Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid
Abstract
Free radicals or reactive oxygen species are thought to contribute to the pathology of many diseases. These include inflammatory conditions, where neutrophils accumulate in large numbers and are stimulated to produce superoxide and other reactive oxidants. Hypochlorous acid (HOCl), produced by myeloperoxidase-catalysed oxidation of chloride by hydrogen peroxide, is the major strong oxidant generated by these cells. Neutrophil-mediated injury may also be important in toxicology when an initial insult is followed by an inflammatory response. It is important to characterize the inflammatory component of such injury and the extent to which it involves reactive oxidants. On the one hand, this requires an understanding of how neutrophil oxidants react with cells and tissue constituents. On the other, specific biomarkers are needed so that oxidative damage can be quantified in clinical material and related to disease severity. This presentation considers biologically relevant reactions of HOCl and the biomarker assays that can be applied to probing the pathological role of myeloperoxidase and its products.
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VAS2870 and VAS3947 do not have a noticeable effect on XO- or eNOS-dependent ROS production, so they can be considered specific pan-NOX inhibitors.
“These inhibitors do not have a noticeable effect on XO- or eNOS-dependent ROS production, so they can be considered specific pan-NOX inhibitors.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1016]
Cites
Inflammation. Basic principles and clinical correlates
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90156-x · Cited by 2,388 · see citing works
Hazen, S. L., & Heinecke, J. W. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119379 · Cited by 842 · see citing works
Protein Carbonyl Measurement by a Sensitive ELISA Method
Buss, H., Chan, T., Sluis, K. B., Domigan, N. M., & Winterbourn, C. C. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00104-4 · Cited by 687 · see citing works
Self-citationInflammation: Basic Principles and Clinical Correlates
Ehrlich, G. E. (2000) · JAMA · doi:10.1001/jama.283.1.123 · Cited by 624 · see citing works
Presence of hypochlorite-modified proteins in human atherosclerotic lesions.
Hazell, L. J., Arnold, L., Flowers, D., Waeg, G., Malle, E., & Stocker, R. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118576 · Cited by 592 · see citing works
Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463 · see citing works
Self-citationPeskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 335 · see citing works
Self-citationChlorination of Tyrosyl Residues in Peptides by Myeloperoxidase and Human Neutrophils
Domigan, N. M., Charlton, T. S., Duncan, M. W., Winterbourn, C. C., & Kettle, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16542 · Cited by 329 · see citing works
Self-citationHazell, L. J., van den Berg, J. J. M., & Stocker, R. (1994) · Biochemical Journal · doi:10.1042/bj3020297 · Cited by 267 · see citing works
Chlorohydrin Formation From Unsaturated Fatty Acids Reacted With Hypochlorous Acid
Winterbourn, C. C., van den Berg, J. J. M., Roitman, E., & Kuypers, F. A. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90609-z · Cited by 258 · see citing works
Self-citationMyeloperoxidase and protein oxidation in cystic fibrosis
van der Vliet, A., Nguyen, M. N., Shigenaga, M. K., Eiserich, J. P., Marelich, G. P., & Cross, C. E. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l537 · Cited by 203 · see citing works
Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
Kettle, A. J. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01494-2 · Cited by 188 · see citing works
Winterbourn, C. C., & Brennan, S. O. (1997) · Biochemical Journal · doi:10.1042/bj3260087 · Cited by 146 · see citing works
Self-citationHeinecke, J. W., Li, W., Mueller, D. M., Bohrer, A., & TURK, J. W. (1994) · Biochemistry · doi:10.1021/bi00199a041 · Cited by 141 · see citing works
Immunological evidence for hypochlorite-modified proteins in human kidney.
Malle, E., Woenckhaus, C., Waeg, G., Esterbauer, H., Gröne, E. F., & Gröne, H. (1997) · Europe PMC (PubMed Central) · Cited by 127 · see citing works
Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS
Jerlich, A., Pitt, A. R., Schaur, R. J., & Spickett, C. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00273-7 · Cited by 110 · see citing works
Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
Carr, A. C., & Winterbourn, C. C. (1997) · Biochemical Journal · doi:10.1042/bj3270275 · Cited by 108 · see citing works
Self-citationPullar, J. M., Winterbourn, C. C., & Vissers, M. C. M. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.4.h1505 · Cited by 102 · see citing works
Self-citationVissers, M. C. M., Pullar, J. M., & Hampton, M. B. (1999) · Biochemical Journal · doi:10.1042/bj3440443 · Cited by 95 · see citing works
Heinecke, J. W., Hsu, F., Crowley, J. R., Hazen, S. L., Leeuwenburgh, C., Mueller, D. M., RASMUSSEN, J. E., & TURK, J. W. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00121-4 · Cited by 94 · see citing works
Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102088200 · Cited by 91 · see citing works
Self-citationHypochlorous Acid Stimulation of the Mitogen-Activated Protein Kinase Pathway Enhances Cell Survival
Midwinter, R. G., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2530 · Cited by 90 · see citing works
Self-citationCarr, A. C., Vissers, M. C. M., Domigan, N. M., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747122 · Cited by 75 · see citing works
Self-citationOn the Irreversible Destruction of Reduced Nicotinamide Nucleotides by Hypohalous Acids
Prütz, W. A., Kissner, R., Koppenol, W. H., & Rüegger, H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1914 · Cited by 67 · see citing works
Chapman, A., Senthilmohan, R., Winterbourn, C. C., & Kettle, A. J. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1744 · Cited by 65 · see citing works
Self-citationVile, G. F., Rothwell, L. A., & Kettle, A. J. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1706 · Cited by 50 · see citing works
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Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,561 · see citing works
Hydrogen acts as a therapeutic antioxidant by selectively reducing cytotoxic oxygen radicals
Ohsawa, I., Ishikawa, M., Takahashi, K., Watanabe, M., Nishimaki, K., Yamagata, K., Katsura, K., Katayama, Y., Asoh, S., & Ohta, S. (2007) · Nature Medicine · doi:10.1038/nm1577 · Cited by 2,572 · see citing works
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Role of vitamin E as a lipid-soluble peroxyl radical scavenger: in vitro and in vivo evidence
Niki, E. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.022 · Cited by 677 · see citing works
Yuan, L., Wang, L., Agrawalla, B. K., Park, S. J., Zhu, H., Balasubramaniam, S., Peng, J., Xu, Q., & Chang, Y. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b00042 · Cited by 557 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Understanding oxidants and antioxidants: Classical team with new players
Ali, S. S., Ahsan, H., Zia, M. K., Siddiqui, T., & Khan, F. H. (2020) · Journal of Food Biochemistry · doi:10.1111/jfbc.13145 · Cited by 497 · see citing works
TRPA1 is a major oxidant sensor in murine airway sensory neurons
Bessac, B. F., Sivula, M., von Hehn, C. A., Escalera, J., Cohn, L. E., & Jordt, S. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34192 · Cited by 451 · see citing works
Takaki, A., Kawai, D., & Yamamoto, K. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141020704 · Cited by 452 · see citing works
Myeloperoxidase mediates neutrophil activation by association with CD11b/CD18 integrins
Lau, D., Mollnau, H., Eiserich, J. P., Freeman, B. Α., Daiber, A., Gehling, U. M., Brümmer, J., Rudolph, V., Münzel, T. F., Heitzer, T. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405193102 · Cited by 431 · see citing works
Breathtaking TRP Channels: TRPA1 and TRPV1 in Airway Chemosensation and Reflex Control
Bessac, B. F., & Jordt, S. (2008) · Physiology · doi:10.1152/physiol.00026.2008 · Cited by 431 · see citing works
Winterbourn, C. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.004 · Cited by 420 · see citing works
Self-citationMyeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
Davies, M. J. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-006fr · Cited by 412 · see citing works
Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700339200 · Cited by 393 · see citing works
Self-citationRedox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 357 · see citing works
Hydrogen sulphide: a novel inhibitor of hypochlorous acid-mediated oxidative damage in the brain?
Whiteman, M., Cheung, N. S., Zhu, Y. Z., Chu, S. H., Siau, J. L., Wong, B., Armstrong, J. S., & Moore, P. K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.110 · Cited by 333 · see citing works
The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease
Davies, M. J., & Hawkins, C. L. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8030 · Cited by 332 · see citing works
Ohta, S. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211797052664 · Cited by 299 · see citing works
Zhao, T., Wu, W., Sui, L., Huang, Q., Nan, Y., Liu, J., & Ai, K. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.06.006 · Cited by 270 · see citing works
Mangerich, A., Knutson, C. G., Parry, N. M., Muthupalani, S., Ye, W., Prestwich, E. G., Liang, C., McFaline‐Figueroa, J. L., Mobley, M. W., Ge, Z., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207829109 · Cited by 243 · see citing works
Oxidant/Antioxidant Balance in Animal Nutrition and Health: The Role of Protein Oxidation
Celi, P., & Gabai, G. (2015) · Frontiers in Veterinary Science · doi:10.3389/fvets.2015.00048 · Cited by 226 · see citing works
van Golen, R. F., van Gulik, T. M., & Heger, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.013 · Cited by 221 · see citing works
Gałecki, P., Szemraj, J., Bieńkiewicz, M., Florkowski, A., & Gałecka, E. (2009) · Pharmacological Reports · doi:10.1016/s1734-1140(09)70084-2 · Cited by 214 · see citing works
Fu, Y., Ito, M., Fujita, Y., Ito, M., Ichihara, M., Masuda, A., Suzuki, Y., Maesawa, S., Kajita, Y., Hirayama, M., et al. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.02.016 · Cited by 214 · see citing works
Ohta, S. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.05.006 · Cited by 202 · see citing works
Myeloperoxidase: A Leukocyte-Derived Protagonist of Inflammation and Cardiovascular Disease
Nußbaum, C., Klinke, A., Adam, M., Baldus, S. E., & Sperandio, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4783 · Cited by 196 · see citing works
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 · see citing works
Neutrophil-Mediated Regulation of Innate and Adaptive Immunity: The Role of Myeloperoxidase
Odobasic, D., Kitching, A. R., & Holdsworth, S. R. (2016) · Journal of Immunology Research · doi:10.1155/2016/2349817 · Cited by 191 · see citing works
Surviving Reactive Chlorine Stress: Responses of Gram-Negative Bacteria to Hypochlorous Acid
Nizer, W. S. D. C., Inkovskiy, V., & Overhage, J. (2020) · Microorganisms · doi:10.3390/microorganisms8081220 · Cited by 196 · see citing works
Reactive Oxygen Species and Their Involvement in Red Blood Cell Damage in Chronic Kidney Disease
Gwoździński, K., Pieniążek, A., & Gwoździński, Ł. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6639199 · Cited by 195 · see citing works
Ilié, M., Hofman, V., Ortholan, C., Bonnetaud, C., Coëlle, C., Mouroux, J., & Hofman, P. M. (2011) · Cancer · doi:10.1002/cncr.26456 · Cited by 179 · see citing works
Pattison, D. I., Davies, M. J., & Hawkins, C. L. (2012) · Free Radical Research · doi:10.3109/10715762.2012.667566 · Cited by 175 · see citing works
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810735 · Cited by 166 · see citing works
Zhu, B., Liu, W., Zhang, M., Wang, Y., Liu, C., Wang, Z., Duan, Q., & Jia, P. (2018) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2018.02.023 · Cited by 163 · see citing works
Bench-to-bedside review: Sepsis - from the redox point of view
Andrades, M. É., Morina, A., Spasić, S. D., & Spasojević, I. (2011) · Critical Care · doi:10.1186/cc10334 · Cited by 158 · see citing works
Inflammatory pathways in the early steps of colorectal cancer development
Mariani, F. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i29.9716 · Cited by 156 · see citing works
Hemoglobin-based oxygen carriers: from mechanisms of toxicity and clearance to rational drug design
Buehler, P. W., D’Agnillo, F., & Schaer, D. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.07.006 · Cited by 142 · see citing works
Gałecki, P., Gałecka, E., Maes, M., Chamielec, M., Orzechowska, A., Bobińska, K., Lewiński, A., & Szemraj, J. (2012) · Journal of Affective Disorders · doi:10.1016/j.jad.2012.01.016 · Cited by 141 · see citing works
Biomarkers for Duchenne muscular dystrophy: myonecrosis, inflammation and oxidative stress
Grounds, M. D., Terrill, J. R., Al-Mshhdani, B. A., Duong, M. N., Radley‐Crabb, H. G., & Arthur, P. G. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.043638 · Cited by 132 · see citing works
Myeloperoxidase Inactivates TIMP-1 by Oxidizing Its N-terminal Cysteine Residue
Wang, Y., Rosen, H., Madtes, D. K., Shao, B., Martin, T. R., Heinecke, J. W., & Fu, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704894200 · Cited by 132 · see citing works
Gałecki, P., Szemraj, J., Bieńkiewicz, M., Zboralski, K., & Gałecka, E. (2009) · Human Psychopharmacology: Clinical and Experimental · doi:10.1002/hup.1014 · Cited by 124 · see citing works
What Are the Plasma Targets of the Oxidant Hypochlorous Acid? A Kinetic Modeling Approach
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800372d · Cited by 123 · see citing works
Whiteman, M., Rose, P. E., Siau, J. L., Cheung, N. S., Tan, G. S., Halliwell, B. B., & Armstrong, J. S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.030 · Cited by 121 · see citing works
Xie, K., Yu, Y., Zhang, Z., Liu, W., Pei, Y., Xiong, L., Hou, L., & Wang, G. (2010) · Shock · doi:10.1097/shk.0b013e3181def9aa · Cited by 111 · see citing works
Sinha, K., Sadhukhan, P., Saha, S., Pal, P. B., & Sil, P. C. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.01.008 · Cited by 114 · see citing works
Knutson, C. G., Mangerich, A., Zeng, Y., Raczynski, A. R., Liberman, R. G., Kang, P., Ye, W., Prestwich, E. G., Lü, K., Wishnok, J. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222669110 · Cited by 113 · see citing works
Hypochlorous Acid-Mediated Modification of Proteins and its Consequences
Hawkins, C. L. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190045 · Cited by 106 · see citing works
A Step into the Future: Applications of Nanoparticle Enzyme Mimics
Korschelt, K., Tahir, M. N., & Tremel, W. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201800384 · Cited by 102 · see citing works
Reevaluating gel-forming mucins' roles in cystic fibrosis lung disease
Pérez-Vilar, J., & Boucher, R. C. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.027 · Cited by 102 · see citing works
Jun, Y. W., Sarkar, S., Singha, S., Reo, Y. J., Kim, H. R., Kim, J.-J., Chang, Y., & Ahn, K. H. (2017) · Chemical Communications · doi:10.1039/c7cc05834a · Cited by 101 · see citing works
Functional Enzyme Mimics for Oxidative Halogenation Reactions that Combat Biofilm Formation
Herget, K., Frerichs, H., Pfitzner, F., Tahir, M. N., & Tremel, W. (2018) · Advanced Materials · doi:10.1002/adma.201707073 · Cited by 98 · see citing works
Boronate-Based Probes for Biological Oxidants: A Novel Class of Molecular Tools for Redox Biology
Sikora, A., Zielonka, J., Dębowska, K., Michalski, R., Smulik-Izydorczyk, R., Pięta, J., Podsiadły, R., Artelska, A., Pierzchała, K., & Kalyanaraman, B. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.580899 · Cited by 88 · see citing works
Sandvik, E. L., McLeod, B. R., Parker, A. E., & Stewart, P. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055118 · Cited by 87 · see citing works
Myeloperoxidase-induced Genomic DNA-centered Radicals
Gomez-Mejiba, S., Zhai, Z., Giménez, M. S., Ashby, M. T., Chilakapati, J., Kitchin, K. T., Mason, R. P., & Ramírez, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086579 · Cited by 85 · see citing works
Zhuang, Z., Zhou, M., You, W., Zhu, L., Ma, C., Sun, X., & Shi, J. (2012) · BMC Neuroscience · doi:10.1186/1471-2202-13-47 · Cited by 83 · see citing works
Ji, X.-T., Liu, W., Xie, K., Liu, W.-P., Qu, Y., Chao, X., Chen, T., Zhou, J., & Fei, Z. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.038 · Cited by 83 · see citing works
Hypochlorous Acid Generated by Neutrophils Inactivates ADAMTS13
Wang, Y., Chen, J., Ling, M., López, J. A., Chung, D. W., & Fu, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599084 · Cited by 79 · see citing works
Fedeles, B. I., Freudenthal, B., Yau, E., Singh, V., Chang, S.-C., Li, D., Delaney, J. C., Wilson, S. H., & Essigmann, J. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507709112 · Cited by 79 · see citing works
Meotti, F. C., Senthilmohan, R., Harwood, D. T., Missau, F. C., Pizzolatti, M. G., & Kettle, A. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.017 · Cited by 78 · see citing works
Adegoke, O., & Forbes, P. B. C. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2014.08.036 · Cited by 78 · see citing works
Antonelou, M., Michaëlsson, E., Evans, R. D. R., Wang, C. J., Henderson, S. R., Walker, L. S. K., Unwin, R. J., Salama, A. D., & RAVE-ITN Investigators (2019) · Journal of the American Society of Nephrology · doi:10.1681/asn.2019060618 · Cited by 73 · see citing works
Neutrophil-derived granule cargoes: paving the way for tumor growth and progression
Rawat, K., Syeda, S., & Shrivastava, A. (2021) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09951-1 · Cited by 69 · see citing works
The antioxidant properties of green carbon dots: a review
Sharma, N., Sharma, A., & Lee, H. (2025) · Environmental Chemistry Letters · doi:10.1007/s10311-025-01831-w · Cited by 70 · see citing works
Ex Tenebris Lux: Illuminating Reactive Oxygen and Nitrogen Species with Small Molecule Probes
Cabello, M. C., Chen, G., Melville, M. J., Osman, R., Kumar, G., Domaille, D. W., & Lippert, A. R. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00892 · Cited by 67 · see citing works
Thiocyanate Is an Efficient Endogenous Scavenger of the Phagocytic Killing Agent Hypobromous Acid
Nagy, P., Beal, J. L., & Ashby, M. T. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050338c · Cited by 67 · see citing works
Bindu, S., Mazumder, S., Dey, S., Pal, C., Goyal, M., Alam, A., Iqbal, M. S., Sarkar, S., Siddiqui, A. A., Banerjee, C., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.027 · Cited by 66 · see citing works
Choi, J., Yoon, B.-S., Lee, S., Hwang, J., & Ryang, R. (2007) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.30.324 · Cited by 63 · see citing works
Lopes, A. D. A., da Fonseca, F. N., Rocha, T. M., Freitas, L. B. N., Araújo, E. V. O., Wong, D. V. T., Júnior, R. C. P. L., & Leal, L. K. A. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8194849 · Cited by 64 · see citing works
Chen, S., Pan, J., Gong, Z., Wu, M., Zhang, X., Chen, H., Yang, D., Qi, S., Peng, Y., & Shen, J. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02991-8 · Cited by 62 · see citing works
Reactive oxygen species and anti-proteinases
Siddiqui, T., Zia, M. K., Ali, S. S., Rehman, A. A., Ahsan, H., & Khan, F. H. (2015) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2015.1115525 · Cited by 61 · see citing works
Summers, F. A., Morgan, P. E., Davies, M. J., & Hawkins, C. L. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8001719 · Cited by 59 · see citing works
Terrill, J. R., Duong, M. N., Turner, R., Guiner, C. L., Boyatzis, A. E., Kettle, A. J., Grounds, M. D., & Arthur, P. G. (2016) · Redox Biology · doi:10.1016/j.redox.2016.08.016 · Cited by 60 · see citing works
HEPES is not suitable for fluorescence detection of HClO: a novel probe for HClO in absolute PBS
Xing, P., Gao, K., Wang, B., Gao, J., Yan, H., Wen, J., Li, W., Xu, Y., Li, H., Chen, J., et al. (2016) · Chemical Communications · doi:10.1039/c6cc00880a · Cited by 59 · see citing works
Novío, S., Núñez, M. J., Amigo, G., & Freire-Garabal, M. (2011) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2011.00736.x · Cited by 60 · see citing works
Kim, K. H., Kim, S. J., Singha, S., Yang, Y. J., Park, S. K., & Ahn, K. H. (2021) · ACS Sensors · doi:10.1021/acssensors.1c00930 · Cited by 58 · see citing works
Barrett, T. J., Pattison, D. I., Leonard, S. E., Carroll, K. S., Davies, M. J., & Hawkins, C. L. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.024 · Cited by 58 · see citing works
Antioxidant screening of medicinal herbal teas
Speisky, H., Rocco, C., Carrasco‐Pozo, C., Lissi, E. A., & López‐Alarcón, C. (2006) · Phytotherapy Research · doi:10.1002/ptr.1878 · Cited by 57 · see citing works
Neutrophil differentiation from human‐induced pluripotent stem cells
Morishima, T., Watanabe, K., Niwa, A., Fujino, H., Matsubara, H., Adachi, S., Suemori, H., Nakahata, T., & Heike, T. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22456 · Cited by 56 · see citing works
Ji, X.-T., Tian, Y., Xie, K., Liu, W.-P., Qu, Y., & Fei, Z. (2012) · Journal of Surgical Research · doi:10.1016/j.jss.2011.12.038 · Cited by 51 · see citing works
Induction of IL-8 byMycoplasma pneumoniaemembrane in BEAS-2B cells
Chmura, K., Bai, X., Nakamura, M., Kandasamy, P., McGibney, M., Kuronuma, K., Mitsuzawa, H., Voelker, D. R., & Chan, E. D. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90204.2008 · Cited by 57 · see citing works
Bozonet, S. M., Scott-Thomas, A., Nagy, P., & Vissers, M. C. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.028 · Cited by 53 · see citing works
Photodynamic activity of platinum(IV) chloride surface-modified TiO2 irradiated with visible light
Kyzioł, A., Wolnicka-Głubisz, A., Urbańska, K., Kisch, H., Stochel, G., & Macyk, W. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.019 · Cited by 53 · see citing works
Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation
Hawkins, C. L., Pattison, D. I., Stanley, N., & Davies, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20070941 · Cited by 53 · see citing works
Abd‐Allah, A. R. A., Al‐Majed, A. A., Al‐Yahya, A. A., Fouda, S. I., & Al-Shabana, O. A. (2005) · Archives of Toxicology · doi:10.1007/s00204-004-0643-3 · Cited by 52 · see citing works
Ma, H., Song, B., Wang, Y., Liu, C., Wang, X., & Yuan, J. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.01.062 · Cited by 50 · see citing works
Molecular hydrogen and radiation protection
Chuai, Y., Qian, L., Sun, X., & Cai, J. (2012) · Free Radical Research · doi:10.3109/10715762.2012.689429 · Cited by 46 · see citing works
Ma, H., Chen, K., Song, B., Tang, Z., Huang, Y., Zhang, T., Wang, H., Sun, W., & Yuan, J. (2020) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2020.112560 · Cited by 45 · see citing works
Microbial‐derived indoles inhibit neutrophil myeloperoxidase to diminish bystander tissue damage
Alexeev, E. E., Dowdell, A. S., Henen, M. A., Lanis, J. M., Lee, J. S., Cartwright, I. M., Schaefer, R. E. M., Ornelas, A., Onyiah, J. C., Vögeli, B., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100027r · Cited by 44 · see citing works
Whiteman, M., Spencer, J. P. E., Szeto, H. H., & Armstrong, J. S. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1879 · Cited by 44 · see citing works
Valcheva-Kuzmanova, S., Kuzmanov, A., Kuzmanova, V., & Tzaneva, M. A. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.01.011 · Cited by 44 · see citing works
A meta-analysis of impacts of immune response and infection on oxidative status in vertebrates
Costantini, D. (2022) · Conservation Physiology · doi:10.1093/conphys/coac018 · Cited by 41 · see citing works
RUTIN, a widely consumed flavonoid, that commonly induces hormetic effects
Calabrese, E. J., Pressman, P., Hayes, A. W., Dhawan, G., Kapoor, R., Agathokleous, E., & Calabrese, V. (2024) · Food and Chemical Toxicology · doi:10.1016/j.fct.2024.114626 · Cited by 40 · see citing works
Meng, X., Shi, Y., Chen, Z., Song, L., Zhao, M., Zou, L., Liu, S., Huang, W., & Zhao, Q. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b14717 · Cited by 39 · see citing works
Therapeutic effect of liposomal-N-acetylcysteine against acetaminophen-induced hepatotoxicity
Alipour, M., Buonocore, C., Omri, A., Szabo, M., Pucaj, K., & Suntres, Z. E. (2013) · Journal of drug targeting · doi:10.3109/1061186x.2013.765443 · Cited by 37 · see citing works
Myeloperoxidase gene expression and cognitive functions in depression
Talarowska, M. E., Szemraj, J., & Gałecki, P. (2014) · Advances in Medical Sciences · doi:10.1016/j.advms.2014.06.001 · Cited by 37 · see citing works
Oxidant/antioxidant imbalance is an inherent feature of depression
Talarowska, M. E., Szemraj, J., Berk, M., Maes, M. H. J., & Gałecki, P. (2015) · BMC Psychiatry · doi:10.1186/s12888-015-0454-5 · Cited by 37 · see citing works
Homan, T., Tsuzuki, T., Dogishi, K., Shirakawa, H., Oyama, T., Nakagawa, T., & Kaneko, S. (2013) · Journal of Pharmacological Sciences · doi:10.1254/jphs.12265fp · Cited by 35 · see citing works
Batistel, F., Osorio, J. S., Tariq, M. R., Li, C., Caputo, J., Socha, M. T., & Loor, J. J. (2017) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-017-0163-7 · Cited by 35 · see citing works
Venkatesan, P., Rajakumar, G., Periyasami, G., Rahaman, M., Pandiaraj, S., Thiruvengadam, M., Thirumalaivasan, N., & Wu, S. (2023) · Journal of Materials Research and Technology · doi:10.1016/j.jmrt.2023.04.181 · Cited by 35 · see citing works
3-chlorotyrosine in Sputum of COPD Patients: Relationship with Airway Inflammation
O’Donnell, C., Newbold, P., White, P., Thong, B., Stone, H., & Stockley, R. A. (2010) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.3109/15412555.2010.528086 · Cited by 35 · see citing works
- Authors
- Winterbourn, C. C.
- Corresponding author
- Winterbourn, Christine C.
- Venue
- Toxicology
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 181-182
- Pages
- 223-227
- ISSN
- 0300-483X (ISSN-L)
- OpenAlex
- W2065076024
- Cited by
- 247
- References
- 26
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 17 · 2023: 9 · 2022: 11 · 2021: 13 · 2020: 15 · 2019: 10 · 2018: 12 · 2017: 9 · 2016: 10 · 2015: 9 · 2014: 16 · 2013: 19 · 2012: 13
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Toxicology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- hypochlorous acid, neutrophils, myeloperoxidase, reactive oxygen species, oxidative stress, biomarkers, oxidative damage, inflammation, neutrophil-mediated injury, superoxide, hydrogen peroxide, biomarker assays
- MeSH terms
- Animals, Chlorohydrins, Humans, Hypochlorous Acid, Neutrophils, Oxidation-Reduction, Proteins, Sulfhydryl Compounds, Tyrosine, Biomarkers, Oxidants
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