-1 monocytes to endothelial cells
Lin, Y., Liu, J., Li, Y., & Qi, G. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.03.152 · Cited by 41
Hypochlorous acid-modified extracellular matrix contributes to the behavioral switching of human coronary artery smooth muscle cells
Cai, H., Chuang, C. Y., Vanichkitrungruang, S., Hawkins, C. L., & Davies, M. J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.044 · Cited by 41
Role of Lysine during Protein Modification by HOCl and HOBr: Halogen-Transfer Agent or Sacrificial Antioxidant?
Sivey, J. D., Howell, S. C., Bean, D. J., McCurry, D. L., Mitch, W. A., & Wilson, C. J. (2013) · Biochemistry · doi:10.1021/bi301523s · Cited by 41
Association of the serum myeloperoxidase/high-density lipoprotein particle ratio and incident cardiovascular events in a multi-ethnic population: Observations from the Dallas Heart Study
Khine, H., Teiber, J. F., Haley, R. W., Khera, A., Ayers, C. R., & Rohatgi, A. K. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.06.007 · Cited by 41
Hypochlorite modification of high density lipoprotein: effects on cholesterol efflux from J774 macrophages
Bergt, C., Reicher, H., Malle, E., & Sattler, W. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00677-8 · Cited by 41
LDL oxidation by activated monocytes: characterization of the oxidized LDL and requirement for transition metal ions
Xing, X., Baffic, J., & Sparrow, C. P. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32475-5 · Cited by 40
Differential microRNA response to a high-cholesterol, high-fat diet in livers of low and high LDL-C baboons
Karere, G. M., Glenn, J. P., VandeBerg, J. L., & Cox, L. A. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-320 · Cited by 40
Transformed target cell-derived superoxide anions drive apoptosis induction by myeloperoxidase
Engelmann, I., Dormann, S., Sarán, M., & Bauer, G. (2000) · Redox Report · doi:10.1179/135100000101535762 · Cited by 40
Myeloperoxidase in Cardiovascular Disease
Koeth, R., Haselden, V. N., & Tang, W. H. W. (2013) · Advances in clinical chemistry · doi:10.1016/b978-0-12-800096-0.00001-9 · Cited by 40
Emerging Associations Between Neutrophils, Atherosclerosis, and Psoriasis
Sanda, G. E., Belur, A. D., Teague, H., & Mehta, N. N. (2017) · Current Atherosclerosis Reports · doi:10.1007/s11883-017-0692-8 · Cited by 40
Highly sensitive and selective “off-on” fluorescent sensing platform for ClO− in water based on silicon quantum dots coupled with nanosilver
Liu, L., Zhu, G., Zeng, W. D., Lv, B., & Yi, Y. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01597-5 · Cited by 40
A ratiometric flavone-based fluorescent probe for hypochlorous acid detection with large Stokes shift and long-wavelength emission
He, L., Zhang, Y., Xiong, H., Wang, J., Geng, Y., Wang, B., Wang, Y., Yang, Z., & Song, X. (2019) · Dyes and Pigments · doi:10.1016/j.dyepig.2019.03.029 · Cited by 40
Non-Canonical Functions of Myeloperoxidase in Immune Regulation, Tissue Inflammation and Cancer
Lockhart, J., & Sumagin, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012250 · Cited by 43
Update on the Role of Neutrophils in Atherosclerotic Plaque Vulnerability
Carbone, F., Mach, F., & Montecucco, F. (2015) · Current Drug Targets · doi:10.2174/1389450115666141110093013 · Cited by 39
Myeloperoxidase-mediated protein lysine oxidation generates 2-aminoadipic acid and lysine nitrile in vivo
Lin, H., Levison, B. S., Buffa, J. A., Huang, Y. R., Fu, X., Wang, Z., Gogonea, V., DiDonato, J. A., & Hazen, S. L. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.006 · Cited by 39
A new ratiometric fluorescent probe for sensing HOCl based on TBET in real time
Song, G., Ma, H., Luo, J., Cao, X., & Zhao, B. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.09.022 · Cited by 38
UiO-68-PT MOF-Based Sensor and Its Mixed Matrix Membrane for Detection of HClO in Water
Li, Q.-Y., Li, Y.-A., Guan, Q., Li, W., Dong, X., & Dong, Y. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01032 · Cited by 39
Potential role of plasma myeloperoxidase level in predicting long-term outcome of acute myocardial infarction.
Kaya, M. G., Yalçin, R., Okyay, K., Poyraz, F., Bayraktar, N., Paşaoğlu, H., Boyacı, B., & Çengel, A. (2012) · Europe PMC (PubMed Central) · Cited by 39
Protective Effect of Infliximab on Ischemia/Reperfusion-Induced Damage in Rat Kidney
Taşdemir, C., Taşdemir, S., Vardı, N., Ateş, B., Parlakpınar, H., Katı, B., Karaaslan, M. G., & Acet, A. (2012) · Renal Failure · doi:10.3109/0886022x.2012.717490 · Cited by 39
Probucol Protects against Hypochlorite-induced Endothelial Dysfunction
Witting, P. K., Wu, B. J., Raftery, M. J., Southwell‐Keely, P. T., & Stocker, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414256200 · Cited by 39
Formation of Active Oxygen Species and Lipid Peroxidation Induced by Hypochlorite
Noguchi, N., Nakada, A., Itoh, Y., Watanabe, A., & Niki, E. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2689 · Cited by 39
Characterization of peroxynitrite-oxidized low density lipoprotein binding to human CD36
Guy, R. A., Maguire, G. F., Crandall, I., Connelly, P. W., & Kain, K. C. (2001) · Atherosclerosis · doi:10.1016/s0021-9150(00)00524-4 · Cited by 39
Coronary plaque injury triggers neutrophil activation in patients with coronary artery disease
Rudolph, V., Steven, D., Gehling, U. M., Goldmann, B. U., Rudolph, T. K., Friedrichs, K. P., Meinertz, T., Heitzer, T. A., & Baldus, S. E. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.004 · Cited by 39

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