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3. Guidelines for measuring reactive oxygen species and oxidative damage in cells and in vivo

Author

Murphy, Michael P, Bayir, Hülya, Belousov, Vsevolod, Chang, Christopher J, Davies, Kelvin JA, Davies, Michael J, Dick, Tobias P, Finkel, Toren, Forman, Henry J, Janssen-Heininger, Yvonne, Gems, David, Kagan, Valerian E, Kalyanaraman, Balaraman, Larsson, Nils-Göran, Milne, Ginger L, Nyström, Thomas, Poulsen, Henrik E, Radi, Rafael, Van Remmen, Holly, Schumacker, Paul T, Thornalley, Paul J, Toyokuni, Shinya, Winterbourn, Christine C, Yin, Huiyong, and Halliwell, Barry

Subjects
Generic health relevance, Antioxidants, Oxidation-Reduction, Oxidative Stress, Reactive Oxygen Species, Signal Transduction
Abstract

Multiple roles of reactive oxygen species (ROS) and their consequences for health and disease are emerging throughout biological sciences. This development has led researchers unfamiliar with the complexities of ROS and their reactions to employ commercial kits and probes to measure ROS and oxidative damage inappropriately, treating ROS (a generic abbreviation) as if it were a discrete molecular entity. Unfortunately, the application and interpretation of these measurements are fraught with challenges and limitations. This can lead to misleading claims entering the literature and impeding progress, despite a well-established body of knowledge on how best to assess individual ROS, their reactions, role as signalling molecules and the oxidative damage that they can cause. In this consensus statement we illuminate problems that can arise with many commonly used approaches for measurement of ROS and oxidative damage, and propose guidelines for best practice. We hope that these strategies will be useful to those who find their research requiring assessment of ROS, oxidative damage and redox signalling in cells and in vivo.

Published
2022

9. The ‘mitoflash’ probe cpYFP does not respond to superoxide

Author

Schwarzländer, Markus, Wagner, Stephan, Ermakova, Yulia G, Belousov, Vsevolod V, Radi, Rafael, Beckman, Joseph S, Buettner, Garry R, Demaurex, Nicolas, Duchen, Michael R, Forman, Henry J, Fricker, Mark D, Gems, David, Halestrap, Andrew P, Halliwell, Barry, Jakob, Ursula, Johnston, Iain G, Jones, Nick S, Logan, David C, Morgan, Bruce, Müller, Florian L, Nicholls, David G, Remington, S James, Schumacker, Paul T, Winterbourn, Christine C, Sweetlove, Lee J, Meyer, Andreas J, Dick, Tobias P, and Murphy, Michael P

Subjects
Aging, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Animals, Caenorhabditis elegans, Longevity, Male, Mitochondria, Superoxides, General Science & Technology
Abstract

Ageing and lifespan of organisms are determined by complicated interactions between their genetics and the environment, but the cellular mechanisms remain controversial. There have been a number of studies suggesting that cellular energy metabolism and free radical dynamics affect lifespan, implicating mitochondrial function. Recently, Shen et al. provided apparent mechanistic insight by reporting that mitochondrial oscillations of ‘free radical production’, called ‘mitoflashes’, in the pharynx of 3-day old Caenorhabditis elegans correlated inversely with lifespan. The interpretation of ‘mitoflashes’ as ‘bursts of superoxide’ radicals assumes that circularly permuted yellow fluorescent protein (cpYFP) is a reliable indicator of mitochondrial superoxide. This interpretation has been criticised because experiments and theoretical considerations both show that changes in cpYFP fluorescence are due to alterations in pH, not superoxide-. We now provide direct evidence that purified cpYFP is completely unresponsive to superoxide. Therefore ‘mitoflashes’ do not reflect superoxide generation and are not evidence for a link between mitochondrial free radical dynamics and lifespan.

Published
2014

14. Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors.

Author

Paumann-Page, Martina, Obinger, Christian, Winterbourn, Christine C., and Furtmüller, Paul G.

Subjects
PHLOROGLUCINOL, COLLAGEN, LEAD compounds, HIGH throughput screening (Drug development), PEROXIDASE, EXTRACELLULAR matrix, FREE radicals
Abstract

Human peroxidasin (PXDN) is a ubiquitous peroxidase enzyme expressed in most tissues in the body. PXDN represents an interesting therapeutic target for inhibition, as it plays a role in numerous pathologies, including cardiovascular disease, cancer and fibrosis. Like other peroxidases, PXDN generates hypohalous acids and free radical species, thereby facilitating oxidative modifications of numerous biomolecules. We have studied the inhibition of PXDN halogenation and peroxidase activity by phloroglucinol and 14 other peroxidase inhibitors. Although a number of compounds on their own potently inhibited PXDN halogenation activity, only five were effective in the presence of a peroxidase substrate with IC50 values in the low μM range. Using sequential stopped-flow spectrophotometry, we examined the mechanisms of inhibition for several compounds. Phloroglucinol was the most potent inhibitor with a nanomolar IC50 for purified PXDN and IC50 values of 0.95 μM and 1.6 μM for the inhibition of hypobromous acid (HOBr)-mediated collagen IV cross-linking in a decellularized extracellular matrix and a cell culture model. Other compounds were less effective in these models. Most interestingly, phloroglucinol was identified to irreversibly inhibit PXDN, either by mechanism-based inhibition or tight binding. Our work has highlighted phloroglucinol as a promising lead compound for the design of highly specific PXDN inhibitors and the assays used in this study provide a suitable approach for high-throughput screening of PXDN inhibitors. [ABSTRACT FROM AUTHOR]

Published
2024
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20. Lethal Weapons

Author

Roos, Dirk and Winterbourn, Christine C.

Published
2002

23. Guidelines for measuring reactive oxygen species and oxidative damage in cells and in vivo

Author

Murphy, Michael P., Bayir, Hülya, Belousov, Vsevolod, Chang, Christopher J., Davies, Kelvin J.A., Davies, Michael J., Dick, Tobias P., Finkel, Toren, Forman, Henry J., Janssen-Heininger, Yvonne, Gems, David, Kagan, Valerian E., Kalyanaraman, Balaraman, Larsson, Nils Göran, Milne, Ginger L., Nyström, Thomas, Poulsen, Henrik E., Radi, Rafael, Van Remmen, Holly, Schumacker, Paul T., Thornalley, Paul J., Toyokuni, Shinya, Winterbourn, Christine C., Yin, Huiyong, Halliwell, Barry, Murphy, Michael P., Bayir, Hülya, Belousov, Vsevolod, Chang, Christopher J., Davies, Kelvin J.A., Davies, Michael J., Dick, Tobias P., Finkel, Toren, Forman, Henry J., Janssen-Heininger, Yvonne, Gems, David, Kagan, Valerian E., Kalyanaraman, Balaraman, Larsson, Nils Göran, Milne, Ginger L., Nyström, Thomas, Poulsen, Henrik E., Radi, Rafael, Van Remmen, Holly, Schumacker, Paul T., Thornalley, Paul J., Toyokuni, Shinya, Winterbourn, Christine C., Yin, Huiyong, and Halliwell, Barry

Abstract

Multiple roles of reactive oxygen species (ROS) and their consequences for health and disease are emerging throughout biological sciences. This development has led researchers unfamiliar with the complexities of ROS and their reactions to employ commercial kits and probes to measure ROS and oxidative damage inappropriately, treating ROS (a generic abbreviation) as if it were a discrete molecular entity. Unfortunately, the application and interpretation of these measurements are fraught with challenges and limitations. This can lead to misleading claims entering the literature and impeding progress, despite a well-established body of knowledge on how best to assess individual ROS, their reactions, role as signalling molecules and the oxidative damage that they can cause. In this consensus statement we illuminate problems that can arise with many commonly used approaches for measurement of ROS and oxidative damage, and propose guidelines for best practice. We hope that these strategies will be useful to those who find their research requiring assessment of ROS, oxidative damage and redox signalling in cells and in vivo.

Published
2022

26. Unraveling the Biological Roles of Reactive Oxygen Species

Author

Murphy, Michael P., Holmgren, Arne, Larsson, Nils-Göran, Halliwell, Barry, Chang, Christopher J., Kalyanaraman, Balaraman, Rhee, Sue Goo, Thornalley, Paul J., Partridge, Linda, Gems, David, Nyström, Thomas, Belousov, Vsevolod, Schumacker, Paul T., and Winterbourn, Christine C.

Published
2011
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33. Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential

Author

Paumann-Page, Martina, primary, Kienzl, Nikolaus F., additional, Motwani, Jyoti, additional, Bathish, Boushra, additional, Paton, Louise N., additional, Magon, Nicholas J., additional, Sevcnikar, Benjamin, additional, Furtmüller, Paul G., additional, Traxlmayr, Michael W., additional, Obinger, Christian, additional, Eccles, Mike R., additional, and Winterbourn, Christine C., additional

Published
2021
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50. Reactions of superoxide with myeloperoxidase

Author

Kettle, Anthony J., Anderson, Robert F., Hampton, Mark B., and Winterbourn, Christine C.

Subjects
Superoxide -- Chemical properties, Superoxide -- Structure, Peroxidase -- Chemical properties, Peroxidase -- Structure, Neutrophils -- Chemical properties, Neutrophils -- Structure, Biological sciences, Chemistry
Abstract

The pulse radiolysis was used to determine kinetic parameters of superoxide reacting with redox forms of myeloperoxidase and analyze the steady-state kinetic. The findings suggest that interactions of superoxide and myeloperoxidase would have a major influence on the way neutrophils use oxygen to kill bacteria.

Published
2007

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