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Martina Paumann-PageResearch Fellow

MSc PhD (Vienna)

Email martina.paumann-page@otago.ac.nz
Tel 64 3 364 0566

Research interests

Dr Martina Paumann-Page graduated from the University of Natural Resources and Applied Life Sciences (BOKU), Vienna, Austria, with a Master of Science in Biotechnology and Food Science, followed by a PhD in Biochemistry at the University of Vienna, Austria. As recipient of an Erwin Schrödinger Fellowship from the FWF Austrian Science Fund for research abroad, she joined the Centre for Free Radical Research as a postdoctoral research fellow in 2009. After a postdoctoral position in Vienna from 2013-2016 she permanently joined the Centre for Free Radical Research in 2017.

In 2017, Dr Paumann-Page was the recipient of the Freemasons Carrell-Espiner Research Fellowship and a CMRF Canterbury Medical Research Foundation Major Project Grant. Since 2019 she has been an associate investigator on a Mardsen grant. Since 2017 she has co-supervised one PhD student, one honours student and two summer students.

Dr Paumann-Page’s main research interest is how the reactions of mammalian peroxidases are involved in health and disease. Currently she investigates a newly identified extracellular peroxidase called peroxidasin, which was shown to be upregulated in invasive metastatic melanoma and other cancers. The mechanism by which peroxidasin contributes to tumour cell invasion is unknown, but most likely connected to its enzymatic activity. Peroxidasin generates hypobromous acid, a strong oxidant similar to chlorine bleach, which reacts with a multitude of biological molecules and modifies intra- and extracellular components. Dr Paumann-Page is investigating well-characterized cell lines from the New Zealand melanoma cell panel to characterize peroxidasin expression levels, activity, cellular location and the effect of modulation of peroxidasin protein levels and activity on cell invasiveness.

Her expertise lies in protein biochemistry (including cloning, expression and characterization of proteins) and enzymology with a particular focus on structure, function and reactivity of mammalian peroxidases and their reaction products.

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Publications

Sevcnikar, B., Paumann-Page, M., Hofbauer, S., Pfanzagl, V., Furtmüller, P. G., & Obinger, C. (2020). Reaction of human peroxidasin 1 compound I and compound II with one-electron donors. Archives of Biochemistry & Biophysics, 681, 108267. doi: 10.1016/j.abb.2020.108267

Sevcnikar, B., Schaffner, I., Chaung, C. Y., Gamon, L., Paumann-Page, M., Hofbauer, S., … Obinger, C. (2020). The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. Archives of Biochemistry & Biophysics. Advance online publication. doi: 10.1016/j.abb.2020.108443

Bathish, B., Paumann-Page, M., Paton, L. N., Kettle, A. J., & Winterbourn, C. C. (2020). Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix. Journal of Biological Chemistry. Advance online publication. doi: 10.1074/jbc.RA120.014504

Bathish, B., Turner, R., Paumann-Page, M., Kettle, A. J., & Winterbourn, C. C. (2018). Characterisation of peroxidasin activity in isolated extracellular matrix and direct detection of hypobromous acid formation. Archives of Biochemistry & Biophysics, 646, 120-127. doi: 10.1016/j.abb.2018.03.038

Paumann-Page, M., Bathish, B., Eccles, M., & Winterbourn, C. (2018). Peroxidasin, a newly identified peroxidase, and its role in invasive metastatic melanoma. Proceedings of the New Zealand Society for Oncology (NZSO) Conference. Retrieved from http://www.nzsoncology.org.nz/

Journal - Research Article

Sevcnikar, B., Paumann-Page, M., Hofbauer, S., Pfanzagl, V., Furtmüller, P. G., & Obinger, C. (2020). Reaction of human peroxidasin 1 compound I and compound II with one-electron donors. Archives of Biochemistry & Biophysics, 681, 108267. doi: 10.1016/j.abb.2020.108267

Bathish, B., Paumann-Page, M., Paton, L. N., Kettle, A. J., & Winterbourn, C. C. (2020). Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix. Journal of Biological Chemistry. Advance online publication. doi: 10.1074/jbc.RA120.014504

Sevcnikar, B., Schaffner, I., Chaung, C. Y., Gamon, L., Paumann-Page, M., Hofbauer, S., … Obinger, C. (2020). The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. Archives of Biochemistry & Biophysics. Advance online publication. doi: 10.1016/j.abb.2020.108443

Bathish, B., Turner, R., Paumann-Page, M., Kettle, A. J., & Winterbourn, C. C. (2018). Characterisation of peroxidasin activity in isolated extracellular matrix and direct detection of hypobromous acid formation. Archives of Biochemistry & Biophysics, 646, 120-127. doi: 10.1016/j.abb.2018.03.038

Grishkovskaya, I., Paumann-Page, M., Tscheliessnig, R., Stampler, J., Hofbauer, S., Soudi, M., … Obinger, C. (2017). Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation. Journal of Biological Chemistry, 292(20), 8244-8261. doi: 10.1074/jbc.M117.775031

Paumann-Page, M., Katz, R.-S., Bellei, M., Schwartz, I., Edenhofer, E., Sevcnikar, B., … Obinger, C. (2017). Pre-steady-state kinetics reveal the substrate specificity and mechanism of halide oxidation of truncation human peroxidasin 1. Journal of Biological Chemistry, 292(11), 4583-4592. doi: 10.1074/jbc.M117.775213

Soudi, M., Paumann-Page, M., Delporte, C., Pirker, K. F., Bellei, M., Edenhofer, E., … Obinger, C. (2015). Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase. Journal of Biological Chemistry, 290(17), 10876-10890. doi: 10.1074/jbc.M114.632273

Chapman, A. L. P., Mocatta, T. J., Shiva, S., Seidel, A., Chen, B., Khalilova, I., Paumann-Page, M. E., Jameson, G. N. L., Winterbourn, C. C., & Kettle, A. J. (2013). Ceruloplasmin is an endogenous inhibitor of myeloperoxidase. Journal of Biological Chemistry, 288(9), 6465-6477. doi: 10.1074/jbc.M112.418970

Paumann-Page, M., Furtmüller, P. G., Hofbauer, S., Paton, L. N., Obinger, C., & Kettle, A. J. (2013). Inactivation of human myeloperoxidase by hydrogen peroxide. Archives of Biochemistry & Biophysics, 539(1), 51-62. doi: 10.1016/j.abb.2013.09.004

Burner, U., Obinger, C., Paumann, M., Furtmuller, P. G., & Kettle, A. J. (1999). Transient and steady-state kinetics of the oxidation of substituted benzoic acid hydrazides by myeloperoxidase. Journal of Biological Chemistry, 274, 9494-9592. doi: 10.1074/jbc.274.14.9494

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Conference Contribution - Published proceedings: Abstract

Paumann-Page, M., Bathish, B., Eccles, M., & Winterbourn, C. (2018). Peroxidasin, a newly identified peroxidase, and its role in invasive metastatic melanoma. Proceedings of the New Zealand Society for Oncology (NZSO) Conference. Retrieved from http://www.nzsoncology.org.nz/

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