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Professor Mark Hampton

Mark Hampton

Principal Investigator, Centre for Free Radical Research

PhD (Otago)
MSc Hons (Canterbury)

Email mark.hampton@otago.ac.nz 
Tel 64 3 378 6225

Research interests

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.

Computer-generated image of a mitochondrionMitochondria 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.

In the media

Professor Mark Hampton was featured on Radio New Zealand's Our Changing World series in April 2013.

Major review articles

  1. Winterbourn C.C., Kettle A.J. and Hampton M.B. Reactive oxygen species and neutrophil function. Ann. Rev. Biochem. in press, 2016.
  2. Hampton M.B. and O’Connor K.M. Peroxiredoxins and the regulation of cell death. Mol. Cells 39:72-76, 2016.
  3. Poynton R.A. and Hampton M.B. Peroxiredoxins as biomarkers of oxidative stress. Biochim Biophys Acta 1840:906-912, 2014.
  4. Brown K.K. and Hampton M.B. Biological targets of isothiocyanates. Biochim. Biophys. Acta. 1810:888-894, 2011.
  5. Cox A.G., Winterbourn C.C. and Hampton M.B. Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 425:313-325, 2010.
  6. Winterbourn C.C. and Hampton M.B. Thiol chemistry and specificity in redox signalling. Free Rad. Biol. Med. 45:549-561, 2008.
  7. Low F.M., Hampton M.B. and Winterbourn C.C. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid. Redox Signal. 10:1621-1629, 2008.
  8. Hampton, M.B., Fadeel, B, and Orrenius S. Redox regulation of the caspases during apoptosis. Ann. N.Y. Acad. Sci. 854:328-335, 1998.
  9. Hampton, M.B. and Orrenius S. Redox regulation of apoptotic cell death. BioFactors 8:1-5, 1998.
  10. Hampton, M.B., Kettle, A.J., and Winterbourn C.C. Inside the neutrophil phagosome: oxidants, myeloperoxidase and bacterial killing. Blood 92:3007-3017, 1998.

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Publications

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

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

Hampton, M. B., & O'Connor, K. M. (2016). Peroxiredoxins and the regulation of cell death. Molecules & Cells, 39(1), 72-76. doi: 10.14348/molcells.2016.2351

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

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

Chapter in Book - Research

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). (pp. 291-306). New York: Springer. doi: 10.1007/978-1-62703-845-4_19

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

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

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.

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Journal - Research Article

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

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

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

Hampton, M. B., & O'Connor, K. M. (2016). Peroxiredoxins and the regulation of cell death. Molecules & Cells, 39(1), 72-76. doi: 10.14348/molcells.2016.2351

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

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

Winterbourn, C. C., & Hampton, M. B. (2015). Signaling via a peroxiredoxin sensor. Nature Chemical Biology, 11(1), 5-6. doi: 10.1038/nchembio.1722

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

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

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

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

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

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, 489-511. doi: 10.1016/j.freeradbiomed.2015.09.009

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

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

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 (MPO)-dependant oxidation of epicatechins. Biochemical Journal, 462(2), 303-314. doi: 10.1042/BJ20140612

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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