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2. Neutrophil-vascular interactions drive myeloperoxidase accumulation in the brain in Alzheimer’s disease

Author

Smyth, Leon C. D., Murray, Helen C., Hill, Madison, van Leeuwen, Eve, Highet, Blake, Magon, Nicholas J., Osanlouy, Mahyar, Mathiesen, Sophie N., Mockett, Bruce, Singh-Bains, Malvindar K., Morris, Vanessa K., Clarkson, Andrew N., Curtis, Maurice A., Abraham, Wickliffe C., Hughes, Stephanie M., Faull, Richard L. M., Kettle, Anthony J., Dragunow, Mike, and Hampton, Mark B.

Published
2022
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21. Additional file 1 of Neutrophil-vascular interactions drive myeloperoxidase accumulation in the brain in Alzheimer���s disease

Author

Smyth, Leon C. D., Murray, Helen C., Hill, Madison, van Leeuwen, Eve, Highet, Blake, Magon, Nicholas J., Osanlouy, Mahyar, Mathiesen, Sophie N., Mockett, Bruce, Singh-Bains, Malvindar K., Morris, Vanessa K., Clarkson, Andrew N., Curtis, Maurice A., Abraham, Wickliffe C., Hughes, Stephanie M., Faull, Richard L. M., Kettle, Anthony J., Dragunow, Mike, and Hampton, Mark B.

Abstract

Additional file 1. Figure S1: MPO labelling is predominantly confined to neutrophils. Figure S2: Neutrophil accumulation is independent of sex, age, and post-mortem delay. Figure S3: Regional analysis of neutrophil accumulation in APP/PS1 mice. Figure S4: Amyloid-��1-42 does not induce NETosis in vitro. Figure S5: Specificity of antibody labelling across multiple rounds of multiplexed immunohistochemistry. Table S1: Case details of tissue used in tissue microarray and immunohistochemistry experiments. Table S2: Details of antibodies used for these studies.

Published
2022
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33. Additional file 1 of Genome-wide impact of hydrogen peroxide on maintenance DNA methylation in replicating cells

Author

Seddon, Annika R., Yusmiati Liau, Pace, Paul E., Miller, Allison L., Das, Andrew B., Kennedy, Martin A., Hampton, Mark B., and Stevens, Aaron J.

Subjects
ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, ComputingMilieux_COMPUTERSANDEDUCATION, Data_FILES, ComputerApplications_COMPUTERSINOTHERSYSTEMS
Abstract

Additional file 1. Supplementary tables and figures.

Published
2021
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34. Insights into H2O2-induced signaling in Jurkat cells from analysis of gene expression.

Author

Taylor, Megan F., Black, Michael A., Hampton, Mark B., and Ledgerwood, Elizabeth C.

Subjects
GENE expression, CELL analysis, CELL communication, CELL death, SULFHYDRYL group, T cells
Abstract

Hydrogen peroxide (H2O2) is a ubiquitous oxidant produced in a regulated manner by various enzymes in mammalian cells. H2O2 reversibly oxidizes thiol groups of cysteine residues to mediate intracellular signaling. While examples of H2O2-dependent signaling have been reported, the exact molecular mechanism(s) of signaling and the pathways affected are not well understood. Here, the transcriptomic response of Jurkat T cells to H2O2 was investigated to determine global effects on gene expression. With a low H2O2 concentration (10 µM) that did not induce an oxidative stress response or cell death, extensive changes in gene expression occurred after 4 h (6803 differentially expressed genes). Of the genes with a greater then 2-fold change in expression, 85% were upregulated suggesting that in a physiological setting H2O2 predominantly activates gene expression. Pathway analysis identified gene expression signatures associated with FOXO and NTRK signaling. These signatures were associated with an overlapping set of transcriptional regulators. Overall, our results provide a snapshot of gene expression changes in response to H2O2, which, along with further studies, will lead to new insights into the specific pathways that are activated in response to endogenous production of H2O2, and the molecular mechanisms of H2O2 signaling. [ABSTRACT FROM AUTHOR]

Published
2022
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41. Oxidation of bacillithiol during killing of Staphylococcus aureusUSA300 inside neutrophil phagosomes

Author

Ashby, Louisa V, Springer, Reuben, Loi, Vu Van, Antelmann, Haike, Hampton, Mark B, Kettle, Anthony J, and Dickerhof, Nina

Abstract

Targeting immune evasion tactics of pathogenic bacteria may hold the key to treating recalcitrant bacterial infections. Staphylococcus aureusproduces bacillithiol (BSH), its major low‐molecular‐weight thiol, which is thought to protect this opportunistic human pathogen against the bombardment of oxidants inside neutrophil phagosomes. Here, we show that BSH was oxidized when human neutrophils phagocytosed S. aureus, but provided limited protection to the bacteria. We used mass spectrometry to measure the oxidation of BSH upon exposure of S. aureusUSA300 to either a bolus of hypochlorous acid (HOCl) or a flux generated by the neutrophil enzyme myeloperoxidase. Oxidation of BSH and loss of bacterial viability were strongly correlated (r= 0.99, p< 0.001). BSH was fully oxidized after exposure of S. aureusto lethal doses of HOCl. However, there was no relationship between the initial BSH levels and the dose of HOCl required for bacterial killing. In contrast to the HOCl systems, only 50% of total BSH was oxidized when neutrophils killed the majority of phagocytosed bacteria. Oxidation of BSH was decreased upon inhibition of myeloperoxidase, implicating HOCl in phagosomal BSH oxidation. A BSH‐deficient S. aureusUSA300 mutant was slightly more susceptible to treatment with either HOCl or ammonia chloramine, or to killing within neutrophil phagosomes. Collectively, our data show that myeloperoxidase‐derived oxidants react with S. aureusinside neutrophil phagosomes, leading to partial BSH oxidation, and contribute to bacterial killing. However, BSH offers only limited protection against the neutrophil's multifaceted killing mechanisms. Bacterial bacillithiol was oxidized during phagocytosis but provided minimal protection against the neutrophil's killing mechanisms.

Published
2022
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44. 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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