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Professor Christine Winterbourn

Christine Winterbourn

Principal Investigator

MSc (Auckland), PhD (Massey) CNZM, FRSNZ

Email christine.winterbourn@otago.ac.nz
Tel 64 3 364 0564

Education

Professor Christine Winterbourn is an Auckland University chemistry graduate who received her PhD in biochemistry from Massey University.

She did postdoctoral work at the University of British Columbia, Canada before returning to the Pathology Department, University of Otago, Christchurch, where she now has a personal chair.

Research interests

Professor Winterbourn has published more than 250 scientific papers. Her field of research is the biological chemistry of free radicals and other reactive oxidants and their involvement in health and disease.

Professor Winterbourn's focus is on understanding mechanisms of reactive oxidant production, the biochemistry of biological damage and the consequences for disease pathology.

Her current interests include:

  • the production of reactive oxidants by neutrophils and their involvement in microbial killing and inflammation
  • how neutrophils form extracellular traps (NETs)
  • how thiol proteins contribute to antioxidant defence and redox regulated cell signaling
  • biochemistry and cellular functions of mammalian peroxiredoxins
  • mechanisms of oxidative protein crosslinking
  • oxidant-antioxidant interactions in red blood cells

Other positions

  • Past member of the Health Research Council
  • Past member of the Marsden Fund Council
  • Editor of the Biochemical Journal
  • Editorial Board of Free Radical Biology and Medicine

Awards

  • University of Auckland Distinguished Alumni 2015
  • Royal Society of New Zealand’s Rutherford Medal - the first woman to receive the award in its 20 year history
  • NZ Association of Scientists’ Marsden Medal
  • Massey University 75th Anniversary Medal
  • Society for Free Radical Research (Australasia) Distinguished Service Award
  • University of Otago Distinguished Research Medal and Society for Free Radical Research (International) Trevor Slater Award

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Publications

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

Ronsein, G. E., Winterbourn, C. C., Di Mascio, P., & Kettle, A. J. (2014). Cross-linking methionine and amine residues with reactive halogen species. Free Radical Biology & Medicine, 70, 278-287. doi: 10.1016/j.freeradbiomed.2014.01.023

Kasperkiewicz, P., Poreba, M., Snipas, S. J., Parker, H., Winterbourn, C. C., Salvesen, G. S., & Drag, M. (2014). Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling. PNAS, 111(7), 2518-2523. doi: 10.1073/pnas.1318548111

Cheah, F.-C., Peskin, A. V., Wong, F.-L., Ithnin, A., Othman, A., & Winterbourn, C. C. (2014). Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants. FASEB Journal, 28(7), 3205-3210. doi: 10.1096/fj.14-250050

Green, J. N., Kettle, A. J., & Winterbourn, C. C. (2014). Protein chlorination in neutrophil phagosomes and correlation with bacterial killing. Free Radical Biology & Medicine, 77, 49-56. doi: 10.1016/j.freeradbiomed.2014.08.013

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). (2nd ed.) (pp. 291-306). New York, NY: Springer. doi: 10.1007/978-1-62703-845-4_19

Winterbourn, C. C. (2012). Biological chemistry of reactive oxygen species. In C. Chatgilialoglu & A. Studer (Eds.), Encyclopedia of radicals in chemistry, biology and materials. (pp. 1259-1281). Chichester, UK: Wiley. doi: 10.1002/9781119953678.rad077

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Journal - Research Article

Kasperkiewicz, P., Poreba, M., Snipas, S. J., Parker, H., Winterbourn, C. C., Salvesen, G. S., & Drag, M. (2014). Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling. PNAS, 111(7), 2518-2523. doi: 10.1073/pnas.1318548111

Cheah, F.-C., Peskin, A. V., Wong, F.-L., Ithnin, A., Othman, A., & Winterbourn, C. C. (2014). Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants. FASEB Journal, 28(7), 3205-3210. doi: 10.1096/fj.14-250050

Winterbourn, C. C. (2014). The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells. Biochimica et Biophysica Acta: General Subjects, 1840(2), 730-738. doi: 10.1016/j.bbagen.2013.05.004

Green, J. N., Kettle, A. J., & Winterbourn, C. C. (2014). Protein chlorination in neutrophil phagosomes and correlation with bacterial killing. Free Radical Biology & Medicine, 77, 49-56. doi: 10.1016/j.freeradbiomed.2014.08.013

Ronsein, G. E., Winterbourn, C. C., Di Mascio, P., & Kettle, A. J. (2014). Cross-linking methionine and amine residues with reactive halogen species. Free Radical Biology & Medicine, 70, 278-287. doi: 10.1016/j.freeradbiomed.2014.01.023

Das, A. B., Nauser, T., Koppenol, W. H., Kettle, A. J., Winterbourn, C. C., & Nagy, P. (2014). Rapid reaction of superoxide with insulin-tyrosyl radicals to generate a hydroperoxide with subsequent glutathione addition. Free Radical Biology & Medicine, 70, 86-95. doi: 10.1016/j.freeradbiomed.2014.02.006

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

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

Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2013). Myeloperoxidase: A front-line defender against phagocytosed microorganisms. Journal of Leukocyte Biology, 93(2), 185-198. doi: 10.1189/jlb.0712349

Winterbourn, C. C., & Kettle, A. J. (2013). Redox reactions and microbial killing in the neutrophil phagosome. Antioxidants & Redox Signaling, 18(6), 642-660. doi: 10.1089/ars.2012.4827

Parker, H., & Winterbourn, C. C. (2013). Reactive oxidants and myeloperoxidase and their involvement in neutrophil extracellular traps. Frontiers in Immunology, 3, 424. doi: 10.3389/fimmu.2012.00424

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

Nagy, P., Lechte, T. P., Das, A. B., & Winterbourn, C. C. (2012). Conjugation of glutathione to oxidized tyrosine residues in peptides and proteins. Journal of Biological Chemistry, 287(31), 26068-26076. doi: 10.1074/jbc.M112.371690

Parker, H., Albrett, A. M., Kettle, A. J., & Winterbourn, C. C. (2012). Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide. Journal of Leukocyte Biology, 91(3), 369-376. doi: 10.1189/jlb.0711387

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

Harwood, D. T., Darlow, B. A., Cheah, F. C., McNeill, N., Graham, P., & Winterbourn, C. C. (2011). Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: Association with bacterial infection. Pediatric Research, 69(1), 28-33. doi: 10.1203/PDR.0b013e3181ff2378

Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., … Winterbourn, C. C. (2011). Unraveling the biological roles of reactive oxygen species. Cell Metabolism, 13(4), 361-366. doi: 10.1016/j.cmet.2011.03.010

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

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

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

Winterbourn, C. C. (2008). Reconciling the chemistry and biology of reactive oxygen species. Nature Chemical Biology, 4(5), 278-286. doi: 10.1038/nchembio.85

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