Accessibility Skip to Global Navigation Skip to Local Navigation Skip to Content Skip to Search Skip to Site Map Menu

Otago Medical School staff profiles

Professor Mark Hampton

PositionProfessor
DepartmentDepartment of Pathology and Biomedical Science(UOC)
QualificationsMSc(Hons)(Cant), PhD(Otago)
Research summaryFree Radical research

Research

Oxidants (also called reactive oxygen species or free radicals) are continuously generated in our body, and we rely on sophisticated antioxidant systems to prevent them from causing damage. However, oxidants also have beneficial roles. They can act as signalling molecules that regulate a number of life and death pathways in cells, and they are generated by the immune system to fight microbes. My research is focused on how understanding how cells sense and respond to oxidants, and how these pathways might be modulated to prevent and treat human disease.

Mitochondria are the small organelles inside cells that convert food into energy. These powerhouses are also a major site of oxidant production. Mitochondrial oxidants can cause damage, and they have been linked to various cardiovascular and neurodegenerative diseases as well as ageing, but they also regulate normal biological processes. We measure mitochondrial function in human cells, and study mitochondrial antioxidant defenses, including the peroxiredoxins, which act as sensors and markers of oxidative stress. We are also interested in a class of dietary compounds called isothiocyanates that can influence antioxidant networks and mitochondrial function.

All of our cells have self-destruct programs that ensure removal when they become damaged or are no longer needed in the body. Mitochondria are central players in these cell death pathways, and it appears that mitochondrial oxidants are involved in regulating cell death, but it is not clear exactly how this happens. Cancer cells are often resistant to undergoing cell death, and it has been proposed that their antioxidant defenses are more powerful. It may be possible to target these defenses, making it easier to kill cancer cells. White blood cells generate oxidants to destroy pathogenic bacteria, but these oxidants also appear to regulate the lifespan of immune cells and the resolution of inflammation. We are studying the effects of oxidants on the function of white blood cells and other cells and mediators present at an inflammatory site.

Publications

de Souza, L. F., Pearson, A. G., Pace, P. E., Dafre, A. L., Hampton, M. B., Meotti, F. C., & Winterbourn, C. C. (2019). Peroxiredoxin expression and redox status in neutrophils and HL-60 cells. Free Radical Biology & Medicine. Advance online publication. doi: 10.1016/j.freeradbiomed.2019.03.007

Pace, P. E., Peskin, A. V., Konigstorfer, A., Jasoni, C. J., Winterbourn, C. C., & Hampton, M. B. (2018). Peroxiredoxin interaction with the cytoskeletal-regulatory protein CRMP2: Investigation of a putative redox relay. Free Radical Biology & Medicine, 129, 383-393. doi: 10.1016/j.freeradbiomed.2018.10.407

Hampton, M. B., Vick, K. A., Skoko, J. J., & Neumann, C. A. (2018). Peroxiredoxin involvement in the initiation and progression of human cancer. Antioxidants & Redox Signaling, 28(7), 591-608. doi: 10.1089/ars.2017.7422

Yewdall, N. A., Peskin, A. V., Hampton, M. B., Goldstone, D. C., Pearce, F. G., & Gerrard, J. A. (2018). Quaternary structure influences the peroxidase activity of peroxiredoxin 3. Biochemical & Biophysical Research Communications, 497(2), 558-563. doi: 10.1016/j.bbrc.2018.02.093

Richards, S. J. G., Frizelle, F. A., Geddes, J. A., Eglinton, T. W., & Hampton, M. B. (2018). Frailty in surgical patients. International Journal of Colorectal Disease, 33(12), 1657-1666. doi: 10.1007/s00384-018-3163-y

Edited Book - Research

Vissers, M. C. M., Hampton, M. B., & Kettle, A. J. (Eds.). (2017). Hydrogen peroxide metabolism in health and disease. Boca Raton, FL: CRC Press, 456p.

^ Top of page

Chapter in Book - Research

Hampton, M. B. (2017). Hydrogen peroxide-dependent redox signaling: Basic concepts and unanswered questions. In M. C. M. Vissers, M. B. Hampton & A. J. Kettle (Eds.), Hydrogen peroxide metabolism in health and disease. (pp. 353-364). Boca Raton, FL: CRC Press.

Parker, H. A., Magon, N. J., Green, J. N., Hampton, M. B., & Winterbourn, C. C. (2014). Analysis of neutrophil bactericidal activity. In M. T. Quinn & F. R. DeLeo (Eds.), Neutrophil methods and protocols: Methods in Molecular Biology (Vol. 1124). (2nd ed.) (pp. 291-306). New York, NY: Springer. doi: 10.1007/978-1-62703-845-4_19

Requejo, R., Chouchani, E. T., Hurd, T. R., Menger, K. E., Hampton, M. B., & Murphy, M. P. (2010). Measuring mitochondrial protein thiol redox state. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Thiol redox transitions in cell signaling: Part B: Cellular localization and signaling (Vol. 474). (pp. 123-147). San Diego, CA: Academic Press. doi: 10.1016/S0076-6879(10)74004-0

Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010). Measuring the redox state of cellular peroxiredoxins by immunoblotting. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Thiol redox transitions in cell signaling: Part B: Cellular localization and signaling (Vol. 474). (pp. 51-66). San Diego, CA: Academic Press. doi: 10.1016/S0076-6879(10)74004-0

Green, J. N., Winterbourn, C. C., & Hampton, M. B. (2007). Analysis of neutrophil bactericidal activity. In M. T. Quinn, F. R. DeLeo & G. M. Bokoch (Eds.), Neutrophil methods and protocols. (pp. 319-332). Totowa, USA: Humana Press.

Hampton, M. B., Baty, J. W., & Winterbourn, C. C. (2006). Use of a proteomic technique to identify oxidant-sensitive thiol proteins in cultured cells. In I. Dalle-Donne, A. Scaloni & D. A. Butterfield (Eds.), Redox Proteomics: From protein modifications to cellular dysfunction and diseases. (pp. 253-265). Hoboken, NJ: John Wiley & Sons.

Winterbourn, C. C., van Dalen, C. J., Hampton, M. B., & Kettle, A. J. (2000). Reactions of myeloperoxidase and production of hypochlorous acid in neutrophil phagosomes. In P. E. Petrides & W. M. Nauseef (Eds.), The Peroxidase Multigene Family of Enzymes. (pp. 58-67). Berlin: Springer.

^ Top of page

Journal - Research Article

de Souza, L. F., Pearson, A. G., Pace, P. E., Dafre, A. L., Hampton, M. B., Meotti, F. C., & Winterbourn, C. C. (2019). Peroxiredoxin expression and redox status in neutrophils and HL-60 cells. Free Radical Biology & Medicine. Advance online publication. doi: 10.1016/j.freeradbiomed.2019.03.007

Pace, P. E., Peskin, A. V., Konigstorfer, A., Jasoni, C. J., Winterbourn, C. C., & Hampton, M. B. (2018). Peroxiredoxin interaction with the cytoskeletal-regulatory protein CRMP2: Investigation of a putative redox relay. Free Radical Biology & Medicine, 129, 383-393. doi: 10.1016/j.freeradbiomed.2018.10.407

Richards, S. J. G., Frizelle, F. A., Geddes, J. A., Eglinton, T. W., & Hampton, M. B. (2018). Frailty in surgical patients. International Journal of Colorectal Disease, 33(12), 1657-1666. doi: 10.1007/s00384-018-3163-y

Yewdall, N. A., Peskin, A. V., Hampton, M. B., Goldstone, D. C., Pearce, F. G., & Gerrard, J. A. (2018). Quaternary structure influences the peroxidase activity of peroxiredoxin 3. Biochemical & Biophysical Research Communications, 497(2), 558-563. doi: 10.1016/j.bbrc.2018.02.093

Hampton, M. B., Vick, K. A., Skoko, J. J., & Neumann, C. A. (2018). Peroxiredoxin involvement in the initiation and progression of human cancer. Antioxidants & Redox Signaling, 28(7), 591-608. doi: 10.1089/ars.2017.7422

Dagnell, M., Pace, P. E., Cheng, Q., Frijhoff, J., Östman, A., Arnér, E. S. J., Hampton, M. B., & Winterbourn, C. C. (2017). Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H2O2 exposure. Journal of Biological Chemistry, 292(35), 14371-14380. doi: 10.1074/jbc.M117.793745

Schindler, L., Dickerhof, N., Hampton, M. B., & Bernhagen, J. (2017). Post-translational regulation of macrophage migration inhibitory factor: Basis for functional fine-tuning. Redox Biology, 15, 135-142. doi: 10.1016/j.redox.2017.11.028

Poynton, R. A., Peskin, A. V., Haynes, A. C., Lowther, W. T., Hampton, M. B., & Winterbourn, C. C. (2016). Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation. Biochemical Journal, 473, 411-421. doi: 10.1042/bj20150572

Cuddihy, S. L., Drake, S., Harwood, T., Selwood, A. I., McNabb, P. S., & Hampton, M. B. (2016). The marine cytotoxin portimine is a potent and selective inducer of apoptosis. Apoptosis, 21(12), 1447-1452. doi: 10.1007/s10495-016-1302-x

Bayer, S. B., Low, F. M., Hampton, M. B., & Winterbourn, C. C. (2016). Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane. Free Radical Research, 50(12), 1329-1339. doi: 10.1080/10715762.2016.1241995

Yewdall, N. A., Venugopal, H., Desfosses, A., Abrishami, V., Yosaatmadja, Y., Hampton, M. B., … Radjainia, M. (2016). Structures of human peroxiredoxin 3 suggest self-chaperoning assembly that maintains catalytic state. Structure, 24(7), 1120-1129. doi: 10.1016/j.str.2016.04.013

Magon, N. J., Turner, R., Gearry, R. B., Hampton, M. B., Sly, P. D., & Kettle, A. J. (2015). Oxidation of calprotectin by hypochlorous acid prevents chelation of essential metal ions and allows bacterial growth: Relevance to infections in cystic fibrosis. Free Radical Biology & Medicine, 86, 133-144. doi: 10.1016/j.freeradbiomed.2015.05.022

Radjainia, M., Venugopal, H., Desfosses, A., Phillips, A. M., Yewdall, N. A., Hampton, M. B., … Mitra, A. K. (2015). Cryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone. Structure, 23(5), 912-920. doi: 10.1016/j.str.2015.03.019

Balasubramanain, D., Deng, A. X., Doudney, K., Hampton, M. B., & Kennedy, M. A. (2015). Valproic acid exposure leads to upregulation and increased promoter histone acetylation of sepiapterin reductase in a serotonergic cell line. Neuropharmacology, 99, 79-88. doi: 10.1016/j.neuropharm.2015.06.018

Dickerhof, N., Schindler, L., Bernhagen, J., Kettle, A. J., & Hampton, M. B. (2015). Macrophage migration inhibitory factor (MIF) Is rendered enzymatically inactive by myeloperoxidase-derived oxidants but retains its immunomodulatory function. Free Radical Biology & Medicine, 89, 498-511. doi: 10.1016/j.freeradbiomed.2015.09.009

Bayer, S. B., Hampton, M. B., & Winterbourn, C. C. (2015). Accumulation of oxidized peroxiredoxin 2 in red blood cells and its prevention. Transfusion, 55(8), 1909-1918. doi: 10.1111/trf.13039

Spencer, E. S., Dale, E. J., Gommans, A. L., Rutledge, M. T., Vo, C. T., Nakatani, Y., Gamble, A. B., Smith, R. A. J., Wilbanks, S. M., Hampton, M. B., & Tyndall, J. D. A. (2015). Multiple binding modes of isothiocyanates that inhibit macrophage migration inhibitory factor. European Journal of Medicinal Chemistry, 93, 501-510. doi: 10.1016/j.ejmech.2015.02.012

Wilkie-Grantham, R. P., Magon, N. J., Harwood, D. T., Kettle, A. J., Vissers, M. C., Winterbourn, C. C., & Hampton, M. B. (2015). Myeloperoxidase-dependent lipid peroxidation promotes the oxidative modification of cytosolic proteins in phagocytic neutrophils. Journal of Biological Chemistry, 290(15), 9896-9905. doi: 10.1074/jbc.M114.613422

Newman, T. A. C., Carleton, C. R., Leeke, B., Hampton, M. B., & Horsfield, J. A. (2015). Embryonic oxidative stress results in reproductive impairment for adult zebrafish. Redox Biology, 6, 648-655. doi: 10.1016/j.redox.2015.10.010

Jodczyk, S., Pearson, J. F., Aitchison, A., Miller, A. L., Hampton, M. B., & Kennedy, M. A. (2015). Telomere length measurement on the Roche LightCycler 480 platform. Genetic Testing & Molecular Biomarkers, 19(2), 63-68. doi: 10.1089/gtmb.2014.0208

Poynton, R. A., & Hampton, M. B. (2014). Peroxiredoxins as biomarkers of oxidative stress. Biochimica et Biophysica Acta: General Subjects, 1840(2), 906-912. doi: 10.1016/j.bbagen.2013.08.001

Dickerhof, N., Magon, N. J., Tyndall, J. D. A., Kettle, A. J., & Hampton, M. B. (2014). Potent inhibition of macrophage migration inhibitory factor (MIF) by myeloperoxidase-dependant oxidation of epicatechins. Biochemical Journal, 462(2), 303-314. doi: 10.1042/BJ20140612

Kumar, V., Kleffmann, T., Hampton, M. B., Cannell, M. B., & Winterbourn, C. C. (2013). Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry. Free Radical Biology & Medicine, 58, 109-117. doi: 10.1016/j.freeradbiomed.2013.01.021

Falvey, J. D., Bentley, R. W., Merriman, T. R., Hampton, M. B., Barclay, M. L., Gearry, R. B., & Roberts, R. L. (2013). Macrophage migration inhibitory factor gene polymorphisms in inflammatory bowel disease: An association study in New Zealand Caucasians and meta-analysis. World Journal of Gastroenterology, 19(39), 6656-6664. doi: 10.3748/wjg.v19.i39.6656

Bayer, S. B., Maghzal, G., Stocker, R., Hampton, M. B., & Winterbourn, C. C. (2013). Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation. FASEB Journal, 27(8), 3315-3322. doi: 10.1096/fj.13-227298

Pace, P. E., Peskin, A. V., Han, M.-H., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46. Biochemical Journal, 453, 475-485. doi: 10.1042/BJ20130030

Peskin, A. V., Dickerhof, N., Poynton, R. A., Paton, L. N., Pace, P. E., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidation of peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine. Journal of Biological Chemistry, 288, 14170-14177. doi: 10.1074/jbc.M113.460881

Hock, B. D., Taylor, K. G., Cross, N. B., Kettle, A. J., Hampton, M. B., & McKenzie, J. L. (2012). Effect of activated human polymorphonuclear leucocytes on T lymphocyte proliferation and viability. Immunology, 137(3), 249-258. doi: 10.1111/imm.12004

Tyndall, J. D. A., Lue, H., Rutledge, M. T., Bernhagen, J., Hampton, M. B., & Wilbanks, S. M. (2012). Macrophage migration inhibitory factor covalently complexed with phenethyl isothiocyanate. Acta Crystallographica Section F, 68(9), 999-1002. doi: 10.1107/s1744309112030552

Stacey, M. M., Cuddihy, S. L., Hampton, M. B., & Winterbourn, C. C. (2012). Protein thiol oxidation and formation of S-glutathionylated cyclophilin A in cells exposed to chloramines and hypochlorous acid. Archives of Biochemistry & Biophysics, 527(1), 45-54. doi: 10.1016/j.abb.2012.07.011

Keenan, J. I., Salm, N., Wallace, A. J., & Hampton, M. B. (2012). Using food to reduce H. pylori-associated inflammation. Phytotherapy Research, 26(11), 1620-1625. doi: 10.1002/ptr.4618

Parker, H., Dragunow, M., Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (2012). Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus. Journal of Leukocyte Biology, 92(4), 841-849. doi: 10.1189/jlb.1211601

Karton, A., Nagy, P., Betz, A., Peskin, A. V., Pace, P., O'Reilly, R. J., Hampton, M. B., … Winterbourn, C. C. (2011). Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide; a kinetic and computational study. Journal of Biological Chemistry, 286(20), 18048-18055. doi: 10.1074/jbc.M111.232355

Brown, K. K., & Hampton, M. B. (2011). Biological targets of isothiocyanates. Biochimica et Biophysica Acta: General Subjects, 1810(9), 888-894. doi: 10.1016/j.bbagen.2011.06.004

Cuddihy, S. L., Winterbourn, C. C., & Hampton, M. B. (2011). Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling. Antioxidants & Redox Signaling, 15(1), 167-174. doi: 10.1089/ars.2010.3843

Keenan, J. I., Salm, N., Hampton, M. B., & Wallace, A. J. (2010). Individual and combined effects of foods on Helicobacter pylori growth. Phytotherapy Research, 24(8), 1229-1233. doi: 10.1002/ptr.3167

Parker, H., Chitcholtan, K., Hampton, M. B., & Keenan, J. I. (2010). Uptake of Helicobacter pylori outer membrane vesicles by gastric epithelial cells. Infection & Immunity, 78(12), 5054-5061. doi: 10.1128/IAI.00299-10

Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010). Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochemical Journal, 425(2), 313-325. doi: 10.1042/BJ20091541

Brown, K. K., Cox, A. G., & Hampton, M. B. (2010). Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin. FEBS Letters, 584, 1257-1262. doi: 10.1016/j.febslet.2010.02.042

Peskin, A. V., Cox, A. G., Nagy, P., Morgan, P. E., Hampton, M. B., Davies, M. J., & Winterbourn, C. C. (2010). Removal of amino acid, peptide and protein hydroperoxides by reaction with peroxiredoxins 2 and 3. Biochemical Journal, 432, 313-321. doi: 10.1042/BJ20101156

Bernal, A. B., Vickers, M. H., Hampton, M. B., Poynton, R. A., & Sloboda, D. M. (2010). Maternal undernutrition significantly impacts ovarian follicle number and increases ovarian oxidative stress in adult rat offspring. PLoS ONE, 5(12), e15558. doi: 10.1371/journal.pone.0015558

Kumar, V., Kitaeff, N., Hampton, M. B., Cannell, M. B., & Winterbourn, C. C. (2009). Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion. FEBS Letters, 583(6), 997-1000. doi: 10.1016/j.febslet.2009.02.018

Cox, A. G., Pearson, A. G., Pullar, J. M., Jönsson, T. J., Lowther, W. T., Winterbourn, C. C., & Hampton, M. B. (2009). Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochemical Journal, 421(1), 51-58. doi: 10.1042/BJ20090242

Brown, K. K., Blaikie, F. H., Smith, R. A. J., Tyndall, J. D. A., Lue, H., Bernhagen, J., Winterbourn, C. C., & Hampton, M. B. (2009). Direct modification of the proinflammatory cytokine macrophage migration inhibitory factor by dietary isothiocyanates. Journal of Biological Chemistry, 284(47), 32425-32433. doi: 10.1074/jbc.M109.047092

Cuddihy, S. L., Baty, J. W., Brown, K. K., Winterbourn, C. C., & Hampton, M. B. (2009). Proteomic detection of oxidized and reduced thiol proteins in cultured cells. Methods in Molecular Biology, 519, 363-375. doi: 10.1007/978-1-59745-281-6_23

Cox, A. G., Peskin, A. V., Paton, L. N., Winterbourn, C. C., & Hampton, M. B. (2009). Redox potential and peroxide reactivity of human peroxiredoxin 3. Biochemistry, 48(27), 6495-6501. doi: 10.1021/bi900558g

Brown, K. K., Eriksson, S. E., Arnér, E. S. J., & Hampton, M. B. (2008). Mitochondrial peroxiredoxin 3 is rapidly oxidized in cells treated with isothiocyanates. Free Radical Biology & Medicine, 45(4), 494-502. doi: 10.1016/j.freeradbiomed.2008.04.030

Low, F. M., Hampton, M. B., & Winterbourn, C. C. (2008). Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxidants & Redox Signaling, 10(9), 1621-1629. doi: 10.1089/ars.2008.2081

Cox, A. G., Brown, K. K., Arner, E. S. J., & Hampton, M. B. (2008). The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation. Biochemical Pharmacology, 76(9), 1097-1109. doi: 10.1016/j.bcp.2008.08.021

Chitcholtan, K., Hampton, M. B., & Keenan, J. I. (2008). Outer membrane vesicles enhance the carcinogenic potential of Helicobacter pylori. Carcinogenesis, 29(12), 2400-2405. doi: 10.1093/carcin/bgn218

Cox, A. G., Pullar, J. M., Hughes, G., Ledgerwood, E. C., & Hampton, M. B. (2008). Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Radical Biology & Medicine, 44(6), 1001-1009. doi: 10.1016/j.freeradbiomed.2007.11.017

Winterbourn, C. C., & Hampton, M. B. (2008). Thiol chemistry and specificity in redox signaling. Free Radical Biology & Medicine, 45(5), 549-561. doi: 10.1016/j.freeradbiomed.2008.05.004

Thomson, S. J., Cox, A. G., Cuddihy, S. L., Pullar, J. M., & Hampton, M. B. (2008). Inhibition of receptor-mediated apoptosis upon Bcl-2 overexpression is not associated with increased antioxidant status. Biochemical & Biophysical Research Communications, 375(1), 145-150. doi: 10.1016/j.bbrc.2008.07.133

Cuddihy, S. L., Brown, K. K., Thomson, S. J., & Hampton, M. B. (2008). Induction of apoptosis by phenethyl isothiocyanate in cells overexpressing Bcl-XL. Cancer Letters, 271(2), 215-221. doi: 10.1016/j.canlet.2008.06.002

Piuhola, J., Kerkelä, R., Keenan, J. I., Hampton, M. B., Richards, A. M., & Pemberton, C. J. (2008). Direct cardiac actions of erythropoietin (EPO): Effects on cardiac contractility, BNP secretion and ischaemia/reperfusion injury. Clinical Science, 114(4), 293-304. doi: 10.1042/CS20070229

Kettle, A. J., Anderson, R. F., Hampton, M. B., & Winterbourn, C. C. (2007). Reactions of superoxide with myeloperoxidase. Biochemistry, 46, 4888-4897.

Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007). The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents. Journal of Biological Chemistry, 282(16), 11885-11892.

Low, F. M., Hampton, M. B., Peskin, A. V., & Winterbourn, C. C. (2007). Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood, 109(6), 2611-2617.

Cox, A. G., & Hampton, M. B. (2007). Bcl-2 over-expression promotes genomic instability by inhibiting apoptosis of cells exposed to hydrogen peroxide. Carcinogenesis, 28(10), 2166-2171.

Wilkie, R. P., Vissers, M. C. M., Dragunow, M., & Hampton, M. B. (2007). A functional NADPH oxidase prevents caspase involvement in the clearance of phagocytic neutrophils. Infection & Immunity, 75(7), 3256-3263.

Thomson, S. J., Brown, K. K., Pullar, J. M., & Hampton, M. B. (2006). Phenethyl isothiocyanate triggers apoptosis in Jurkat cells made resistant by the overexpression of Bcl-2. Cancer Research, 66(13), 6772-6777.

Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006). Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing. Journal of Biological Chemistry, 281(52), 39860-39869.

Cheah, F. C., Hampton, M. B., Darlow, B. A., Winterbourn, C. C., & Vissers, M. C. M. (2005). Detection of apoptosis by caspase-3 activation in tracheal aspirate neurophils from premature infants: Relationship with NF-KB activation. Journal of Leukocyte Biology, 77, 432-437.

Keenan, J. I., Peterson, II, R. A., & Hampton, M. B. (2005). NADPH oxidase involvement in the pathology of Helicobacter pylori infection. Free Radical Biology & Medicine, 38, 1188-1196.

Baird, S. K., Reid, L., Hampton, M. B., & Gieseg, S. P. (2005). OxLDL induced cell death is inhibited by the macrophage synthesised pterin, 7,8-dihydroneopterin, in U937 cells but not THP-1 cells. Biochimica et Biophysica Acta: Molecular Cell Reserch, 1745, 361-369. doi: 10.1016/j.bbamcr.2005.07.001

Baty, J. W., Hampton, M. B., & Winterbourn, C. C. (2005). Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells. Biochemical Journal, 390(3), 785-795.

Baird, S. K., Hampton, M. B., & Gieseg, S. P. (2004). Oxidized LDL triggers phosphatidylserine exposure in human monocyte cell lines by both caspase-dependent and -independent mechanisms. FEBS Letters, 578, 169-174.

Pullar, J. M., Thomson, S. J., King, M. J., Turnbull, C. I., Midwinter, R. G., & Hampton, M. B. (2004). The chemopreventive agent phenethyl isothiocyanate sensitizes cells to Fas-mediated apoptosis. Carcinogenesis, 25(5), 765-772.

Ismail, S., Hampton, M. B., & Keenan, J. I. (2003). Helicobacter pylori outer membrane vesicles modulate proliferation and interleukin-8 production by gastric epithelial cells. Infection & Immunity, 71(10), 5670-5675.

Pullar, J. M., & Hampton, M. B. (2002). Diphenyleneiodonium triggers the efflux of glutathione from cultured cells. Journal of Biological Chemistry, 277(22), 19402-19407.

Chapman, A. L. P., Hampton, M. B., Senthilmohan, R., Winterbourn, C. C., & Kettle, A. J. (2002). Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. Journal of Biological Chemistry, 277(12), 9757-9762.

Hampton, M. B., Vissers, M. C., Keenan, J. I., & Winterbourn, C. C. (2002). Oxidant-mediated phosphatidylserine exposure and macrophage uptake of activated neutrophils: possible impairment in chronic granulomatous disease. Journal of Leukocyte Biology, 71(5), 775-781.

Hampton, M. B., Morgan, P., & Davies, M. (2002). Inactivation of cellular caspases by peptide-derived tryptophan and tyrosine peroxides. FEBS Letters, 527, 289-292.

Hampton, M. B., & Winterbourn, C. C. (2002). Redox regulation of neutrophil function. Antioxidants & Redox Signaling, 4(1), 1-3.

Hampton, M. B., Stamenkovic, G., & Winterbourn, C. C. (2002). Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide. FEBS Letters, 517, 229-232.

Baty, J. W., Hampton, M. B., & Winterbourn, C. C. (2002). Detection of oxidant-sensitive thiol proteins by fluorescent labeling and two dimensional electrophoresis. Proteomics, 2, 1261-1266.

Vissers, M. C. M., Lee, W. G., & Hampton, M. B. (2001). Regulation of apoptosis by vitamin C. Specific protection of the apoptotic machinery against exposure to chlorinated oxidants. Journal of Biological Chemistry, 276(50), 46835-46840. doi: 10.1074/jbc.M107664200

Vissers, M. C. M., Pullar, J. M., & Hampton, M. B. (1999). Hypochlorous acid causes caspase activation and apoptosis or growth arrest in human endothelial cells. Biochemical Journal, 344, 443-449.

Stridh, H., Orrenius, S., & Hampton, M. B. (1999). Caspase involvement in the induction of apoptosis by the environmental toxicants tributylin and triphenyltin. Toxicology & Applied Pharmacology, 156, 141-146.

Hampton, M. B., & Winterbourn, C. C. (1999). Methods for quantifying phagocytosis and bacterial killing by human neutrophils. Journal of Immunological Methods, 232, 15-22.

Hampton, M. B., & Orrenius, S. (1998). Redox regulation of apoptotic cell death. BioFactors, 8, 1-5.

Vollebregt, M., Hampton, M. B., & Winterbourn, C. C. (1998). Activation of NF-KB in human neutrophils during phagocytosis of bacteria independently of oxidant generation. FEBS Letters, 432, 40-44.

Hampton, M. B., Fadeel, B., & Orrenius, S. (1998). Redox regulation of the caspases during apoptosis. Annals of the New York Academy of Sciences, 854, 328-335.

Stridh, H., Kimland, M., Jones, D. P., Orrenius, S., & Hampton, M. B. (1998). Cytochrome c release a cascade activation in hydrogen peroxide and tributyltin induced apoptosis. FEBS Letters, 429, 351-355.

Hampton, M. B., & Orrenius, S. (1998). Redox regulation of apoptotic cell death in the immune system. Toxicology Letters, 102-103, 355-358.

Fadeel, B., Ahlin, A., Henter, J., Orrenius, S., & Hampton, M. B. (1998). Involvement of caspases in neutrophil apoptosis: Evidence for a regulatory role of reactive oxygen species. Blood, 92, 4808-4818.

Hampton, M. B., Zhivotovsky, B., Burgess, D. H., Slater, A. F. G., & Orrenius, S. (1998). Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochemical Journal, 329, 95-99.

Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998). Inside the neutrophil phagosome: oxidants, myeloperoxidase and bacterial killing. Blood, 92, 3007-3017.

Hampton, M. B., & Orrenius, S. (1997). Dual regulation of caspase activity by hydrogen peroxide: Implications for apoptosis. FEBS Letters, 414, 552-556.

Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1996). Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Straphuylococcus aureus by neutrophils. Infection & Immunity, 64(9), 3512-3517.

^ Top of page

Journal - Research Other

Fischer, J., Eglinton, T. W., Frizelle, F. A., & Hampton, M. B. (2018). Peroxiredoxins in colorectal cancer: Predictive biomarkers of radiation response and therapeutic targets to increase radiation sensitivity? Antioxidants, 7(10), 136. doi: 10.3390/antiox7100136

Winterbourn, C. C., Kettle, A. J., & Hampton, M. B. (2016). Reactive oxygen species and neutrophil function. Annual Review of Biochemistry, 85, 765-792. doi: 10.1146/annurev-biochem-060815-014442

More publications...